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Conserved domains on  [gi|1958802101|ref|XP_038939395|]
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adhesion G protein-coupled receptor E2 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
624-886 1.56e-158

epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


:

Pssm-ID: 320555 [Multi-domain]  Cd Length: 263  Bit Score: 464.89  E-value: 1.56e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15439     1 DLALTVITYVGLIISLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd15439    81 CFAWMFLEAVHLFLTVRNLKVVNYFSSHRFKKRFMYPVGYGLPAVIVAISAAVNPQGYGTPKHCWLSMEKGFIWSFLGPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGA 863
Cdd:cd15439   161 CVIIVINLVLFCLTLWILREKLSSLNAEVSTLKNTRLLTFKAIAQLFILGCTWILGLFQVGPVATVMAYLFTITNSLQGV 240
                         250       260
                  ....*....|....*....|...
gi 1958802101 864 FIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15439   241 FIFLVHCLLNRQVREEYRRWITG 263
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
571-620 4.47e-13

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


:

Pssm-ID: 197639  Cd Length: 49  Bit Score: 64.33  E-value: 4.47e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958802101  571 ERSICVSWNTDveDGRWTPSGCETVEASETHTVCSCNRMTNLAIIMASGE 620
Cdd:smart00303   1 FNPICVFWDES--SGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPP 48
EGF_CA smart00179
Calcium-binding EGF-like domain;
112-151 3.69e-08

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.94  E-value: 3.69e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958802101  112 DVDECLTIGICPKNSNCSNSVGSYSCTCQSGFvSNGSTCE 151
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY-TDGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
152-182 2.28e-07

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 2.28e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958802101  152 DEDECVTRNACPEHATCHNTLGSYYCTCNEG 182
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPG 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
201-234 3.31e-07

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 3.31e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958802101  201 DVDECSRNStLCGPSFICINTLGSYSCSCPAGFS 234
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
251-280 1.37e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.37e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958802101  251 DIDEC--DDICPSNSSCTNTLGSYFCTCHPGF 280
Cdd:smart00179   1 DIDECasGNPCQNGGTCVNTVGSYRCECPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
298-328 4.95e-05

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.07  E-value: 4.95e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101 298 DIDECTQDPFRCGRNSSCTNVPGSYNCSCLP 328
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPD 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
12-42 6.98e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 6.98e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101  12 VNECQDTTTCPAYATCTDTTESYYCTCKQGF 42
Cdd:cd00054     2 IDECASGNPCQNGGTCVNTVGSYRCSCPPGY 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
60-88 1.65e-03

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 1.65e-03
                           10        20
                   ....*....|....*....|....*....
gi 1958802101   60 DVNECLrSDSPCGSNSVCTNIPGRARCSC 88
Cdd:smart00179   1 DIDECA-SGNPCQNGGTCVNTVGSYRCEC 28
 
Name Accession Description Interval E-value
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
624-886 1.56e-158

epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320555 [Multi-domain]  Cd Length: 263  Bit Score: 464.89  E-value: 1.56e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15439     1 DLALTVITYVGLIISLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd15439    81 CFAWMFLEAVHLFLTVRNLKVVNYFSSHRFKKRFMYPVGYGLPAVIVAISAAVNPQGYGTPKHCWLSMEKGFIWSFLGPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGA 863
Cdd:cd15439   161 CVIIVINLVLFCLTLWILREKLSSLNAEVSTLKNTRLLTFKAIAQLFILGCTWILGLFQVGPVATVMAYLFTITNSLQGV 240
                         250       260
                  ....*....|....*....|...
gi 1958802101 864 FIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15439   241 FIFLVHCLLNRQVREEYRRWITG 263
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
625-865 1.28e-84

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 271.46  E-value: 1.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 625 FSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQT--------ACAIIAGF 696
Cdd:pfam00002   2 LSLKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKQdldhcswvGCKVVAVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 697 LHYLFLACFFWMLVEAVMLFLMVrnlkvVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFI 776
Cdd:pfam00002  82 LHYFFLANFFWMLVEGLYLYTLL-----VEVFFSERKYFWWYLLIGWGVPALVVGIWAGVDPKGYGEDDGCWLSNENGLW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 777 WSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGP---LASIMAYL 853
Cdd:pfam00002 157 WIIRGPILLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLAKSTLLLLPLLGITWVFGLFAFNPentLRVVFLYL 236
                         250
                  ....*....|..
gi 1958802101 854 FTTINSLQGAFI 865
Cdd:pfam00002 237 FLILNSFQGFFV 248
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
571-620 4.47e-13

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 64.33  E-value: 4.47e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958802101  571 ERSICVSWNTDveDGRWTPSGCETVEASETHTVCSCNRMTNLAIIMASGE 620
Cdd:smart00303   1 FNPICVFWDES--SGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPP 48
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
574-615 2.03e-11

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


Pssm-ID: 460350  Cd Length: 44  Bit Score: 59.24  E-value: 2.03e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958802101 574 ICVSWN-TDVEDGRWTPSGCETVEASETHTVCSCNRMTNLAII 615
Cdd:pfam01825   2 QCVFWDfTNSTTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
EGF_CA smart00179
Calcium-binding EGF-like domain;
112-151 3.69e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.94  E-value: 3.69e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958802101  112 DVDECLTIGICPKNSNCSNSVGSYSCTCQSGFvSNGSTCE 151
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY-TDGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
112-151 2.23e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 47.63  E-value: 2.23e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958802101 112 DVDECLTIGICPKNSNCSNSVGSYSCTCQSGFVsnGSTCE 151
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
152-182 2.28e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 2.28e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958802101  152 DEDECVTRNACPEHATCHNTLGSYYCTCNEG 182
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPG 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
201-234 3.31e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 3.31e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958802101  201 DVDECSRNStLCGPSFICINTLGSYSCSCPAGFS 234
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
201-237 3.60e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 47.25  E-value: 3.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958802101 201 DVDECSRNStLCGPSFICINTLGSYSCSCPAGFSLST 237
Cdd:cd00054     1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGYTGRN 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
152-182 5.02e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.86  E-value: 5.02e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101 152 DEDECVTRNACPEHATCHNTLGSYYCTCNEG 182
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPG 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
251-280 1.37e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.37e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958802101  251 DIDEC--DDICPSNSSCTNTLGSYFCTCHPGF 280
Cdd:smart00179   1 DIDECasGNPCQNGGTCVNTVGSYRCECPPGY 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
251-280 7.98e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 7.98e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 251 DIDECDD--ICPSNSSCTNTLGSYFCTCHPGF 280
Cdd:cd00054     1 DIDECASgnPCQNGGTCVNTVGSYRCSCPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
251-279 8.89e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 42.99  E-value: 8.89e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 251 DIDECDD---ICPSNSSCTNTLGSYFCTCHPG 279
Cdd:pfam07645   1 DVDECATgthNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
201-232 1.72e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 42.22  E-value: 1.72e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 201 DVDECSRNSTLCGPSFICINTLGSYSCSCPAG 232
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
112-142 2.28e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.84  E-value: 2.28e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 112 DVDECLTIG-ICPKNSNCSNSVGSYSCTCQSG 142
Cdd:pfam07645   1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
152-182 3.48e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.45  E-value: 3.48e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 152 DEDECVT-RNACPEHATCHNTLGSYYCTCNEG 182
Cdd:pfam07645   1 DVDECATgTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
298-328 4.95e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.07  E-value: 4.95e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101 298 DIDECTQDPFRCGRNSSCTNVPGSYNCSCLP 328
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPD 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
298-331 7.68e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 7.68e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958802101  298 DIDECTQDPfRCGRNSSCTNVPGSYNCSCLPDFR 331
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
298-331 4.90e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.39  E-value: 4.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958802101 298 DIDECTQDPfRCGRNSSCTNVPGSYNCSCLPDFR 331
Cdd:cd00054     1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
12-42 6.98e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 6.98e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101  12 VNECQDTTTCPAYATCTDTTESYYCTCKQGF 42
Cdd:cd00054     2 IDECASGNPCQNGGTCVNTVGSYRCSCPPGY 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
12-42 1.25e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.23  E-value: 1.25e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958802101   12 VNECQDTTTCPAYATCTDTTESYYCTCKQGF 42
Cdd:smart00179   2 IDECASGNPCQNGGTCVNTVGSYRCECPPGY 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
60-88 1.65e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 1.65e-03
                           10        20
                   ....*....|....*....|....*....
gi 1958802101   60 DVNECLrSDSPCGSNSVCTNIPGRARCSC 88
Cdd:smart00179   1 DIDECA-SGNPCQNGGTCVNTVGSYRCEC 28
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
60-88 4.19e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.69  E-value: 4.19e-03
                          10        20
                  ....*....|....*....|....*....
gi 1958802101  60 DVNECLrSDSPCGSNSVCTNIPGRARCSC 88
Cdd:cd00054     1 DIDECA-SGNPCQNGGTCVNTVGSYRCSC 28
 
Name Accession Description Interval E-value
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
624-886 1.56e-158

epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320555 [Multi-domain]  Cd Length: 263  Bit Score: 464.89  E-value: 1.56e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15439     1 DLALTVITYVGLIISLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd15439    81 CFAWMFLEAVHLFLTVRNLKVVNYFSSHRFKKRFMYPVGYGLPAVIVAISAAVNPQGYGTPKHCWLSMEKGFIWSFLGPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGA 863
Cdd:cd15439   161 CVIIVINLVLFCLTLWILREKLSSLNAEVSTLKNTRLLTFKAIAQLFILGCTWILGLFQVGPVATVMAYLFTITNSLQGV 240
                         250       260
                  ....*....|....*....|...
gi 1958802101 864 FIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15439   241 FIFLVHCLLNRQVREEYRRWITG 263
7tmB2_EMR_Adhesion_II cd15931
EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of ...
624-885 7.30e-134

EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. On the other hand, EMR2 generates four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320597 [Multi-domain]  Cd Length: 262  Bit Score: 401.12  E-value: 7.30e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15931     1 DPFLEWINRVGVIVSLFCLGLAIFTFLLCRWIPKINTTAHLHLCLCLSMSHTLFLAGIEYVENELACTVMAGLLHYLFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd15931    81 SFVWMLLEALQLHLLVRRLTKVQVIQRDGLPRPLLCLIGYGVPFLIVGVSALVYSDGYGEAKMCWLSQERGFNWSFLGPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGA 863
Cdd:cd15931   161 IAIIGINWILFCATLWCLRQTLSNMNSDISQLKDTRLLTFKAVAQLFILGCTWVLGLFQTNPVALVFQYLFTILNSLQGA 240
                         250       260
                  ....*....|....*....|..
gi 1958802101 864 FIFLIHCLLNRQVRDEYRKLLT 885
Cdd:cd15931   241 FLFLVHCLLNKEVREEYIKWLT 262
7tmB2_CD97 cd15438
CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
625-886 2.87e-96

CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320554 [Multi-domain]  Cd Length: 261  Bit Score: 302.84  E-value: 2.87e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 625 FSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLAC 704
Cdd:cd15438     2 WPLTLITKVGLSVSLFCLFLCILTFLFCRSIRGTRNTIHLHLCLSLFLAHLIFLLGINNTNNQVACAVVAGLLHYFFLAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 705 FFWMLVEAVMLFLMVrnlkvVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVC 784
Cdd:cd15438    82 FCWMSLEGVELYLMV-----VQVFNTQSLKKRYLLLIGYGVPLVIVAISAAVNSKGYGTQRHCWLSLERGFLWSFLGPVC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 785 MIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAF 864
Cdd:cd15438   157 LIILVNAIIFVITVWKLAEKFSSINPDMEKLRKIRALTITAIAQLCILGCTWIFGFFQFSDSTLVMSYLFTILNSLQGLF 236
                         250       260
                  ....*....|....*....|..
gi 1958802101 865 IFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15438   237 IFLLHCLLSKQVREEYSRWLCA 258
7tmB2_latrophilin-like_invertebrate cd15440
invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane ...
624-884 8.44e-85

invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; This subgroup includes latrophilin-like proteins that are found in invertebrates such as insects and worms. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of vertebrate latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320556 [Multi-domain]  Cd Length: 259  Bit Score: 272.60  E-value: 8.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15440     1 QSALTFITYIGCIISIVCLLLAFITFTCFRNLQCDRNTIHKNLCLCLLIAEIVFLLGIDQTENRTLCGVIAGLLHYFFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMvrnlkVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd15440    81 AFSWMLLEGFQLYVM-----LVEVFEPEKSRIKWYYLFGYGLPALIVAVSAGVDPTGYGTEDHCWLSTENGFIWSFVGPV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWVL--RQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQ 861
Cdd:cd15440   156 IVVLLANLVFLGMAIYVMcrHSSRSASKKDASKLKNIRGWLKGSIVLVVLLGLTWTFGLLFINQESIVMAYIFTILNSLQ 235
                         250       260
                  ....*....|....*....|...
gi 1958802101 862 GAFIFLIHCLLNRQVRDEYRKLL 884
Cdd:cd15440   236 GLFIFIFHCVLNEKVRKELRRWL 258
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
625-865 1.28e-84

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 271.46  E-value: 1.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 625 FSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQT--------ACAIIAGF 696
Cdd:pfam00002   2 LSLKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKQdldhcswvGCKVVAVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 697 LHYLFLACFFWMLVEAVMLFLMVrnlkvVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFI 776
Cdd:pfam00002  82 LHYFFLANFFWMLVEGLYLYTLL-----VEVFFSERKYFWWYLLIGWGVPALVVGIWAGVDPKGYGEDDGCWLSNENGLW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 777 WSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGP---LASIMAYL 853
Cdd:pfam00002 157 WIIRGPILLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLAKSTLLLLPLLGITWVFGLFAFNPentLRVVFLYL 236
                         250
                  ....*....|..
gi 1958802101 854 FTTINSLQGAFI 865
Cdd:pfam00002 237 FLILNSFQGFFV 248
7tmB2_Latrophilin_Adhesion_I cd15252
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of ...
627-884 7.59e-76

Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; Group I adhesion GPCRs consist of latrophilins (also called lectomedins or latrotoxin receptors) and ETL (EGF-TM7-latrophilin-related protein. These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320380 [Multi-domain]  Cd Length: 257  Bit Score: 248.57  E-value: 7.59e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFF 706
Cdd:cd15252     4 LTRITQVGIIISLVCLAICIFTFWFFRGLQSDRTTIHKNLCISLFLAELVFLIGINTTTNKIFCSVIAGLLHYFFLAAFA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 707 WMLVEAVMLFLMVrnlkvVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVCMI 786
Cdd:cd15252    84 WMFIEGIQLYLML-----VEVFENEGSRHKNFYIFGYGSPAVIVGVSAALGYRYYGTTKVCWLSTENYFIWSFIGPATLI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 787 ITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAFIF 866
Cdd:cd15252   159 ILLNLIFLGVAIYKMFRHTAGLKPEVSCLENIRSWARGAIALLFLLGLTWIFGVLHINHASVVMAYLFTVSNSLQGMFIF 238
                         250
                  ....*....|....*...
gi 1958802101 867 LIHCLLNRQVRDEYRKLL 884
Cdd:cd15252   239 LFHCVLSRKVRKEYYKLF 256
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
624-880 4.04e-75

adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320168 [Multi-domain]  Cd Length: 253  Bit Score: 246.33  E-value: 4.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHN-TYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFL 702
Cdd:cd15040     1 EKALSIITYIGCGLSLLGLLLTIITYILFRKLRKRKpTKILLNLCLALLLANLLFLFGINSTDNPVLCTAVAALLHYFLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 703 ACFFWMLVEAVMLFLMvrnLKVVNYFSSRNIkMLHLCAFGYGLPVVVVIISATVHPWGYGMH-NRCWLNTETGFIWSFLG 781
Cdd:cd15040    81 ASFMWMLVEALLLYLR---LVKVFGTYPRHF-ILKYALIGWGLPLIIVIITLAVDPDSYGNSsGYCWLSNGNGLYYAFLG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 782 PVCMIITINSALLAWTLWVLRQKlcSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQ 861
Cdd:cd15040   157 PVLLIILVNLVIFVLVLRKLLRL--SAKRNKKKRKKTKAQLRAAVSLFFLLGLTWIFGILAIFGARVVFQYLFAIFNSLQ 234
                         250
                  ....*....|....*....
gi 1958802101 862 GAFIFLIHCLLNRQVRDEY 880
Cdd:cd15040   235 GFFIFIFHCLRNKEVRKAW 253
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
624-880 2.44e-70

class B family of seven-transmembrane G protein-coupled receptors; The class B of seven-transmembrane GPCRs is classified into three major subfamilies: subfamily B1 (secretin-like receptor family), B2 (adhesion family), and B3 (Methuselah-like family). The class B receptors have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi or prokaryotes. The B1 subfamily comprises receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the subfamily B1 receptors preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The subfamily B2 consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Furthermore, the subfamily B3 includes Methuselah (Mth) protein, which was originally identified in Drosophila as a GPCR affecting stress resistance and aging, and its closely related proteins.


Pssm-ID: 410627 [Multi-domain]  Cd Length: 260  Bit Score: 233.64  E-value: 2.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQ--TACAIIAGFLHYLF 701
Cdd:cd13952     1 DLALSIITYIGCSLSLVGLLLTIITYLLFPKLRNLRGKILINLCLSLLLAQLLFLIGQLLTSSDrpVLCKALAILLHYFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 702 LACFFWMLVEAVMLFLMVrnlkVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMH-----NRCWLNTETGFI 776
Cdd:cd13952    81 LASFFWMLVEAFDLYRTF----VKVFGSSERRRFLKYSLYGWGLPLLIVIITAIVDFSLYGPSpgyggEYCWLSNGNALL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 777 WSFLGPVCMIITINSALLAWTLWVLRQKLcsVNSEVSKLKDTRLLTFKA-IAQIFILGCSWVLGIFQI-GPLASIMAYLF 854
Cdd:cd13952   157 WAFYGPVLLILLVNLVFFILTVRILLRKL--RETPKQSERKSDRKQLRAyLKLFPLMGLTWIFGILAPfVGGSLVFWYLF 234
                         250       260
                  ....*....|....*....|....*.
gi 1958802101 855 TTINSLQGAFIFLIHCLLNRQVRDEY 880
Cdd:cd13952   235 DILNSLQGFFIFLIFCLKNKEVRRLL 260
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
627-880 1.89e-69

orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group V adhesion GPCRs include orphan receptors GPR133, GPR144, and closely related proteins. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the G(s) protein, leading to activation of adenylate cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320599 [Multi-domain]  Cd Length: 252  Bit Score: 230.68  E-value: 1.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFF 706
Cdd:cd15933     4 LSIISYIGCGISIACLALTLIIFLVLRVLSSDRFQIHKNLCVALLLAQILLLAGEWAEGNKVACKVVAILLHFFFMAAFS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 707 WMLVEAVMLFLMVrnLKVVNYfssrNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVCMI 786
Cdd:cd15933    84 WMLVEGLHLYLMI--VKVFNY----KSKMRYYYFIGWGLPAIIVAISLAILFDDYGSPNVCWLSLDDGLIWAFVGPVIFI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 787 ITINSALLAWTLWVlRQKLCSVNSEVSKLKDTRL-LTFKAIAQIF-ILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAF 864
Cdd:cd15933   158 ITVNTVILILVVKI-TVSLSTNDAKKSQGTLAQIkSTAKASVVLLpILGLTWLFGVLVVNSQTIVFQYIFVILNSLQGLM 236
                         250
                  ....*....|....*.
gi 1958802101 865 IFLIHCLLNRQVRDEY 880
Cdd:cd15933   237 IFLFHCVLNSEVRSAF 252
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
624-884 5.63e-69

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320673 [Multi-domain]  Cd Length: 258  Bit Score: 229.81  E-value: 5.63e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd16007     1 ELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVrnLKVVNYFSSRNiKMLHLCafGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd16007    81 AFSWLCLEGVQLYLML--VEVFESEYSRK-KYYYLC--GYCFPALVVGISAAIDYRSYGTEKACWLRVDNYFIWSFIGPV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGA 863
Cdd:cd16007   156 SFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAITLLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGM 235
                         250       260
                  ....*....|....*....|.
gi 1958802101 864 FIFLIHCLLNRQVRDEYRKLL 884
Cdd:cd16007   236 FIFIFHCALQKKVHKEYSKCL 256
7tmB2_ETL cd15437
Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; ...
630-886 1.53e-60

Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; member of the class B2 family of seven-transmembrane G protein-coupled receptors; ETL (EGF-TM7-latrophilin-related protein) belongs to Group I adhesion GPCRs, which also include latrophilins (also called lectomedins or latrotoxin receptors). All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. ETL, for instance, contains EGF-like repeats, which also present in other EGF-TM7 adhesion GPCRs, such as Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3), EGF-like module receptors (EMR1-3), CD97, and Flamingo. ETL is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320553 [Multi-domain]  Cd Length: 258  Bit Score: 206.65  E-value: 1.53e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 630 ISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWML 709
Cdd:cd15437     7 ITQLGIIISLICLSMCIFTFWFFSEIQSTRTTIHKNLCCSLFLAELIFLIGINMNANKLFCSIIAGLLHYFFLAAFAWMC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 710 VEAVMLFLMVRNLKVVNYFSSRNIKmlhlcAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVCMIITI 789
Cdd:cd15437    87 IEGIHLYLIVVGVIYNKGFLHKNFY-----IFGYGSPAVVVGISAALGYKYYGTTKVCWLSTENNFIWSFIGPACLIILV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 790 NSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAFIFLIH 869
Cdd:cd15437   162 NLLAFGVIIYKVFRHTAMLKPEVSCYENIRSCARGALALLFLLGATWIFGVLHVVYGSVVTAYLFTISNAFQGMFIFIFL 241
                         250
                  ....*....|....*..
gi 1958802101 870 CLLNRQVRDEYRKLLTR 886
Cdd:cd15437   242 CVLSRKIQEEYYRLFKN 258
7tmB2_Latrophilin cd15436
Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
624-884 3.56e-60

Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320552 [Multi-domain]  Cd Length: 258  Bit Score: 205.80  E-value: 3.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15436     1 ELLLFVITWVGIVISLVCLLICIFTFCFFRGLQTDRNTIHKNLCINLFIAELLFLIGINRTQYTIACPIFAGLLHFFFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVRNLkvvnyFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd15436    81 AFCWLCLEGVQLYLLLVEV-----FESEYSRRKYFYLCGYSFPALVVAVSAAIDYRSYGTEKACWLRVDNYFIWSFIGPV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGA 863
Cdd:cd15436   156 TFVITLNLVFLVITLHKMVSHSDLLKPDSSRLDNIKSWALGAIALLFLLGLTWSFGLMFINEESVVMAYLFTIFNAFQGV 235
                         250       260
                  ....*....|....*....|.
gi 1958802101 864 FIFLIHCLLNRQVRDEYRKLL 884
Cdd:cd15436   236 FIFIFHCALQKKVRKEYSKCL 256
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
624-882 7.22e-60

Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320672 [Multi-domain]  Cd Length: 258  Bit Score: 204.76  E-value: 7.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd16006     1 ELLLTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVrnlkvVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd16006    81 AFAWMCLEGVQLYLML-----VEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLRVDNYFIWSFIGPV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGA 863
Cdd:cd16006   156 TFIILLNLIFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGM 235
                         250
                  ....*....|....*....
gi 1958802101 864 FIFLIHCLLNRQVRDEYRK 882
Cdd:cd16006   236 FIFIFHCALQKKVRKEYSK 254
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
625-886 8.57e-58

cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuron migration and axon guidance in the CNS.


Pssm-ID: 320557 [Multi-domain]  Cd Length: 254  Bit Score: 199.01  E-value: 8.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 625 FSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLAC 704
Cdd:cd15441     2 LLLKIVTYIGIGISLVLLVIAFLVLSCLRGLQSNSNSIHKNLVACLLLAELLFLLGINQTENLFPCKLIAILLHYFYLSA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 705 FFWMLVEAVMLFLMVRNLKVVNYFssrniKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVC 784
Cdd:cd15441    82 FSWLLVESLHLYRMLTEPRDINHG-----HMRFYYLLGYGIPAIIVGLSVGLRPDGYGNPDFCWLSVNETLIWSFAGPIA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 785 MIITINSALLAWTLwvlrQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAF 864
Cdd:cd15441   157 FVIVITLIIFILAL----RASCTLKRHVLEKASVRTDLRSSFLLLPLLGATWVFGLLAVNEDSELLHYLFAGLNFLQGLF 232
                         250       260
                  ....*....|....*....|..
gi 1958802101 865 IFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15441   233 IFLFYCIFNKKVRRELKNALLR 254
7tmB2_Latrophilin-3 cd16005
Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled ...
627-884 1.77e-56

Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320671 [Multi-domain]  Cd Length: 258  Bit Score: 195.55  E-value: 1.77e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFF 706
Cdd:cd16005     4 LDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 707 WMLVEAVMLFLMVrnlkvVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVCMI 786
Cdd:cd16005    84 WMFLEGVQLYIML-----VEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 787 ITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAFIF 866
Cdd:cd16005   159 IMLNVIFLGIALYKMFHHTAILKPESGCLDNIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIF 238
                         250
                  ....*....|....*...
gi 1958802101 867 LIHCLLNRQVRDEYRKLL 884
Cdd:cd16005   239 IFHCVLQKKVRKEYGKCL 256
7tmB2_GPR133 cd15256
orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G ...
624-881 2.70e-49

orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR133 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR144. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320384 [Multi-domain]  Cd Length: 260  Bit Score: 175.11  E-value: 2.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAV---QNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYL 700
Cdd:cd15256     1 QVALSSITYVGCSLSIFCLAITLVTFAVLSSVstiRNQRYHIHANLSFAVLVAQILLLISFRFEPGTLPCKIMAILLHFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 701 FLACFFWMLVEAVMLFLMVrnlkvVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFL 780
Cdd:cd15256    81 FLSAFAWMLVEGLHLYSMV-----IKVFGSEESKHFYYYGIGWGSPLLICIISLTSALDSYGESDNCWLSLENGAIWAFV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 781 GPVCMIITINSALLAWTLWVLRQkLCSVNSEVSKLKDTRLLTFKAIAQIF-ILGCSWVLGIFQIGPLASIMAYLFTTINS 859
Cdd:cd15256   156 APALFVIVVNIGILIAVTRVISR-ISADNYKVHGDANAFKLTAKAVAVLLpILGSSWVFGVLAVNTHALVFQYMFAIFNS 234
                         250       260
                  ....*....|....*....|..
gi 1958802101 860 LQGAFIFLIHCLLNRQVRDEYR 881
Cdd:cd15256   235 LQGFFIFLFHCLLNSEVRAAFK 256
7tmB3_Methuselah-like cd15039
Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G ...
627-882 6.28e-46

Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G protein-coupled receptors; The subfamily B3 of class B GPCRs consists of Methuselah (Mth) and its closely related proteins found in bilateria. Mth was originally identified in Drosophila as a GPCR affecting stress resistance and aging. In addition to the seven transmembrane helices, Mth contains an N-terminal extracellular domain involved in ligand binding, and a third intracellular loop (IC3) required for the specificity of G-protein coupling. Drosophila Mth mutants showed an increase in average lifespan by 35% and greater resistance to a variety of stress factors, including starvation, high temperature, and paraquat-induced oxidative toxicity. Moreover, mutations in two endogenous peptide ligands of Methuselah, Stunted A and B, showed an increased in lifespan and resistance to oxidative stress induced by dietary paraquat. These results strongly suggest that the Stunted-Methuselah system plays important roles in stress response and aging.


Pssm-ID: 410632 [Multi-domain]  Cd Length: 270  Bit Score: 165.86  E-value: 6.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNhntyLH----LHLCVCLFLAKILFLTGIDKTDN-QTACAIIAGFLHYLF 701
Cdd:cd15039     4 LGILTLIGLIISLVFLLLTLAVYALLPELRN----LHgkclMCLVLSLFVAYLLLLIGQLLSSGdSTLCVALGILLHFFF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 702 LACFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATV------HPW--GYGmHNRCWLNTET 773
Cdd:cd15039    80 LAAFFWLNVMSFDIWRTFRGKRSSSSRSKERKRFLRYSLYAWGVPLLLVAVTIIVdfspntDSLrpGYG-EGSCWISNPW 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 774 GFIWSFLGPVCMIITINSALLAWTLWVLRqKLCSVNSEVSKLKDTRLLTFKAIAQIFIL-GCSWVLGIFQ-IGPLASIMA 851
Cdd:cd15039   159 ALLLYFYGPVALLLLFNIILFILTAIRIR-KVKKETAKVQSRLRSDKQRFRLYLKLFVImGVTWILEIISwFVGGSSVLW 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958802101 852 YLFTTINSLQGAFIFLIhCLLNRQVRDEYRK 882
Cdd:cd15039   238 YIFDILNGLQGVFIFLI-FVCKRRVLRLLKK 267
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
627-885 1.28e-40

Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320657 [Multi-domain]  Cd Length: 254  Bit Score: 150.38  E-value: 1.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFF 706
Cdd:cd15991     4 LKIITYTTVSLSLVALLITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGINQTENPFVCTVVAILLHYFYMSTFA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 707 WMLVEAVMLFLMVRNLkvvnyfssRNIKMLHL---CAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPV 783
Cdd:cd15991    84 WMFVEGLHIYRMLTEV--------RNINTGHMrfyYVVGWGIPAIITGLAVGLDPQGYGNPDFCWLSVQDTLIWSFAGPI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 784 CMIITINSALLAWTLWV---LRQKLCSVNSEVSKLKDTRLLtfkaiaqIFILGCSWVLGIFQIGPLASIMAYLFTTINSL 860
Cdd:cd15991   156 GIVVIINTVIFVLAAKAscgRRQRYFEKSGVISMLRTAFLL-------LLLISATWLLGLMAVNSDTLSFHYLFAIFSCL 228
                         250       260
                  ....*....|....*....|....*
gi 1958802101 861 QGAFIFLIHCLLNRQVRDEYRKLLT 885
Cdd:cd15991   229 QGIFIFFFHCIFNKEVRKHLKNVLT 253
7tmB2_GPR126-like_Adhesion_VIII cd15258
orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family ...
627-881 1.79e-40

orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Group VIII adhesion GPCRs include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. GPR126, on the other hand, is required for Schwann cells, but not oligodendrocyte myelination in the peripheral nervous system. Gpr64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320386 [Multi-domain]  Cd Length: 267  Bit Score: 150.26  E-value: 1.79e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAV-QNHNTYLHLHLCVCLFLAKILFL--TGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15258     4 LTFISYVGCGISAIFLAITILTYIAFRKLrRDYPSKIHMNLCAALLLLNLAFLlsSWIASFGSDGLCIAVAVALHYFLLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVrnLKVVNYFSSRNIkmLHLCAFGYGLPVVVVIISATVHPWGYG---MHNR--------CWLNTE 772
Cdd:cd15258    84 CLTWMGLEAFHLYLLL--VKVFNTYIRRYI--LKLCLVGWGLPALLVTLVLSVRSDNYGpitIPNGegfqndsfCWIRDP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 773 TGFIWSFLGPVCMIITINSALLAWTLWvlrqKLCSVNSEVSKLKDTRLL--TFKAIAQIFILGCSWVLGIFQIGPLASIM 850
Cdd:cd15258   160 VVFYITVVGYFGLTFLFNMVMLATVLV----QICRLREKAQATPRKRALhdLLTLLGLTFLLGLTWGLAFFAWGPFNLPF 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958802101 851 AYLFTTINSLQGAFIFLIHCLLNRQVRDEYR 881
Cdd:cd15258   236 LYLFAIFNSLQGFFIFIWYCSMKENVRKQWR 266
7tmB2_GPR112 cd15997
Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane ...
624-881 1.76e-38

Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR112 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR114, and GPR126. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320663  Cd Length: 269  Bit Score: 144.42  E-value: 1.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLFRAV-QNHNTYLHLHLCVCLFLAKILFLTG--IDKTDNQTACAIIAGFLHYL 700
Cdd:cd15997     1 ERILTLITYLGCGISSIFLGITLVTYLAFEKLrRDYPSKILINLCTALLMLNLVFLLNswLSSFNNYGLCITVAAFLHYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 701 FLACFFWMLVEAV-MLFLMVR--NLKVVNYfssrnikMLHLCAFGYGLPVVVVIISATVHPWGYG----------MHNRC 767
Cdd:cd15997    81 LLASFTWMGLEAVhMYFALVKvfNIYIPNY-------ILKFCIAGWGIPAVVVALVLAINKDFYGnelssdslhpSTPFC 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 768 WLNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQklCSVNSEVSKLKDTRLLTFKAIAQI-FILGCSWVLGIFQIGPL 846
Cdd:cd15997   154 WIQDDVVFYISVVAYFCLIFLCNISMFITVLIQIRS--MKAKKPSRNWKQGFLHDLKSVASLtFLLGLTWGFAFFAWGPV 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958802101 847 ASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYR 881
Cdd:cd15997   232 RIFFLYLFSICNTLQGFFIFVFHCLMKENVRKQWR 266
7tmB2_GPR144 cd15255
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
624-884 1.46e-37

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR144 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR133. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320383 [Multi-domain]  Cd Length: 263  Bit Score: 141.91  E-value: 1.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLalaIATFLLFRAV---QNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYL 700
Cdd:cd15255     1 EATLRTLSFIGCGVSLCAL---IVTFILFLAVgvpKSERTTVHKNLIFALAAAEFLLMFSEWAKGNQVACWAVTALLHLF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 701 FLACFFWMLVEAVMLFlmvRNLKVVNYFSSRNIKMLHlcAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFL 780
Cdd:cd15255    78 FLAAFSWMLVEGLLLW---SKVVAVNMSEDRRMKFYY--VTGWGLPVVIVAVTLATSFNKYVADQHCWLNVQTDIIWAFV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 781 GPVCMIITINSALLAWTLWVL------RQKLCSVNSEVSklKDTRLLTFKAIAQIFI----LGCSWVLGIfqIGPLASIM 850
Cdd:cd15255   153 GPVLFVLTVNTFVLFRVVMVTvssarrRAKMLTPSSDLE--KQIGIQIWATAKPVLVllpvLGLTWLCGV--LVHLSDVW 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958802101 851 AYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLL 884
Cdd:cd15255   229 AYVFITLNSFQGLYIFLVYAIYNSEVRNAIQRMQ 262
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
626-881 8.42e-35

Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuronal migration and axon guidance in the CNS. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320659 [Multi-domain]  Cd Length: 254  Bit Score: 133.43  E-value: 8.42e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACF 705
Cdd:cd15993     3 TLAIVTYSSVSASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLSTF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 706 FWMLVEAVMLFLMVRNLKVVNYFSsrnikMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVCM 785
Cdd:cd15993    83 AWLFVQGLHIYRMQTEARNVNFGA-----MRFYYAIGWGVPAIITGLAVGLDPEGYGNPDFCWISIHDKLVWSFAGPIVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 786 IITINSALLawtLWVLRQkLCSVNSEVSKlKDTRLLTFK-AIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAF 864
Cdd:cd15993   158 VIVMNGVMF---LLVARM-SCSPGQKETK-KTSVLMTLRsSFLLLLLISATWLFGLLAVNNSVLAFHYLHAILCCLQGLA 232
                         250
                  ....*....|....*..
gi 1958802101 865 IFLIHCLLNRQVRDEYR 881
Cdd:cd15993   233 VLLLFCVLNEEVQEAWK 249
7tmB1_hormone_R cd15041
The subfamily B1 of hormone receptors (secretin-like), member of the class B family ...
626-886 1.78e-34

The subfamily B1 of hormone receptors (secretin-like), member of the class B family seven-transmembrane G protein-coupled receptors; The B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of this subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. Moreover, the B1 subfamily receptors play key roles in hormone homeostasis and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression). Furthermore, the subfamilies B2 and B3 consist of receptors that are capable of interacting with epidermal growth factors (EGF) and the Drosophila melanogaster Methuselah gene product (Mth), respectively. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 341321 [Multi-domain]  Cd Length: 273  Bit Score: 133.12  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCV-CLFLAKILFLTGIDKTDNQT--------------AC 690
Cdd:cd15041     3 VVYYIYLVGYSLSLVALLPAIVIFLYFRSLRCTRIRLHINLFLsFILRAVFWIIWDLLVVYDRLtssgvetvlmqnpvGC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 691 AIIAGFLHYLFLACFFWMLVEAVMLFLMvrnlkVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHpwgYGMHN-RCWL 769
Cdd:cd15041    83 KLLSVLKRYFKSANYFWMLCEGLYLHRL-----IVVAFFSEPSSLKLYYAIGWGLPLVIVVIWAIVR---ALLSNeSCWI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 770 -NTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKL-CSVNSEVSKLKdtrlltfKAIAQIFIL----GCSWVLGIFQI 843
Cdd:cd15041   155 sYNNGHYEWILYGPNLLALLVNLFFLINILRILLTKLrSHPNAEPSNYR-------KAVKATLILiplfGIQYLLTIYRP 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958802101 844 GPLASI-MAYLFTT--INSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15041   228 PDGSEGeLVYEYFNaiLNSSQGFFVAVIYCFLNGEVQSELKRKWSR 273
7tmB1_DH_R cd15263
insect diuretic hormone receptors, member of the class B family of seven-transmembrane G ...
629-886 3.42e-33

insect diuretic hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors that specifically bind to insect diuretic hormones found in Manduca sexta (moth) and Acheta domesticus (the house cricket), among others. Insect diuretic hormone and their GPCRs play critical roles in the regulation of water and ion balance. Thus they are attractive targets for developing new insecticides. Activation of the diuretic hormone receptors stimulate adenylate cyclase, thereby increasing cAMP levels in Malpighian tube. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of Gs family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx.


Pssm-ID: 320391 [Multi-domain]  Cd Length: 272  Bit Score: 129.41  E-value: 3.42e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 629 IISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILF-LTGI---DKTDNQTACAIIAGFLHYLFLAC 704
Cdd:cd15263     6 TIYFIGYSLSLVALSLALWIFLYFKDLRCLRNTIHTNLMFTYILADLTWiLTLTlqvSIGEDQKSCIILVVLLHYFHLTN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 705 FFWMLVEAVMLFLMvrnlkVVNYFSSRNIKmLHLCAF-GYGLPVVVVIISATV------------HPWGYGMHnrC-WLN 770
Cdd:cd15263    86 FFWMFVEGLYLYML-----VVETFSGENIK-LRVYAFiGWGIPAVVIVIWAIVkalaptapntalDPNGLLKH--CpWMA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 771 tETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSK--LKDTRLLtfkaIAQIFILGCSWVLGIFqiGPLAS 848
Cdd:cd15263   158 -EHIVDWIFQGPAILVLAVNLVFLVRIMWVLITKLRSANTVETQqyRKAAKAL----LVLIPLLGITYILVIA--GPTEG 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958802101 849 IMAYLFTTIN----SLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15263   231 IAANIFEYVRavllSTQGFTVALFYCFLNTEVRNTLRHHFER 272
7tmB2_GPR64 cd15444
orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B ...
627-884 3.64e-33

orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B secretin-like receptors of seven-transmembrane G protein-coupled receptors; GPR64 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR97, GPR112, GPR114, and GPR126. GPR64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320560 [Multi-domain]  Cd Length: 271  Bit Score: 129.18  E-value: 3.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAV-QNHNTYLHLHLCVCLFLAKILFLtgIDK-----TDNQTACAIIAGFLHYL 700
Cdd:cd15444     4 LTFITYIGCGLSAIFLSVTLVTYIAFEKIrRDYPSKILIQLCVALLLLNLVFL--LDSwialyKDIVGLCISVAVFLHYF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 701 FLACFFWMLVEAVMLFLMVrnLKVVNYFSSRNIkmLHLCAFGYGLPVVVVIISATVHPWGYGMHNR-----------CWL 769
Cdd:cd15444    82 LLVSFTWMGLEAFHMYLAL--VKVFNTYIRKYI--LKFCIVGWGVPAVVVAIVLAVSKDNYGLGSYgkspngstddfCWI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 770 NTETGFIWSFLGPVCMIITINSALLAwtlwVLRQKLCSVNSE--VSKLKDTRLLTFKAIAQI-FILGCSWVLGIFQIGPL 846
Cdd:cd15444   158 NNNIVFYITVVGYFCVIFLLNISMFI----VVLVQLCRIKKQkqLGAQRKTSLQDLRSVAGItFLLGITWGFAFFAWGPV 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958802101 847 ASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLL 884
Cdd:cd15444   234 NLAFMYLFAIFNTLQGFFIFIFYCVAKENVRKQWRRYL 271
7tmB2_GPR116-like_Adhesion_VI cd15932
orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of ...
627-878 7.62e-33

orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group VI adhesion GPCRs consist of orphan receptors GPR110, GPR111, GPR113, GPR115, GPR116, and closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR110 possesses a SEA box in the N-terminal has been identified as an oncogene over-expressed in lung and prostate cancer. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain. GPR112 has extremely long N-terminus (about 2,400 amino acids) containing a number of Ser/Thr-rich glycosylation sites and a pentraxin (PTX) domain. GPR116 has two C2-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320598 [Multi-domain]  Cd Length: 268  Bit Score: 128.20  E-value: 7.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLF--RAVQNHNTYLHlHLC-----VCLFLAKILFLTGI---DKTDNQTACAIIAGF 696
Cdd:cd15932     4 LDYITYVGLGISILSLVLCLIIEALVwkSVTKNKTSYMR-HVClvniaLSLLIADIWFIIGAaisTPPNPSPACTAATFF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 697 LHYLFLACFFWMLVEAVMLFLmvrNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIIS-ATVHPWG-YGMHNRCWLN-TET 773
Cdd:cd15932    83 IHFFYLALFFWMLTLGLLLFY---RLVLVFHDMSKSTMMAIAFSLGYGCPLIIAIITvAATAPQGgYTRKGVCWLNwDKT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 774 GFIWSFLGPVCMIITINSALLAWTLWVLRQKlcSVNSEVSK-LKDTRLLTFKAIAQIF-ILGCSWVLGIFQ-IGPLASIM 850
Cdd:cd15932   160 KALLAFVIPALAIVVVNFIILIVVIFKLLRP--SVGERPSKdEKNALVQIGKSVAILTpLLGLTWGFGLGTmIDPKSLAF 237
                         250       260
                  ....*....|....*....|....*...
gi 1958802101 851 AYLFTTINSLQGAFIFLIHCLLNRQVRD 878
Cdd:cd15932   238 HIIFAILNSFQGFFILVFGTLLDSKVRE 265
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
627-886 1.26e-31

Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320658  Cd Length: 255  Bit Score: 124.16  E-value: 1.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFF 706
Cdd:cd15992     4 LKTLTWSSVGVTLGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLCTFS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 707 WMLVEAVMLFLMVRNLKVVNYFSSRNIKMLhlcafGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVCMI 786
Cdd:cd15992    84 WLFLEGLHIYRMLSEVRDINYGPMRFYYLI-----GWGVPAFITGLAVGLDPEGYGNPDFCWLSIYDTLIWSFAGPVAFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 787 ITINSallawTLWVLRQKL-CSVNSEVSKLKDTRLLTFK-AIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAF 864
Cdd:cd15992   159 VSMNV-----FLYILSSRAsCSAQQQSFEKKKGPVSGLRtAFTVLLLVSVTCLLALLSVNSDVILFHYLFAGFNCLQGPF 233
                         250       260
                  ....*....|....*....|..
gi 1958802101 865 IFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15992   234 IFLSHVVLLKEVRKALKTLCGP 255
7tmB1_CRF-R cd15264
corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane ...
629-882 3.30e-29

corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320392 [Multi-domain]  Cd Length: 265  Bit Score: 117.52  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 629 IISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILF------LTGIDKTDNQTACAIIAGFLHYLFL 702
Cdd:cd15264     6 IIYYLGFSISLVALAVALIIFLYFRSLRCLRNNIHCNLIVTFILRNVTWfimqntLTEIHHQSNQWVCRLIVTVYNYFQV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 703 ACFFWMLVEAVMLFLMvrnlkVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHpwgYGMHN-RCWLNTETGFIWSFL- 780
Cdd:cd15264    86 TNFFWMFVEGLYLHTM-----IVWAYSADKIRFWYYIVIGWCIPCPFVLAWAIVK---LLYENeHCWLPKSENSYYDYIy 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 781 -GPVCMIITINSALLAWTLWVLRQKLCSVNSEvsklkDTRLL--TFKAIAQIF-ILGCSWVLgiFQIGP---LASIMAYL 853
Cdd:cd15264   158 qGPILLVLLINFIFLFNIVWVLITKLRASNTL-----ETIQYrkAVKATLVLLpLLGITYML--FFINPgddKTSRLVFI 230
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958802101 854 F--TTINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15264   231 YfnTFLQSFQGLFVAVFYCFLNGEVRSAIRK 261
7tmB2_GPR113 cd15253
orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G ...
624-886 1.17e-28

orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR113 is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR115, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain, and is primarily expressed in a subset of taste receptor cells. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320381 [Multi-domain]  Cd Length: 271  Bit Score: 116.40  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFSLYIISYVGTVISLVCLALAIATFLLF--RAVQNHNTYLH----LHLCVCLFLAKILFLTG--IDKTDNQTACAIIAG 695
Cdd:cd15253     1 SFWLDFLSQVGLGASILALLLCLGIYRLVwrSVVRNKISYFRhmtlVNIAFSLLLADTCFLGAtfLSAGHESPLCLAAAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 696 FLHYLFLACFFWMLVEAVMLFlmvRNLKVVNYFSSRNIKMLHLCAFGYGLPvvVVIISATV---HPWGYGMH-NRCWLNT 771
Cdd:cd15253    81 LCHFFYLATFFWMLVQALMLF---HQLLFVFHQLAKRSVLPLMVTLGYLCP--LLIAAATVayyYPKRQYLHeGACWLNG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 772 ETGFIWSFLGPVCMIITINSALLAWTLWVLRQKlcSVnSEVSKLKDTRLL--TFKAIAQIF-ILGCSWVLGIFQIGPLAS 848
Cdd:cd15253   156 ESGAIYAFSIPVLAIVLVNLLVLFVVLMKLMRP--SV-SEGPPPEERKALlsIFKALLVLTpVFGLTWGLGVATLTGESS 232
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958802101 849 -IMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15253   233 qVSHYGFAILNAFQGVFILLFGCLMDKKVREALLKRLCK 271
7tmB2_GPR126 cd15996
orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G ...
627-884 1.22e-27

orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR126 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, and GPR114. GPR126 is required in Schwann cells for proper differentiation and myelination via G-Protein Activation. GPR126 is believed to couple to G(s)-protein, which leads to activation of adenylate cyclase for cAMP production. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320662  Cd Length: 271  Bit Score: 113.44  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQ-NHNTYLHLHLCVCLFLAKILFLTG--IDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15996     4 LTFITYIGCGISAIFSAATLLTYIAFEKLRrDYPSKILMNLSTALLFLNLVFLLDgwIASFEIDELCITVAVLLHFFLLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVrnLKVVNYFSSRNIkmLHLCAFGYGLP--VVVVIISATVHPWGYGMHNR----------CWLNT 771
Cdd:cd15996    84 TFTWMGLEAIHMYIAL--VKVFNTYIRRYI--LKFCIIGWGLPalIVSIVLASTNDNYGYGYYGKdkdgqggdefCWIKN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 772 ETGFIWSFLGPVCMIITINSALLAwtlwVLRQKLCSVNSEVSK--LKDTRLLTFKAIAQI-FILGCSWVLGIFQIGPLAS 848
Cdd:cd15996   160 PVVFYVTCAAYFGIMFLMNVAMFI----VVMVQICGRNGKRSNrtLREEILRNLRSVVSLtFLLGMTWGFAFFAWGPVNL 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958802101 849 IMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLL 884
Cdd:cd15996   236 AFMYLFTIFNSLQGLFIFVFHCALKENVQKQWRRHL 271
7tmB2_GPR114 cd15443
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
626-879 1.50e-27

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR114 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR97, GPR112, and GPR126. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320559 [Multi-domain]  Cd Length: 268  Bit Score: 112.93  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNT-YLHLHLCVCLFLAKILFLTG--IDKTDNQTACAIIAGFLHYLFL 702
Cdd:cd15443     3 PLTYISIVGCSISAAASLLTILLHFFSRKQPKDSTtRIHMNLLGSLFLLNGSFLLSppLATSQSTWLCRAAAALLHYSLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 703 ACFFWMLVEAVMLFLMVrnLKVVNYFSSRNIkmLHLCAFGYGLPVVVVIISATVHPWGYGMH-----------NRCWLNT 771
Cdd:cd15443    83 CCLTWMAIEGFHLYLLL--VKVYNIYIRRYV--LKLCVLGWGLPALIVLLVLIFKREAYGPHtiptgtgyqnaSMCWITS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 772 ETGFIWSFLGPVCMIITINSALLAWTLWVLRQklcsVNSEVSKLKD-TRLLTFKAIAQIFILGCSWVLGIFQIGPLASIM 850
Cdd:cd15443   159 SKVHYVLVLGYAGLTSLFNLVVLAWVVRMLRR----LRSRKQELGErARRDWVTVLGLTCLLGTTWALAFFSFGVFLIPQ 234
                         250       260
                  ....*....|....*....|....*....
gi 1958802101 851 AYLFTTINSLQGAFIFLIHCLLNRQVRDE 879
Cdd:cd15443   235 LFLFTIINSLYGFFICLWYCTQRRRSDAS 263
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
636-881 3.95e-27

brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320379  Cd Length: 253  Bit Score: 111.19  E-value: 3.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 636 VISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWMLVEAVML 715
Cdd:cd15251    14 VSCLALLTLLAIYAAFWRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFLSSFCWVLTEAWQS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 716 FlmvrnLKVVNYFSSRNIKMLHLCaFGYGLPVVVVIISAT-VHPWGYGMHNRCWLNTETGFIWSFLGPVCMIITINS--A 792
Cdd:cd15251    94 Y-----MAVTGRMRTRLIRKRFLC-LGWGLPALVVAVSVGfTRTKGYGTSSYCWLSLEGGLLYAFVGPAAAVVLVNMviG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 793 LLAWTLWVLRQKLcSVNSEVSKLKDTRLLTfkaiaqifILGCSWVLGIFQIGPLASIM-AYLFTTINSLQGAFIFLIHCL 871
Cdd:cd15251   168 ILVFNKLVSRDGI-SDNAMASLWSSCVVLP--------LLALTWMSAVLAMTDRRSVLfQILFAVFDSLQGFVIVMVHCI 238
                         250
                  ....*....|
gi 1958802101 872 LNRQVRDEYR 881
Cdd:cd15251   239 LRREVQDAVK 248
7tmB2_GPR97 cd15442
orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G ...
626-867 7.69e-26

orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR97 is an orphan receptor that has been classified into the group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR112, GPR114, and GPR126. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320558 [Multi-domain]  Cd Length: 277  Bit Score: 108.35  E-value: 7.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQ-----NHNTYLHLHLCVCLFLAKILFL--TGIDKTDNQTACAIIAGFLH 698
Cdd:cd15442     3 TLVTISSAGCGVSMVFLIFTIILYFFLRFTYqkfksEDAPKIHVNLSSSLLLLNLAFLlnSGVSSRAHPGLCKALGGVTH 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 699 YLFLACFFWMLVEAVMLFLMVrnLKVVN-YFSSRnikMLHLCAFGYGLPVVVVIISATVHPWG----YGMHNR-----CW 768
Cdd:cd15442    83 YFLLCCFTWMAIEAFHLYLLA--IKVFNtYIHHY---FAKLCLVGWGFPALVVTITGSINSYGaytiMDMANRttlhlCW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 769 LNTETGFIW--SFLGPVCMIITINSALLAWTLWvlrqKLCSVNSevSKLKDTRLLTFKAIAQIF----ILGCSWVLGIFQ 842
Cdd:cd15442   158 INSKHLTVHyiTVCGYFGLTFLFNTVVLGLVAW----KIFHLQS--ATAGKEKCQAWKGGLTVLglscLLGVTWGLAFFT 231
                         250       260
                  ....*....|....*....|....*
gi 1958802101 843 IGPLASIMAYLFTTINSLQGAFIFL 867
Cdd:cd15442   232 YGSMSVPTVYIFALLNSLQGLFIFI 256
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
633-878 1.56e-24

brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320654 [Multi-domain]  Cd Length: 291  Bit Score: 104.65  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 633 VGTVISLVCLALAIATFLLF-RAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWMLVE 711
Cdd:cd15988    10 IGCAVSCMALLILLAIYAAFwRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFLSSFCWVLTE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 712 AVMLFlmvrnLKVVNYFSSRNIKMLHLCaFGYGLPVVVVIISAT-VHPWGYGMHNRCWLNTETGFIWSFLGPVCMIITIN 790
Cdd:cd15988    90 AWQSY-----LAVIGRMRTRLVRKRFLC-LGWGLPALVVAVSVGfTRTKGYGTASYCWLSLEGGLLYAFVGPAAVIVLVN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 791 ---------------------------SALLAWTLWVLRQKLCSVnseVSKLKDTRLLTFKAIAQIF-------ILGCSW 836
Cdd:cd15988   164 mligiivfnklmsrdgisdkskkqragSEAEPCSSLLLKCSKCGV---VSSAAMSSATASSAMASLWsscvvlpLLALTW 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958802101 837 VLGIFQIGPLASIM-AYLFTTINSLQGAFIFLIHCLLNRQVRD 878
Cdd:cd15988   241 MSAVLAMTDRRSILfQVLFAVFNSVQGFVIITVHCFLRREVQD 283
7tmB2_GPR128 cd15257
orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G ...
626-886 3.57e-24

orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR128 is an orphan receptor of the adhesion family (subclass B2) that belongs to the class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance, as its knockout mice showed a decrease in body weight gain and an increase in intestinal contraction frequency compared to wild-type controls. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320385 [Multi-domain]  Cd Length: 303  Bit Score: 103.80  E-value: 3.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHN-TYLHLHLCVCLFLAKILFLTGIDKTDNQTA--------------- 689
Cdd:cd15257     3 TLDIISTIGCVLSIAGLVITIIFHLHTRKLRKSSvTWVLLNLCSSLLLFNIIFTSGVENTNNDYEistvpdretntvlls 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 690 ----------CAIIAGFLHYLFLACFFWMLVEAVMLFLMVRNLkvvnYFSSRNIKMLHLCAFGYGLPVVVVII------- 752
Cdd:cd15257    83 eeyvepdtdvCTAVAALLHYFLLVTFMWNAVYSAQLYLLLIRM----MKPLPEMFILQASAIGWGIPAVVVAItlgatyr 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 753 ---SATVHPWGYGMHNRCWL-------NTETGFIWSFLGPVCMIITINSALLAWTLwvlrQKLCSVNsevSKLKDTRLLT 822
Cdd:cd15257   159 fptSLPVFTRTYRQEEFCWLaaldknfDIKKPLLWGFLLPVGLILITNVILFIMTS----QKVLKKN---NKKLTTKKRS 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958802101 823 FK-----AIAQIFILGCSWVLGIFQI---GPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15257   232 YMkkiyiTVSVAVVFGITWILGYLMLvnnDLSKLVFSYIFCITNTTQGVQIFILYTWRTPEFRKLVSKLSLK 303
7tmB2_BAI1 cd15990
brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 ...
636-889 2.04e-23

brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320656  Cd Length: 267  Bit Score: 100.84  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 636 VISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWMLVEAVML 715
Cdd:cd15990    17 VSSLTLLLLIIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 716 FlmvrnLKVVNYFSSRNIKMLHLCaFGYGLPVVVVIISAT-VHPWGYGMHNRCWLNTETGFIWSFLGPVCMIITINSALL 794
Cdd:cd15990    97 Y-----MAVTGRLRNRIIRKRFLC-LGWGLPALVVAISVGfTKAKGYGTVNYCWLSLEGGLLYAFVGPAAAVVLVNMVIG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 795 AWTLWVLRQKLCSVNSEVSKLKDTRLltFKAIAQIFILGCSWVLGIFQIGPLAS-IMAYLFTTINSLQGAFIFLIHCLLN 873
Cdd:cd15990   171 ILVFNKLVSKDGITDKKLKERAGASL--WSSCVVLPLLALTWMSAVLAITDRRSaLFQILFAVFDSLEGFVIVMVHCILR 248
                         250
                  ....*....|....*..
gi 1958802101 874 RQVRDEYR-KLLTRKTD 889
Cdd:cd15990   249 REVQDAVKcRVVDRQEE 265
7tmB2_BAI3 cd15989
brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 ...
633-881 2.96e-22

brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320655 [Multi-domain]  Cd Length: 293  Bit Score: 98.22  E-value: 2.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 633 VGTVIS-LVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWMLVE 711
Cdd:cd15989    12 VGCGLScLALITLAVVYAALWRYIRSERSIILINFCLSIISSNILILVGQTQTHNKGICTMTTAFLHFFFLASFCWVLTE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 712 AVMLFlmvrnLKVVNYFSSRNIKMLHLCaFGYGLPVVVVIISAT-VHPWGYGMHNRCWLNTETGFIWSFLGPVCMIITIN 790
Cdd:cd15989    92 AWQSY-----MAVTGKIRTRLIRKRFLC-LGWGLPALVVAISMGfTKAKGYGTPHYCWLSLEGGLLYAFVGPAAAVVLVN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 791 SAL-------LAWTLWVLRQKL-----------------CSVNSEVSKLKDTRLLTFKAIAQIF-------ILGCSWVLG 839
Cdd:cd15989   166 MVIgilvfnkLVSRDGILDKKLkhragqmsephsgltlkCAKCGVVSTTALSATTASNAMASLWsscvvlpLLALTWMSA 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958802101 840 IFQIGPLASIM-AYLFTTINSLQGAFIFLIHCLLNRQVRDEYR 881
Cdd:cd15989   246 VLAMTDKRSILfQILFAVFDSLQGFVIVMVHCILRREVQDAFR 288
7tmB2_GPR116_Ig-Hepta cd15254
The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family ...
627-878 7.89e-22

The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR116 (also known as Ig-hepta) is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR113, and GPR115. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR116 has four I-set immunoglobulin-like repeats, which is found in the members of the immunoglobulin superfamily of cell surface proteins, and a SEA (sea urchin sperm protein, enterokinase, and a grin)-box, which is present in the extracellular domain of the transmembrane mucin (MUC) family and known to enhance O-glycosylation. GPR116 is highly expressed in fetal and adult lung, and it has been shown to regulate lung surfactant levels as well as to stimulate breast cancer metastasis through a G(q)-p63-RhoGEF-Rho GTPase signaling pathway. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320382 [Multi-domain]  Cd Length: 275  Bit Score: 96.41  E-value: 7.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIAT-FLLFRAVQNHNTYLHLHLC-----VCLFLAKILFLTGIDKTD-----NQTACAIIAG 695
Cdd:cd15254     4 LDYITYIGLSISILSLAICIVIeSLVWKSVTKNRTSYMRHVCilniaVSLLIADIWFIVVAAIQDqnyavNGNVCVAATF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 696 FLHYLFLACFFWMLVEAVMLFLmvrNLKVVNYFSSRNIKMLHLCAFGYGLPVV--VVIISATVHPWGYGMHNRCWLNTE- 772
Cdd:cd15254    84 FIHFFYLCVFFWMLALGLMLFY---RLVFILHDTSKTIQKAVAFCLGYGCPLIisVITIAVTLPRDSYTRKKVCWLNWEd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 773 TGFIWSFLGPVCMIITINSALLAWTLW-VLRQklcSVNSEVSKLKDTRLltFKAIAQIFI----LGCSWVLGIFQIGPLA 847
Cdd:cd15254   161 SKALLAFVIPALIIVAVNSIITVVVIVkILRP---SIGEKPSKQERSSL--FQIIKSIGVltplLGLTWGFGLATVIKGS 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958802101 848 SIMAY-LFTTINSLQGAFIFLIHCLLNRQVRD 878
Cdd:cd15254   236 SIVFHiLFTLLNAFQGLFILVFGTLWDKKVQE 267
7tmB2_GPR124-like_Adhesion_III cd15259
orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of ...
625-881 1.52e-21

orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group III adhesion GPCRs include orphan GPR123, GPR124, GPR125, and their closely related proteins. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 also interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Furthermore, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl.


Pssm-ID: 320387 [Multi-domain]  Cd Length: 260  Bit Score: 95.13  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 625 FSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNT---YLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLF 701
Cdd:cd15259     2 ELLHPVVYAGAALCLLCLLATIITYIVFHRLIRISRkgrHMLVNLCLHLLLTCVVFVGGINRTANQLVCQAVGILLHYST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 702 LACFFWMLVEA-VMLFLMVRNLKVVNYFSSRNIK---MLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETgFIW 777
Cdd:cd15259    82 LCTLLWVGVTArNMYKQVTKTAKPPQDEDQPPRPpkpMLRFYLIGWGIPLIICGITAAVNLDNYSTYDYCWLAWDP-SLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 778 SFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLtfkaIAQIFILGCSWVLGIFqigPLASIMAYLFTTI 857
Cdd:cd15259   161 AFYGPAALIVLVNCIYFLRIYCQLKGAPVSFQSQLRGAVITLFL----YVAMWACGALAVSQRY---FLDLVFSCLYGAT 233
                         250       260
                  ....*....|....*....|....
gi 1958802101 858 NSLQGAFIFLIHCLLNRQVRDEYR 881
Cdd:cd15259   234 CSSLGLFVLIHHCLSREDVRQSWR 257
7tmB2_GPR56 cd15995
orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G ...
627-877 1.69e-21

orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR56 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320661  Cd Length: 269  Bit Score: 95.28  E-value: 1.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQ-NHNTYLHLHLCVCLFLAKILFLTG--IDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15995     4 LTILTYVGCIISALASVFTIAFYLCSRRKPrDYTIYVHMNLLLAIFLLDTSFLISepLALTGSEAACRAGGMFLHFSLLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLFLMVrnLKVVNYFSSRNIkmLHLCAFGYGLPVVVVIISATVH--------------PWGYGMHNRCWL 769
Cdd:cd15995    84 CLTWMGIEGYNLYRLV--VEVFNTYVPHFL--LKLCAVGWGLPIFLVTLIFLVDqdnygpiilavhrsPEKVTYATICWI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 770 NTETGFIWSFLGPVCMIITINSALLAWTLW-VLRQKlcsvnSEVSKLKDTRLLtfkaIAQIFILGCSWVLGIFQI--GPL 846
Cdd:cd15995   160 TDSLISNITNLGLFSLVFLFNMAMLATMVVeILRLR-----PRTHKWSHVLTL----LGLSLVLGIPWALAFFSFasGTF 230
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958802101 847 ASIMAYLFTTINSLQGAFIFLIHCLLNRQVR 877
Cdd:cd15995   231 QLVIVYLFTIINSLQGFLIFLWYWSMVLQAR 261
7tmB1_PDFR cd15261
The pigment dispersing factor receptor, member of the class B seven-transmembrane G ...
629-886 3.81e-21

The pigment dispersing factor receptor, member of the class B seven-transmembrane G protein-coupled receptors; The pigment dispersing factor receptor (PDFR) is a G protein-coupled receptor that binds the circadian clock neuropeptide PDF, a functional ortholog of the mammalian vasoactive intestinal peptide (VIP), on the pacemaker neurons. The PDFR is implicated in regulating flight circuit development and in modulating acute flight In Drosophila melanogaster. The PDFR activation stimulates adenylate cyclase, thereby increasing cAMP levels in many different pacemakers, and the receptor signaling has been shown to regulate behavioral circadian rhythms and geotaxis in Drosophila. The PDFR belongs to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. . These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. They play key roles in hormone homeostasis in mammals and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression).


Pssm-ID: 320389 [Multi-domain]  Cd Length: 282  Bit Score: 94.74  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 629 IISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLT-----------------------GIDKTD 685
Cdd:cd15261     6 TLEIVGLCLSLVSLIISLFIFSYFRTLRNHRTRIHKNLFLAILLQVIIRLVlyidqaitrsrgshtnaattegrTINSTP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 686 nqTACAIIAGFLHYLFLACFFWMLVEAVMLflmvRNLKVVNYFSSRnIKMLHLCAFGYGLPVVVVIISATVHPWGYGMhN 765
Cdd:cd15261    86 --ILCEGFYVLLEYAKTVMFMWMFIEGLYL----HNIIVVSVFSGK-PNYLFYYILGWGIPIVHTSAWAIVTLIKMKV-N 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 766 RCWLNTE-TGFIWSFLGPVCMIITINSALLAWTLWVLRQKLC-SVNSEVSKLKDTrllTFKAIAQIFILGCSWVLGIFQI 843
Cdd:cd15261   158 RCWFGYYlTPYYWILEGPRLAVILINLFFLLNIIRVLVSKLReSHSREIEQVRKA---VKAAIVLLPLLGITNILQMIPP 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958802101 844 GPLASIM--------AYLFTtinSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15261   235 PLTSVIVgfavwsysTHFLT---SFQGFFVALIYCFLNGEVKNVLKKFWRR 282
7tmB1_GlucagonR-like cd15929
glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G ...
626-886 6.60e-18

glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents the glucagon receptor family of G protein-coupled receptors, which includes glucagon receptor (GCGR), glucagon-like peptide-1 receptor (GLP1R), GLP2R, and closely related receptors. These receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 341353 [Multi-domain]  Cd Length: 279  Bit Score: 84.79  E-value: 6.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHL-------CVCLFLAKILFLTGIDKTDNQ----------- 687
Cdd:cd15929     3 SLQVMYTVGYSLSLAALVLALAILLGLRKLHCTRNYIHANLfasfilrALSVLVKDALLPRRYSQKGDQdlwstllsnqa 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 688 -TACAIIAGFLHYLFLACFFWMLVEAVMLFlmvrNLKVVNYFSSRNIKMLHLcAFGYGLPVVVVIisatvhPWG---YGM 763
Cdd:cd15929    83 sLGCRVAQVLMQYCVAANYYWLLVEGLYLH----TLLVLAVFSERSIFRLYL-LLGWGAPVLFVV------PWGivkYLY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 764 HN-RCW-LNTETGFIWSFLGPVCMIITINSALLAWTLWVLrqklcsvnseVSKLK-------DTRLLTFKA-IAQIFILG 833
Cdd:cd15929   152 ENtGCWtRNDNMAYWWIIRLPILLAILINFFIFVRILKIL----------VSKLRanqmcktDYKFRLAKStLTLIPLLG 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958802101 834 CSWVLGIFQI-----GPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15929   222 VHEVVFAFVTdeqarGTLRFIKLFFELFLSSFQGLLVAVLYCFANKEVQSELRKKWHR 279
7tmB2_GPR111_115 cd15994
orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of ...
630-878 9.49e-18

orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR111 and GPR115 are highly homologous orphan receptors that belong to group VI adhesion-GPCRs along with GPR110, GPR113, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS. Both GPR111 and GPR5 are present only in land-living animals and are predominantly expressed in the developing skin.


Pssm-ID: 320660 [Multi-domain]  Cd Length: 267  Bit Score: 84.12  E-value: 9.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 630 ISYVGTVISLVCLAL--AIATFLLFRAVQNHNTYLHlHLC-----VCLFLAKILFLTGI---DKTDNQTACAIIAGFLHY 699
Cdd:cd15994     7 ITRIGLGLSIFSLALclTIEAVVWSHVTKTEITYMR-HVCivniaTSLLIADVWFILASivhNTALNYPLCVAATFFLHF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 700 LFLACFFWMLVEAVmlfLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVV--VVIISATVHPWGYGMHNRCWLN-TETGFI 776
Cdd:cd15994    86 FYLSLFFWMLTKAL---LILYGILLVFFKITKSVFIATAFSIGYGCPLViaVLTVAITEPKKGYLRPEACWLNwDETKAL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 777 WSFLGPVCMIITINsaLLAWTLWVLRQKLCSVNSevSKLKDTRLLT--FKAIAQIF-ILGCSWVLGIFQIGPLASIMAYL 853
Cdd:cd15994   163 LAFIIPALSIVVVN--LIVVGVVVVKTQRSSIGE--SCKQDVSNIIriSKNVAILTpLLGLTWGFGLATIIDSRSLPFHI 238
                         250       260
                  ....*....|....*....|....*.
gi 1958802101 854 -FTTINSLQGAFIFLIHCLLNRQVRD 878
Cdd:cd15994   239 iFALLNAFQGFFILLFGTILDRKIRI 264
7tmB1_NPR_B4_insect-like cd15260
insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of ...
626-876 4.08e-17

insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from mollusks and annelid worms. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320388 [Multi-domain]  Cd Length: 267  Bit Score: 82.32  E-value: 4.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVgtvISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFL----TGIDKTD----NQTACAIIAGFL 697
Cdd:cd15260     6 YVYIGGYS---VSLIALIISLAIFFSFRSLRCTRITIHMNLFISFALNNLLWIvwykLVVDNPEvlleNPIWCQALHVLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 698 HYLFLACFFWMLVEAVMLFLMVrnlkvVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNtETGFIW 777
Cdd:cd15260    83 QYFMVCNYFWMFCEGLYLHTVL-----VVAFISEKSLMRWFIAIGWGVPLVITAIYAGVRASLPDDTERCWME-ESSYQW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 778 SFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLkdTRLLTFKAIAqIFI--LGCSWVLGIFQIG---PLASIMAY 852
Cdd:cd15260   157 ILIVPVVLSLLINLIFLINIVRVLLTKLRATSPNPAPA--GLRKAVRATL-ILIplLGLQFLLIPFRPEpgaPLETIYQY 233
                         250       260
                  ....*....|....*....|....
gi 1958802101 853 LFTTINSLQGAFIFLIHCLLNRQV 876
Cdd:cd15260   234 VSALLTSLQGLCVAVLFCFCNGEV 257
7tmB1_PTH-R_related cd15272
invertebrate parathyroid hormone-related receptors, member of the class B family of ...
626-886 4.46e-17

invertebrate parathyroid hormone-related receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes parathyroid hormone (PTH)-related receptors found in invertebrates such as mollusks and annelid worms. The PTH family receptors are members of the B1 subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. The parathyroid hormone type 1 receptor (PTH1R) is found in all vertebrate species and is activated by two polypeptide ligands: parathyroid hormone (PTH), an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)- protein that in turn activates adenylyl cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple signaling pathways.


Pssm-ID: 320400 [Multi-domain]  Cd Length: 285  Bit Score: 82.44  E-value: 4.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCL-------FLAKILFLTGI--------DKTDNQT-- 688
Cdd:cd15272     3 SIRLMYNIGYGLSLVSLLIAVIIMLYFKKLHCPRNTIHINLFVSFilravlsFIKENLLVQGVgfpgdvyyDSNGVIEfk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 689 ------ACAIIAGFLHYLFLACFFWMLVEAVMLflmvRNLKVVNYFSSRNiKMLHLCAFGYGLPVVVVIisatvhPW--- 759
Cdd:cd15272    83 degshwECKLFFTMFNYILGANYMWIFVEGLYL----HMLIFVAVFSENS-RVKWYILLGWLSPLLFVL------PWvfv 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 760 -GYGMHNRCW-LNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWV 837
Cdd:cd15272   152 rATLEDTLCWnTNTNKGYFWIIRGPIVISIAINFLFFINIVRVLFTKLKASNTQESRPFRYRKLAKSTLVLIPLFGVHYM 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958802101 838 LGIFQIGPLASIMAYLF-----TTINSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15272   232 VFVVLPDSMSSDEAELVwlyfeMFFNSFQGFIVALLFCFLNGEVQSEIKKKWQR 285
7tmB1_PTHR cd15265
parathyroid hormone receptors, member of the class B family of seven-transmembrane G ...
626-886 5.67e-17

parathyroid hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to a G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. On the other hand, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. Moreover, the PTH3R is more closely related to the PTH1R than PTH2R. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. The PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320393 [Multi-domain]  Cd Length: 289  Bit Score: 82.42  E-value: 5.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHL---------CVCLFLAKILFLTGIDKTD----------- 685
Cdd:cd15265     3 RLYLIYTVGYSISLVSLTVAVFILGYFRRLHCTRNYIHMHLfvsfmlravSIFVKDAVLYSGSGLDELErpsmedlksiv 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 686 --------NQTACAIIAGFLHYLFLACFFWMLVEAvmLFLmvRNLKVVNYFSSRNIkMLHLCAFGYGLPVVVVIISATVH 757
Cdd:cd15265    83 eappvdksQYVGCKVAVTLFLYFLATNYYWILVEG--LYL--HSLIFMAFFSDKKY-LWGFTLIGWGFPAVFVIPWASVR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 758 pwGYGMHNRCWLNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVN-SEVSKLKDTRLLTFKAIAQIFILGCSW 836
Cdd:cd15265   158 --ATLADTRCWDLSAGNYKWIYQVPILAAIVVNFILFLNIVRVLATKLRETNaGRCDTRQQYRKLAKSTLVLIPLFGVHY 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958802101 837 VLGI----FQIGPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15265   236 IVFMgmpyTEVGLLWQIRMHYELFFNSFQGFFVAIIYCFCNGEVQAEIKKRWER 289
7tmB1_GHRHR cd15270
growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane ...
629-882 7.79e-17

growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor (GHRHR) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320398 [Multi-domain]  Cd Length: 268  Bit Score: 81.38  E-value: 7.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 629 IISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKI-LFLTGI-----DKTD----NQTACAIIAGFLH 698
Cdd:cd15270     6 IIYTVGYSISIVSLCVAVAILVAFRRLHCPRNYIHIQLFFTFILKAIaVFIKDAalfqeDDTDhcsmSTVLCKVSVVFCH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 699 YLFLACFFWMLVEAVMLflmvrNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIIsaTVHPWGYGMHNRCW-LNTETGFIW 777
Cdd:cd15270    86 YCVMTNFFWLLVEAVYL-----NCLLASSFPRGKRYFWWLVLLGWGLPTLCTGT--WILCKLYFEDTECWdINNDSPYWW 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 778 SFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVlgIFQIGPLAS---IMAYLF 854
Cdd:cd15270   159 IIKGPIVISVGVNFLLFLNIIRILLKKLDPRQINFNNSAQYRRLSKSTLLLIPLFGTHYI--IFNFLPDYAglgIRLYLE 236
                         250       260
                  ....*....|....*....|....*...
gi 1958802101 855 TTINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15270   237 LCLGSFQGFIVAVLYCFLNQEVQTEISR 264
7tmB1_GLP2R cd15266
glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G ...
627-882 9.03e-16

glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-2 receptor (GLP2R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor (GCGR) and GLP1R. GLP2R is activated by glucagon-like peptide 2, which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. GLP2R belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320394 [Multi-domain]  Cd Length: 280  Bit Score: 78.63  E-value: 9.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAK--------ILFLTGIDKTDNQ----------- 687
Cdd:cd15266     4 LQLIYTIGYSLSLISLSLALLILLLLRKLHCTRNYIHMNLFASFILRAlavlikdiVLYSTYSKRPDDEtgwisylsees 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 688 -TACAIIAGFLHYLFLACFFWMLVEAVMLFlmvrNLKVVNYFSSRNIkMLHLCAFGYGLPVVVVIisatvhPWG----YG 762
Cdd:cd15266    84 sTSCRVAQVFMHYFVGANYFWLLVEGLYLH----TLLVTAVLSERRL-LKKYMLIGWGTPVLFVV------PWGvakiLL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 763 MHNRCW-LNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLcsvNSEVSKLKDTRLLTFKA-IAQIFILGCSWVLGI 840
Cdd:cd15266   153 ENTGCWgRNENMGIWWIIRGPILLCITVNFYIFLKILKLLLSKL---KAQQMRFTDYKYRLARStLVLIPLLGIHEVVFS 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958802101 841 FQI-----GPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15266   230 FITdeqveGFSRHIRLFIQLTLSSFQGFLVAVLYCFANGEVKAELKK 276
7tmB1_calcitonin_R cd15274
calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
625-876 9.25e-16

calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors for calcitonin (CT) and calcitonin gene-related peptides (CGRPs). Calcitonin, a 32-amino acid peptide hormone, is involved in calcium metabolism in many mammalian species and acts to reduce blood calcium levels and directly inhibits bone resorption by acting on osteoclast. Thus, CT acts as an antagonist to parathyroid hormone and is commonly used in the treatment of bone disorders. The CT receptor is predominantly found in osteoclasts, kidney, and brain, and is primarily coupled to stimulatory G(s) protein, which leads to activation of adenylate cyclase, thereby increasing cAMP production. CGRP, a member of the calcitonin family of peptides, is a potent vasodilator and may contribute to migraine. It is expressed in the peripheral and central nervous system and exists in two forms in humans (alpha-CGRP and beta-CGRP). CGRP meditates its physiological effects through calcitonin receptor-like receptor (CRLR) and receptor activity-modifying protein 1 (RAMP1), a single transmembrane domain protein. Thus, the CRLR/RAMP1 complex serves as a functional CGRP receptor. On the other hand, the CRLR/RAMP2 and CRLR/RAMP3 complexes function as adrenomedullin-specific receptors. The CT and CGRP receptors belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide.


Pssm-ID: 341343 [Multi-domain]  Cd Length: 274  Bit Score: 78.67  E-value: 9.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 625 FSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLC---VCLFLAKILFLT-----GIDKTDNQTACAIIAGF 696
Cdd:cd15274     2 YNLYYLAIVGHSLSIATLLISLGIFFFFRSLSCQRVTLHKNLFlsyILNSIIIIIHLVavvpnGELVARNPVSCKILHFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 697 LHYLFLACFFWMLVEAVMLFLMVrnlkVVNYFSSRNIKMLHLcAFGYGLPVVVVIISATVHPWGYgmHNRCWLNTETGFI 776
Cdd:cd15274    82 HQYMMGCNYFWMLCEGIYLHTLI----VVAVFAEKQRLMWYY-LLGWGFPLIPTTIHAITRAVYY--NDNCWLSSETHLL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 777 WSFLGPVCMIITINSALLAWTLWVLrqklcsvnseVSKLKDTR----LLTFKAIAQIFI----LGCSWVLgiFQIGP--- 845
Cdd:cd15274   155 YIIHGPIMAALVVNFFFLLNIVRVL----------VTKLRETHeaesHMYLKAVKATLIlvplLGIQFVL--FPWRPsgk 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958802101 846 -LASIMAYLFTTINSLQGAFIFLIHCLLNRQV 876
Cdd:cd15274   223 iLGKIYDYVMHSLIHFQGFFVATIFCFCNGEV 254
7tmB1_Secretin_R-like cd15930
secretin receptor-like group of hormone receptors, member of the class B family of ...
626-882 2.89e-15

secretin receptor-like group of hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents G protein-coupled receptors for structurally similar peptide hormones that include secretin, growth-hormone-releasing hormone (GHRH), pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptors, which are expressed in the brain, pancreas, stomach, kidney, and liver. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. All B1 subfamily GPCRs are able to increase intracellular cAMP levels by coupling to adenylate cyclase via a stimulatory Gs protein. However, depending on its cellular location, some members of subfamily B1 are also capable of coupling to additional G proteins such as G(i/o) and/or G(q) proteins, thereby leading to activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320596 [Multi-domain]  Cd Length: 268  Bit Score: 77.09  E-value: 2.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKI--------LFLT-GIDKTDNQTA-CAIIAG 695
Cdd:cd15930     3 TVKIIYTVGYSLSLTSLTTAMIILCLFRKLHCTRNYIHMNLFVSFILRAIavfikdavLFSSeDVDHCFVSTVgCKASMV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 696 FLHYLFLACFFWMLVEAVMLFlmvrNLKVVNYFSSRNIkMLHLCAFGYGLPVVVVIISATVHPwgYGMHNRCW-LNTETG 774
Cdd:cd15930    83 FFQYCVMANFFWLLVEGLYLH----TLLVISFFSERRY-FWWYVLIGWGAPTVFVTVWIVARL--YFEDTGCWdINDESP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 775 FIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSW-VLGIFQIGPLASIMAYL 853
Cdd:cd15930   156 YWWIIKGPILISILVNFVLFINIIRILLQKLRSPDIGGNESSQYKRLARSTLLLIPLFGIHYiVFAFFPENISLGIRLYF 235
                         250       260
                  ....*....|....*....|....*....
gi 1958802101 854 FTTINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15930   236 ELCLGSFQGFVVAVLYCFLNGEVQAEIKR 264
7tmB1_GCGR cd15267
glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled ...
626-882 1.30e-14

glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon receptor (GCGR) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon-like peptide-1 receptor (GLP1R) and GLP2R. GCGR is activated by glucagon, which is derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320395 [Multi-domain]  Cd Length: 281  Bit Score: 75.24  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFL--AKILFLTGIDKTDNQT--------------- 688
Cdd:cd15267     5 SFQVMYTVGYSLSLGALLLALAILGGFSKLHCMRNAIHMNLFASFILkaSSVLVIDGLLRTRYSQkieddlsstwlsdea 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 689 --ACAIIAGFLHYLFLACFFWMLVEAVMLFlmvrNLKVVNYFSSRNIKMLHLCaFGYGLPVVVVIISATVHPWgYGMHnR 766
Cdd:cd15267    85 vaGCRVAAVFMQYGIVANYCWLLVEGIYLH----NLLVLAVFPERSYFSLYLC-IGWGAPALFVVPWVVVKCL-YENV-Q 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 767 CW-LNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTrlLTFKAIAQIFILGCSWVLGIF---- 841
Cdd:cd15267   158 CWtSNDNMGFWWILRFPVFLAILINFFIFVRIIQILVSKLRARQMHYTDYKFR--LAKSTLTLIPLLGIHEVVFAFvtde 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958802101 842 -QIGPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15267   236 hAQGTLRSAKLFFDLFLSSFQGLLVAVLYCFLNKEVQSELRR 277
7tmB1_NPR_B7_insect-like cd15273
insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of ...
629-886 1.32e-14

insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from invertebrates. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320401 [Multi-domain]  Cd Length: 285  Bit Score: 75.10  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 629 IISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCL-------FLAKILFLTG-----------------IDKT 684
Cdd:cd15273     6 GISQIGYIVSLITLIIAFAIFLSFKKLHCARNKLHMHLFASFilrafmtLLKDSLFIDGlglladiverngggnevIANI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 685 DNQTACAIIAGFLHYLFLACFFWMLVEAVMLF-LMVRNLkvvnYFSSRNIKMLHLcaFGYGLPVVVVIISATVHpwgYGM 763
Cdd:cd15273    86 GSNWVCKAITSLWQYFIIANYSWILMEGLYLHnLIFLAL----FSDENNIILYIL--LGWGLPLIFVVPWIVAR---ILF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 764 HNR-CWLNTETGFIWSFL-GPVCMIITINSALLAWTLWVLRQKL-CSVNSEVSK----LKDTRLLT--FKAIAQIFiLGC 834
Cdd:cd15273   157 ENSlCWTTNSNLLNFLIIrIPIMISVLINFILFLNIVRVLLVKLrSSVNEDSRRykkwAKSTLVLVplFGVHYTIF-LIL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958802101 835 SWVLGIFQIGPLasimAYLFT--TINSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15273   236 SYLDDTNEAVEL----IWLFCdqLFASFQGFFVALLYCFLNGEVRAEIQRKWRR 285
7tmB1_PTH2R cd15982
parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G ...
627-886 1.50e-14

parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 2 receptor (PTH2R), one of the three subtypes of PTH receptor family, is found in mammals and fish, but not in chicken or frog. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39) but not by PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs. These results suggest that TIP-39 is a natural ligand for PTH2R. Conversely, PTH1R is activated by PTH and PTHrP, but not by TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320648 [Multi-domain]  Cd Length: 289  Bit Score: 75.36  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFL-AKILFL--------------------------- 678
Cdd:cd15982     4 LYIMYTVGYSISFSSLAVAIFIIGYFRRLHCTRNYIHMHLFVSFMLrAASIFVkdkvvhthigvkeldavlmndfqnavd 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 679 -TGIDKTdNQTACAIIAGFLHYLFLACFFWMLVEAVMLflmvRNLKVVNYFSSRNikmlHLCAF---GYGLPVVVVIISA 754
Cdd:cd15982    84 aPPVDKS-QYVGCKIAVVMFIYFLATNYYWILVEGLYL----HSLIFVAFFSDTK----YLWGFtliGWGFPAVFVAAWA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 755 TVHpwGYGMHNRCWLNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNS-EVSKLKDTRLLTFKAIAQIFILG 833
Cdd:cd15982   155 VVR--ATLADARCWELSAGDIKWIYQAPILAAIGLNFILFLNTVRVLATKIWETNAvGYDTRKQYRKLAKSTLVLVLVFG 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958802101 834 CSWVlgIFQIGPLA------SIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15982   233 VHYI--VFVCLPHTftglgwEIRMHCELFFNSFQGFFVSIIYCYCNGEVQTEIKKTWTR 289
7tmB1_VIP-R1 cd15269
vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of ...
633-882 2.17e-14

vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 1 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320397 [Multi-domain]  Cd Length: 268  Bit Score: 74.50  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 633 VGTVISLVCLALAIATFLLFRAVQNHNTYLHLHL-------CVCLFLAKILFLTGIDKTDNQTA---CAIIAGFLHYLFL 702
Cdd:cd15269    10 IGHSLSLISLTAAMIILCLFRKLHCTRNYIHMHLfmsfilrAIAVFIKDAVLFESGEEDHCSVAsvgCKAAMVFFQYCIM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 703 ACFFWMLVEAVMLFlmvrNLKVVNYFSSRNIKMLHLCaFGYGLPVVVVIISATVHpwGYGMHNRCW-LNTETGFIWSFLG 781
Cdd:cd15269    90 ANFFWLLVEGLYLH----TLLAVSFFSERKYFWWYIL-IGWGAPSVFITAWSVAR--IYFEDVGCWdTIIESLLWWIIKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 782 PVCMIITINSALLAWTLWVLRQKLCSV------NSEVSKLKDTRLLTfkaiaqIFILGCSWVLGIFQIGPLASIMAYLFT 855
Cdd:cd15269   163 PILVSILVNFILFICIIRILVQKLHSPdigrneSSQYSRLAKSTLLL------IPLFGIHYIMFAFFPDNFKAEVKLVFE 236
                         250       260
                  ....*....|....*....|....*...
gi 1958802101 856 TI-NSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15269   237 LIlGSFQGFVVAVLYCFLNGEVQAELKR 264
7tmB1_secretin cd15275
secretin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
625-882 2.25e-14

secretin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Secretin receptor is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include vasoactive intestinal peptide (VIP), growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors, and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptor, which is expressed in the brain, pancreas, stomach, kidney, and liver.


Pssm-ID: 320403 [Multi-domain]  Cd Length: 271  Bit Score: 74.39  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 625 FSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHlcvcLFLAKILFLTGIDKTDN--------------QTAC 690
Cdd:cd15275     2 MYLKTMYTVGYSVSLVSLAIALAILCSFRRLHCTRNYIHMQ----LFLSFILRAISIFIKDAvlfsseddnhcdiyTVGC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 691 AIIAGFLHYLFLACFFWMLVEAVMLFLMVrnlkVVNYFSSRniKMLH-LCAFGYGLPVVVVIisatvhPWGYGMH----N 765
Cdd:cd15275    78 KVAMVFSNYCIMANYSWLLVEGLYLHSLL----SISFFSER--KHLWwYIALGWGSPLIFII------SWAIARYlhenE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 766 RCWLNTETGFIWSFL-GPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIF--- 841
Cdd:cd15275   146 GCWDTRRNAWIWWIIrGPVILSIFVNFILFLNILRILMRKLRAPDMRGNEFSQYKRLAKSTLLLIPLFGLHYILFAFfpe 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958802101 842 -QIGPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15275   226 dVSSGTMEIWLFFELALGSFQGFVVAVLYCFLNGEVQLEIQR 267
7tmB1_GHRHR2 cd15271
growth-hormone-releasing hormone receptor type 2, member of the class B family of ...
633-884 5.96e-14

growth-hormone-releasing hormone receptor type 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor type 2 (GHRHR2) is found in non-mammalian vertebrates such as chicken and frog. It is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), vasoactive intestinal peptide, and mammalian growth hormone-releasing hormone. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Mammalian GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. Mammalian GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320399 [Multi-domain]  Cd Length: 267  Bit Score: 72.84  E-value: 5.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 633 VGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTG-----IDKTDNQ-----TACAIIAGFLHYLFL 702
Cdd:cd15271    10 VGYGTSLTSLITAVLIFCTFRKLHCTRNYIHINLFVSFILRALAVFIKdavlfADESVDHctmstVACKAAVTFFQFCVL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 703 ACFFWMLVEAVMLflmvRNLKVVNYFSSRNIKMLHLcAFGYGLPVVVVIISATVHpwgYGMHNR-CWLNTETGFIWSFLG 781
Cdd:cd15271    90 ANFFWLLVEGMYL----QTLLLLTFTSDRKYFWWYI-LIGWGAPSVTVTVWVLTR---LQYDNRgCWDDLESRIWWIIKT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 782 PVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIF---QIGPLASImaYLFTTIN 858
Cdd:cd15271   162 PILLSVFVNFLIFINVIRILVQKLKSPDVGGNDTSHYMRLAKSTLLLIPLFGVHYVVFAFfpeHVGVEARL--YFELVLG 239
                         250       260
                  ....*....|....*....|....*.
gi 1958802101 859 SLQGAFIFLIHCLLNRQVRDEYRKLL 884
Cdd:cd15271   240 SFQGFIVALLYCFLNGEVQAEIKKRL 265
7tmB1_CRF-R1 cd15445
corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane ...
629-882 9.47e-14

corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320561 [Multi-domain]  Cd Length: 265  Bit Score: 72.28  E-value: 9.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 629 IISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKI------LFLTGIDKTDNQTACAIIAGFLHYLFL 702
Cdd:cd15445     6 IINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLITAFILRNAtwfvvqLTMSPEVHQSNVVWCRLVTAAYNYFHV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 703 ACFFWMLVEAVMLFLMVrnlkVVNYFSSRNIKMLHLCaFGYGLPVVVVIisatvhPWGYGM----HNRCWLNTETGFIWS 778
Cdd:cd15445    86 TNFFWMFGEGCYLHTAI----VLTYSTDKLRKWMFIC-IGWCIPFPIIV------AWAIGKlyydNEKCWFGKRAGVYTD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 779 FL--GPVCMIITINSALLAWTLWVLRQKL-CSVNSEVSKLKDTRLLTFKAIAqifILGCSWVLgiFQIGPLAS-----IM 850
Cdd:cd15445   155 YIyqGPMILVLLINFIFLFNIVRILMTKLrASTTSETIQYRKAVKATLVLLP---LLGITYML--FFVNPGEDeisriVF 229
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958802101 851 AYLFTTINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15445   230 IYFNSFLESFQGFFVSVFYCFLNSEVRSAVRK 261
7tmB1_CRF-R2 cd15446
corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane ...
629-882 1.01e-13

corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320562 [Multi-domain]  Cd Length: 264  Bit Score: 72.30  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 629 IISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILF--LTGIDKT---DNQTACAIIAGFLHYLFLA 703
Cdd:cd15446     6 IINYLGHCISVGALVVAFLLFLCLRSIRCLRNIIHWNLITTFILRNVMWflLQMIDHNiheSNEVWCRCITTIYNYFVVT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAVMLflmvrNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPwgYGMHNRCWLNTETGFIWSFL--G 781
Cdd:cd15446    86 NFFWMFVEGCYL-----HTAIVMTYSTDKLRKWVFLFIGWCIPCPIIVAWAIGKL--YYENEQCWFGKEPGKYIDYIyqG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 782 PVCMIITINSALLAWTLWVLRQKLCSvnSEVSKLKDTRLLTFKAIAQIFILGCSWVLgiFQIGP----LASIMAYLFTT- 856
Cdd:cd15446   159 PVILVLLINFVFLFNIVRILMTKLRA--STTSETIQYRKAVKATLVLLPLLGITYML--FFVNPgeddISQIVFIYFNSf 234
                         250       260
                  ....*....|....*....|....*.
gi 1958802101 857 INSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15446   235 LQSFQGFFVSVFYCFLNGEVRSAARK 260
7tmB1_PTH1R cd15984
parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G ...
627-886 1.28e-13

parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320650 [Multi-domain]  Cd Length: 290  Bit Score: 72.29  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHL-------CVCLFLAKILFLTG--IDKTDNQT--------- 688
Cdd:cd15984     4 LYLIYTVGYSISLGSLTVAVLILGYFRRLHCTRNYIHMHLflsfmlrAVSIFVKDAVLYSGsaLEEMERITeedlksite 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 689 ----------ACAIIAGFLHYLFLACFFWMLVEAVMLflmvRNLKVVNYFSSRNIkMLHLCAFGYGLPVVVVIISATVHp 758
Cdd:cd15984    84 appadkaqfvGCKVAVTFFLYFLATNYYWILVEGLYL----HSLIFMAFFSEKKY-LWGFTLFGWGLPAVFVTIWASVR- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 759 wGYGMHNRCWLNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSklkDTRLLTFKAIAQIFIL----GC 834
Cdd:cd15984   158 -ATLADTGCWDLSAGNLKWIIQVPILAAIVVNFILFINIVRVLATKLRETNAGRC---DTRQQYRKLLKSTLVLmplfGV 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958802101 835 SWVlgIFQIGPLASIMAYLFTT-------INSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15984   234 HYI--VFMAMPYTEVSGILWQVqmhyemlFNSFQGFFVAIIYCFCNGEVQAEIKKSWSR 290
7tmB1_NPR_B3_insect-like cd15262
insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of ...
637-882 1.72e-13

insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of hormone receptors; member of the class B secretin-like seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Bombyx mori (silk worm) and its closely related proteins from arthropods. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320390 [Multi-domain]  Cd Length: 270  Bit Score: 71.71  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 637 ISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILF-----------LTGIDK----TDNQTACAIIAGFLHYLF 701
Cdd:cd15262    14 VSVVTSLPAVFIFYSYKRLRITRVILHRNLLISIIIRNILViiskvfvildaLTSSGDdtvmNQNAVVCRLLSIFERAAR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 702 LACFFWMLVEAVMLflmvrNLKVVNYFSsRNIKMLHLCAFGYGLPVVVVIISATVHpwgyGMHN--RCWLNTETGFIWSF 779
Cdd:cd15262    94 NAVFACMFVEGFYL-----HRLIVAVFA-EKSSIRFLYVIGAVLPLFPVIIWAIIR----ALHNdhSCWVVDIEGVQWVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 780 LGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFkaiaQIFILGCSWVLGIFQIGP----LASIMAYLFT 855
Cdd:cd15262   164 DTPRLFILLVNTVLLVDIIRVLVTKLRNTEENSQTKSTTRATLF----LVPLFGLHFVITAYRPSTddcdWEDIYYYANY 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958802101 856 TINSLQGAFIFLIHCLLNRQVRDE----YRK 882
Cdd:cd15262   240 LIEGLQGFLVAILFCYINKEVHYLikntYRK 270
7tmB1_GLP1R cd15268
glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G ...
625-886 2.05e-13

glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-1 receptor (GLP1R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor and GLP2R. GLP1R is activated by glucagon-like peptide 1 (GLP1), which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 341342 [Multi-domain]  Cd Length: 279  Bit Score: 71.52  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 625 FSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHL-------CVCLFLA----KILFLT--------GIDKTD 685
Cdd:cd15268     2 LFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLfasfilrALSVFIKdaalKWMYSTaaqqhqwdGLLSYQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 686 NQTACAIIAGFLHYLFLACFFWMLVEAVMLFlmvrNLKVVNYFSSRNIKMLHLCaFGYGLPVVVVIisatvhPWGYGMH- 764
Cdd:cd15268    82 DSLSCRLVFLLMQYCVAANYYWLLVEGVYLY----TLLAFSVFSEQRIFRLYLS-IGWGVPLLFVI------PWGIVKYl 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 765 ---NRCWLNTETGFIWSFLG-PVCMIITINSALLAWTLWVLRQKL-----CSVNSEVSKLKDTRLLtfkaiaqIFILGCS 835
Cdd:cd15268   151 yedEGCWTRNSNMNYWLIIRlPILFAIGVNFLIFIRVICIVVSKLkanlmCKTDIKCRLAKSTLTL-------IPLLGTH 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958802101 836 WVLGIFQI-----GPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15268   224 EVIFAFVMdeharGTLRFVKLFTELSFTSFQGLMVAILYCFVNNEVQMEFRKSWER 279
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
571-620 4.47e-13

G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin.


Pssm-ID: 197639  Cd Length: 49  Bit Score: 64.33  E-value: 4.47e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958802101  571 ERSICVSWNTDveDGRWTPSGCETVEASETHTVCSCNRMTNLAIIMASGE 620
Cdd:smart00303   1 FNPICVFWDES--SGEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPP 48
7tmB1_GlucagonR-like_1 cd15985
uncharacterized group of glucagon receptor-like proteins, member of the class B family of ...
626-882 2.13e-12

uncharacterized group of glucagon receptor-like proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This group consists of uncharacterized proteins with similarity to members of the glucagon receptor family of G protein-coupled receptors, which include glucagon receptor (GCGR), and glucagon-like peptide-1 receptor (GLP1R), and GLP2R. The glucagon receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320651 [Multi-domain]  Cd Length: 280  Bit Score: 68.42  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFL-----------------AKILFLTGIDKTDNQT 688
Cdd:cd15985     3 SFRMLYTVGYTLSLLTLVSALLILTSIRKLHCTRNYIHANLFASFILravsvivkdtllerrwgREIMRVADWGELLSHK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 689 A---CAIIAGFLHYLFLACFFWMLVEAVMLFlmvrNLKVVNYFSSRNIKMLHLCaFGYGLPVVVVIisatvhPW---GYG 762
Cdd:cd15985    83 AaigCRMAQVVMQYCILANHYWFFVEAVYLY----KLLIGAVFSEKNYYLLYLY-LGWGTPVLFVV------PWmlaKYL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 763 MHNR-CW-LNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSklkDTRLLTFKA-IAQIFILGCSWVLG 839
Cdd:cd15985   152 KENKeCWaLNENMAYWWIIRIPILLASLINLLIFMRILKVILSKLRANQKGYA---DYKLRLAKAtLTLIPLFGIHEVVF 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958802101 840 IFQI-----GPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15985   229 IFATdeqttGILRYIKVFFTLFLNSFQGFLVAVLYCFANKEVKSELLK 276
7tmE_cAMP_R_Slime_mold cd14940
slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G ...
626-872 1.23e-11

slime mold cyclic AMP receptor, member of the class E family of seven-transmembrane G protein-coupled receptors; This family represents the class E of seven-transmembrane G-protein coupled receptors found in soil-living amoebas, commonly referred to as slime molds. The class E family includes cAMP receptors (cAR1-4) and cAMP receptors-like proteins (CrlA-C) from Dictyostelium discoideum, and their highly homologous cAMP receptors (TasA and TasB) from Polysphondylium pallidum. So far, four subtypes of cAMP receptors (cAR1-4) have been identified that play an essential role in the detection and transmit of the periodic extracellular cAMP waves that regulate chemotactic cell movement during Dictyostelium development, from the unicellular amoeba aggregate into many multicellular slugs and then differentiate into a sporocarp, a fruiting body with cells specialized for different functions. These four subtypes differ in their expression levels and patterns during development. cAR1 is high-affinity receptor that is the first one to be expressed highly during early aggregation and continues to be expressed at low levels during later developmental stages. cAR1 detects extracellular cAMP and is coupled to G-alpha2 protein. Cells lacking cAR1 fail to aggregate, demonstrating that cAR1 is responsible for aggregation. During later aggregation the high-affinity cAR3 receptor is expressed at low levels. Nonetheless, cells lacking cAR3 do not show an obviously altered pattern of development and are still able to aggregate into fruiting bodies. In contrast, cAR2 and cAR4 are low affinity receptors expressed predominantly after aggregation in pre-stalk cells. cAR2 is essential for normal tip formation and deletion of the receptor arrests development at the mound stage. On the other hand, CAR4 regulates axial patterning and cellular differentiation, and deletion of the receptor results in defects during culmination. Furthermore, three cAMP receptor-like proteins (CrlA-C) were identified in Dictyostelium that show limited sequence similarity to the cAMP receptors. Of these CrlA is thought to be required for normal cell growth and tip formation in developing aggregates.


Pssm-ID: 320094 [Multi-domain]  Cd Length: 256  Bit Score: 65.84  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 626 SLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTG---IDKTDNQTACAIIAGFLHYLFL 702
Cdd:cd14940     1 ALYAILLFADFSSIIGCLFVLVGFWLLKLLRNHITRVISCFCLTSLLKDIIYTMLtltQSARPDGFLCYLYAIVITYGSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 703 ACFFWMLVEAVMLFLM-VRNLKVVNYFSsrniKMLHLcaFGYGLPVVVVIISATVHPWGYgMHNRCWLNTE-TGFIWS-F 779
Cdd:cd14940    81 SCWLWTLCLAISIYLLiVKREPEPEKFE----KYYHF--VCWGLPLISTIIMLIKHHYGP-VGNWCWIGNQyTGYRFGlF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 780 LGPVCMIITINSALLAWTLWVLRQKlcsVNSEVSKLKDtRLLT--FKAIAQIFILGCSWVlgifqigplasimaylFTTI 857
Cdd:cd14940   154 YGPFFIIFGISAVLVGLTSHYTYQV---IHNWVSDNKD-LHKTyqFKLVNYIIVFLLCWI----------------FAVI 213
                         250       260
                  ....*....|....*....|.
gi 1958802101 858 NSLQGAF------IFLIHCLL 872
Cdd:cd14940   214 NRIQNALnpfpfaLNLLHTYL 234
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
574-615 2.03e-11

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.


Pssm-ID: 460350  Cd Length: 44  Bit Score: 59.24  E-value: 2.03e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958802101 574 ICVSWN-TDVEDGRWTPSGCETVEASETHTVCSCNRMTNLAII 615
Cdd:pfam01825   2 QCVFWDfTNSTTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
627-873 6.83e-11

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


Pssm-ID: 410628 [Multi-domain]  Cd Length: 267  Bit Score: 63.99  E-value: 6.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGI-------DKTDNQTACAIIAGFLHY 699
Cdd:cd14964     1 TTIILSLLTCLGLLGNLLVLLSLVRLRKRPRSTRLLLASLAACDLLASLVVLVLFfllglteASSRPQALCYLIYLLWYG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 700 LFLACFFWMLVEAVMLFLMVRNLKVVNYFSSRNiKMLHLCAFGYGLPVVVVIISATVHpwgYGMHNRCWLNTETGFI--- 776
Cdd:cd14964    81 ANLASIWTTLVLTYHRYFALCGPLKYTRLSSPG-KTRVIILGCWGVSLLLSIPPLVGK---GAIPRYNTLTGSCYLIctt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 777 ---------WSFLGPVCMIITINSALLAwtlwVLRQKLCSVNSEVSKLKDTRLLTFK--AIAQIFILGCSWVLGIFQI-- 843
Cdd:cd14964   157 iyltwgfllVSFLLPLVAFLVIFSRIVL----RLRRRVRAIRSAASLNTDKNLKATKslLILVITFLLCWLPFSIVFIlh 232
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958802101 844 -----GPLASIMAYLFTTINSLQGAFIFLIHCLLN 873
Cdd:cd14964   233 alvaaGQGLNLLSILANLLAVLASTLNPFIYCLGN 267
7tmB1_PACAP-R1 cd15987
pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B ...
633-882 7.35e-11

pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Pituitary adenylate cyclase-activating polypeptide type 1 receptor (PACAP-R1) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. PACAP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level.


Pssm-ID: 320653 [Multi-domain]  Cd Length: 268  Bit Score: 63.83  E-value: 7.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 633 VGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKI-LFLT-GIDKTDNQT--------ACAIIAGFLHYLFL 702
Cdd:cd15987    10 VGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLFVSFILRAIsVFIKdGVLYAEQDSdhcfvstvECKAVMVFFHYCVM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 703 ACFFWMLVEAVMLFlmvrNLKVVNYFSSRNIKMLHlCAFGYGLPVVVVIISATVHPwgYGMHNRCW-LNTETGFIWSFLG 781
Cdd:cd15987    90 SNYFWLFIEGLYLF----TLLVETFFPERRYFYWY-TIIGWGTPTICVTVWAVLRL--HFDDTGCWdMNDNTALWWVIKG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 782 PVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTT-INSL 860
Cdd:cd15987   163 PVVGSIMINFVLFIGIIIILVQKLQSPDIGGNESSIYLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFELgLGSF 242
                         250       260
                  ....*....|....*....|..
gi 1958802101 861 QGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15987   243 QGFVVAVLYCFLNGEVQSEIKR 264
7tmB1_VIP-R2 cd15986
vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of ...
633-882 1.33e-09

vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 2 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320652 [Multi-domain]  Cd Length: 269  Bit Score: 60.20  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 633 VGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFL---------TGIDKTDNQTA---CAIIAGFLHYL 700
Cdd:cd15986    10 LGHSVSLIALTTGSTILCLFRKLHCTRNYIHLNLFFSFILRAISVLvkddilyssSNTEHCTVPPSligCKVSLVILQYC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 701 FLACFFWMLVEAVMLFLMvrnlkVVNYFSSRNIKMLHLCaFGYGLPVVVVIisatvhPWG----YGMHNRCWLNTETGFI 776
Cdd:cd15986    90 IMANFYWLLVEGLYLHTL-----LVVIFSENRHFIVYLL-IGWGIPTVFII------AWIvariYLEDTGCWDTNDHSVP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 777 WSFLG-PVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFT 855
Cdd:cd15986   158 WWVIRiPIIISIILNFILFISIIRILLQKLRSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYIVFVYFPDSSSSNYQIFFE 237
                         250       260
                  ....*....|....*....|....*...
gi 1958802101 856 -TINSLQGAFIFLIHCLLNRQVRDEYRK 882
Cdd:cd15986   238 lCLGSFQGLVVAILYCFLNSEVQGELKR 265
7tmB1_PTH3R cd15983
parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G ...
627-886 2.32e-09

parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 3 receptor (PTH3R), one of the three subtypes of PTH receptor family, is found in chicken and fish, but it is absent in mammals. On the other hand, the PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH1R is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. Conversely, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320649 [Multi-domain]  Cd Length: 285  Bit Score: 59.55  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHL-------CVCLFLAKILFLTGIDKTDNQ------------ 687
Cdd:cd15983     4 LHLMYTIGYSISLAALLVAVCILCYFKRLHCTRNYIHIHLfasficrAGSIFVKDAVLYSGTNEGEALdekiefglspgt 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 688 ----TACAIIAGFLHYLFLACFFWMLVEAVMLflmvRNLKVVNYFSSRNIkMLHLCAFGYGLPVVVVIISATVHpwGYGM 763
Cdd:cd15983    84 rlqwVGCKVTVTLFLYFLATNHYWILVEGLYL----HSLIFMAFLSDKNY-LWALTIIGWGLPAVFVSVWASVR--VSLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 764 HNRCWLNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNS-EVSKLKDTRLLTFKAIAQIFILGCSWVLgiFQ 842
Cdd:cd15983   157 DTQCWDLSAGNLKWIYQVPILAAILVNFFLFLNIVRVLASKLWETNTgKLDPRQQYRKLLKSTLVLMPLFGVHYVL--FM 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958802101 843 IGPLASIMAYLFTT-------INSLQGAFIFLIHCLLNRQVRDEYRKLLTR 886
Cdd:cd15983   235 AMPYTDVTGLLWQIqmhyemlFNSSQGFFVAFIYCFCNGEVQAEIKKAWLR 285
7tmB2_GPR125 cd15999
G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G ...
627-790 3.34e-09

G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR125 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan receptors GPR123 and GPR124. GPR125 directly interacts with dishevelled (Dvl) via its intracellular C-terminus, and together, GPR125 and Dvl recruit a subset of planar cell polarity (PCP) components into membrane subdomains, a prerequisite for activation of Wnt/PCP signaling. Thus, GPR125 influences the noncanonical WNT/PCP pathway, which does not involve beta-catenin, through interacting with and modulating the distribution of Dvl. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320665  Cd Length: 312  Bit Score: 59.49  E-value: 3.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLFRA---VQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLA 703
Cdd:cd15999     4 LHPVVYATAVVLLLCLLTIIVSYIYHHSlvrISRKSWHMLVNLCFHIFLTCAVFVGGINQTRNASVCQAVGIILHYSTLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 704 CFFWMLVEAvmlflmvRNL-KVVNYFSSRNIK----------MLHLCAFGYGLPVVVVIISATVHPWGYGMHNR---CWL 769
Cdd:cd15999    84 TVLWVGVTA-------RNIyKQVTRKAKRCQDpdeppppprpMLRFYLIGGGIPIIVCGITAAANIKNYGSRPNapyCWM 156
                         170       180
                  ....*....|....*....|.
gi 1958802101 770 NTETGfIWSFLGPVCMIITIN 790
Cdd:cd15999   157 AWEPS-LGAFYGPAGFIIFVN 176
7tmB2_GPR124 cd15998
G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G ...
627-881 3.66e-09

G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR124 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, which also includes orphan GPR123 and GPR125. GPR124, also known as tumor endothelial marker 5 (TEM5), is highly expressed in tumor vessels and in the vasculature of the developing embryo. GPR124 is essentially required for proper angiogenic sprouting into neural tissue, CNS-specific vascularization, and formation of the blood-brain barrier. GPR124 interacts with the PDZ domain of DLG1 (discs large homolog 1) through its PDZ-binding motif. Recently, studies of double-knockout mice showed that GPR124 functions as a co-activator of Wnt7a/Wnt7b-dependent beta-catenin signaling in brain endothelium. Moreover, WNT7-stimulated beta-catenin signaling is regulated by GPR124's intracellular PDZ binding motif and leucine-rich repeats (LRR) in its N-terminal extracellular domain. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320664 [Multi-domain]  Cd Length: 268  Bit Score: 58.81  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 627 LYIISYVGTVISLVCLALAIATFLLfravqNHNT--------YLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLH 698
Cdd:cd15998     4 LHPVVYPCTALLLLCLFSTIITYIL-----NHSSihvsrkgwHMLLNLCFHIAMTSAVFAGGITLTNYQMVCQAVGITLH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 699 YLFLACFFWMLVEAVMLFlmvrnlKVVNYFSSRNIK----------MLHLCAFGYGLPVVVVIISATVHPWGYGMHN-RC 767
Cdd:cd15998    79 YSSLSTLLWMGVKARVLH------KELTWRAPPPQEgdpalptprpMLRFYLIAGGIPLIICGITAAVNIHNYRDHSpYC 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 768 WLntetgfIW-----SFLGPVCMIItinsaLLAWTLWVLRQ-KLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIF 841
Cdd:cd15998   153 WL------VWrpslgAFYIPVALIL-----LVTWIYFLCAGlHLRGPSADGDSVYSPGVQLGALVTTHFLYLAMWACGAL 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958802101 842 QIGP---LASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYR 881
Cdd:cd15998   222 AVSQrwlPRVVCSCLYGVAASALGLFVFTHHCARRRDVRASWR 264
EGF_CA smart00179
Calcium-binding EGF-like domain;
112-151 3.69e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 49.94  E-value: 3.69e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958802101  112 DVDECLTIGICPKNSNCSNSVGSYSCTCQSGFvSNGSTCE 151
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY-TDGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
112-151 2.23e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 47.63  E-value: 2.23e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958802101 112 DVDECLTIGICPKNSNCSNSVGSYSCTCQSGFVsnGSTCE 151
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
152-182 2.28e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.63  E-value: 2.28e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958802101  152 DEDECVTRNACPEHATCHNTLGSYYCTCNEG 182
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPG 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
201-234 3.31e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 3.31e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958802101  201 DVDECSRNStLCGPSFICINTLGSYSCSCPAGFS 234
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
201-237 3.60e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 47.25  E-value: 3.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958802101 201 DVDECSRNStLCGPSFICINTLGSYSCSCPAGFSLST 237
Cdd:cd00054     1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGYTGRN 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
152-182 5.02e-07

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.86  E-value: 5.02e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101 152 DEDECVTRNACPEHATCHNTLGSYYCTCNEG 182
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPG 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
251-280 1.37e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.70  E-value: 1.37e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958802101  251 DIDEC--DDICPSNSSCTNTLGSYFCTCHPGF 280
Cdd:smart00179   1 DIDECasGNPCQNGGTCVNTVGSYRCECPPGY 32
7tmB2_GPR123 cd16000
G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G ...
624-870 1.98e-06

G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR123 is an orphan receptor that has been classified as that belongs to the group III of adhesion GPCRs, and also includes orphan receptors GPR124 and GPR125. GPR123 is predominantly expressed in the CNS including thalamus, brain stem and regions containing large pyramidal cells, yet its biological function remains to be determined. Adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320666 [Multi-domain]  Cd Length: 275  Bit Score: 50.34  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 624 EFsLYIISYVGTVISLVCLALAIATFLLFRA---VQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYL 700
Cdd:cd16000     2 EF-LHPVVYACTAVMLLCLFASIITYIVHHStirISRKGWHMLLNFCFHTALTFAVFAGGINRTKYPIICQAVGIVLHYS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 701 FLACFFWMLVEAVMLFLMV--RNLKVVNYFSSRNIK--MLHLCAFGYGLPVVVVIISATVHPWGYGMHNR----CWLNTE 772
Cdd:cd16000    81 TLSTMLWIGVTARNIYKQVtkKPHLCQDTDQPPYPKqpLLRFYLVSGGVPFIICGITAATNINNYGTEDEdtpyCWMAWE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 773 TGfIWSFLGPVCMIITINSALLAWTLWVLR---QKLCSVNSEVSKLKDTRLLTFkaiaQIFILGCSWVLGIFQI--GP-L 846
Cdd:cd16000   161 PS-LGAFYGPVAFIVLVTCIYFLCTYVQLRrhpERKYELKNEHSFKAQLRAAAF----TLFLFTATWAFGALAVsqGHfL 235
                         250       260
                  ....*....|....*....|....
gi 1958802101 847 ASIMAYLFTTINSLQGAFIFLIHC 870
Cdd:cd16000   236 DMIFSCLYGAFCVTLGLFILIHHC 259
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
251-280 7.98e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 7.98e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 251 DIDECDD--ICPSNSSCTNTLGSYFCTCHPGF 280
Cdd:cd00054     1 DIDECASgnPCQNGGTCVNTVGSYRCSCPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
251-279 8.89e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 42.99  E-value: 8.89e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 251 DIDECDD---ICPSNSSCTNTLGSYFCTCHPG 279
Cdd:pfam07645   1 DVDECATgthNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
201-232 1.72e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 42.22  E-value: 1.72e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 201 DVDECSRNSTLCGPSFICINTLGSYSCSCPAG 232
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
112-142 2.28e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.84  E-value: 2.28e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 112 DVDECLTIG-ICPKNSNCSNSVGSYSCTCQSG 142
Cdd:pfam07645   1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
152-182 3.48e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.45  E-value: 3.48e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958802101 152 DEDECVT-RNACPEHATCHNTLGSYYCTCNEG 182
Cdd:pfam07645   1 DVDECATgTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA pfam07645
Calcium-binding EGF domain;
298-328 4.95e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 41.07  E-value: 4.95e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101 298 DIDECTQDPFRCGRNSSCTNVPGSYNCSCLP 328
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPD 31
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
120-150 6.55e-05

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 40.66  E-value: 6.55e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101 120 GICPKNSNCSNSVGSYSCTCQSGFVSNGSTC 150
Cdd:pfam12947   6 GGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
298-331 7.68e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 7.68e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958802101  298 DIDECTQDPfRCGRNSSCTNVPGSYNCSCLPDFR 331
Cdd:smart00179   1 DIDECASGN-PCQNGGTCVNTVGSYRCECPPGYT 33
Dicty_CAR pfam05462
Slime mold cyclic AMP receptor; This family consists of cyclic AMP receptor (CAR) proteins ...
616-840 1.48e-04

Slime mold cyclic AMP receptor; This family consists of cyclic AMP receptor (CAR) proteins from slime molds. CAR proteins are responsible for controlling development in Dictyostelium discoideum.


Pssm-ID: 283188  Cd Length: 305  Bit Score: 44.78  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 616 MASGELTMEFSLYIISYVGTVISlvCLALAIAtFLLFRAVQNHNTYLHLHLCVCLFLaKILFLTGIDKTDNQTA----CA 691
Cdd:pfam05462   2 MTQQEIDLSYSVLLIADFSSIIG--CFLVLIG-FWRLKLLRNHITKVISCFCATSLL-KDLISTILTLTNSAQSggfpCY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 692 IIAGFLHYLFLACFFWMLveavMLFLMVRNLKVVNYFSSRNIKMLHLCaFGYGLPVVVVII---SATVHPWGygmhNRCW 768
Cdd:pfam05462  78 LYAIVITYGSLACWLWTL----CLAFSIYNLIVKREPEPEKFEKYYFF-VCWGLPLISTIVmlsKDTIEFVG----NWCW 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958802101 769 L-NTETGFIWS-FLGPVCMIITINSALLAWTlwvLRQKLCSVNSEVSKLKDTRL-LTFKAIAQIFILGCSWVLGI 840
Cdd:pfam05462 149 IgEQYTGYRFGlFYGPFFAIWGISAVLVGLT---SRYTYSVIRNSVSDNKDKHMtYQFKLINYIIVFLVCWVFAV 220
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
156-189 3.55e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 38.73  E-value: 3.55e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1958802101 156 CVTRNA-CPEHATCHNTLGSYYCTCNEGleFSGGG 189
Cdd:pfam12947   1 CSDNNGgCHPNATCTNTGGSFTCTCNDG--YTGDG 33
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
155-182 4.34e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 38.61  E-value: 4.34e-04
                          10        20
                  ....*....|....*....|....*...
gi 1958802101 155 ECVTRNACPEHATCHNTLGSYYCTCNEG 182
Cdd:cd00053     1 ECAASNPCSNGGTCVNTPGSYRCVCPPG 28
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
298-331 4.90e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.39  E-value: 4.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958802101 298 DIDECTQDPfRCGRNSSCTNVPGSYNCSCLPDFR 331
Cdd:cd00054     1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGYT 33
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
205-234 6.28e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 37.96  E-value: 6.28e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958802101 205 CSRNSTLCGPSFICINTLGSYSCSCPAGFS 234
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYT 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
12-42 6.98e-04

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 38.00  E-value: 6.98e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958802101  12 VNECQDTTTCPAYATCTDTTESYYCTCKQGF 42
Cdd:cd00054     2 IDECASGNPCQNGGTCVNTVGSYRCSCPPGY 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
12-42 1.25e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.23  E-value: 1.25e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958802101   12 VNECQDTTTCPAYATCTDTTESYYCTCKQGF 42
Cdd:smart00179   2 IDECASGNPCQNGGTCVNTVGSYRCECPPGY 32
DUF2975 pfam11188
Protein of unknown function (DUF2975); This family of bacterial proteins have no known ...
699-803 1.30e-03

Protein of unknown function (DUF2975); This family of bacterial proteins have no known function. These proteins are likely to be integral membrane proteins. The proteins contain a highly conserved glutamic acid close to their C-terminus.


Pssm-ID: 463239  Cd Length: 130  Bit Score: 39.91  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958802101 699 YLFLACFFWMLVEAVMLFLMVRNLKVvnyFSSRNIKML----HLCAFGYGLPVVVVIISATVHPWGYGMHnrcwlntetg 774
Cdd:pfam11188  25 YLAAIPFQVALVQLWRLLRSIRKDRA---FSEANVRRLrvigYAAVAIAVLYVAGGVFLYFLAAVLAPGI---------- 91
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958802101 775 FIWSFLGPVCMIItinSALLAWTL-WVLRQ 803
Cdd:pfam11188  92 LLLLLGVIFASLV---IGLLVLVLrELLAQ 118
EGF_CA smart00179
Calcium-binding EGF-like domain;
60-88 1.65e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 1.65e-03
                           10        20
                   ....*....|....*....|....*....
gi 1958802101   60 DVNECLrSDSPCGSNSVCTNIPGRARCSC 88
Cdd:smart00179   1 DIDECA-SGNPCQNGGTCVNTVGSYRCEC 28
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
204-237 1.76e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 36.69  E-value: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958802101 204 ECSRNSTlCGPSFICINTLGSYSCSCPAGFSLST 237
Cdd:cd00053     1 ECAASNP-CSNGGTCVNTPGSYRCVCPPGYTGDR 33
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
115-151 4.18e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 35.53  E-value: 4.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958802101 115 ECLTIGICPKNSNCSNSVGSYSCTCQSGFVSNGsTCE 151
Cdd:cd00053     1 ECAASNPCSNGGTCVNTPGSYRCVCPPGYTGDR-SCE 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
60-88 4.19e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.69  E-value: 4.19e-03
                          10        20
                  ....*....|....*....|....*....
gi 1958802101  60 DVNECLrSDSPCGSNSVCTNIPGRARCSC 88
Cdd:cd00054     1 DIDECA-SGNPCQNGGTCVNTVGSYRCSC 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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