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Conserved domains on  [gi|1034560524|ref|XP_016857394|]
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adhesion G protein-coupled receptor B2 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
929-1186 7.98e-165

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.


The actual alignment was detected with superfamily member cd15988:

Pssm-ID: 475119 [Multi-domain]  Cd Length: 291  Bit Score: 498.33  E-value: 7.98e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  929 AGSPSVPLVIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFL 1008
Cdd:cd15988      1 TGSPSVPLMIGCAVSCMALLILLAIYAAFWRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1009 SSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIV 1088
Cdd:cd15988     81 SSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTASYCWLSLEGGLLYAFVGPAAVIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1089 LVNMLIGIIVFNKLMARDGISDKSKKQRAG---------------------------------ASLWSSCVVLPLLALTW 1135
Cdd:cd15988    161 LVNMLIGIIVFNKLMSRDGISDKSKKQRAGseaepcsslllkcskcgvvssaamssatassamASLWSSCVVLPLLALTW 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560524 1136 MSAVLAMTDRRSVLFQALFAVFNSAQGFVITAVHCFLRREVQDVVKCQMGV 1186
Cdd:cd15988    241 MSAVLAMTDRRSILFQVLFAVFNSVQGFVIITVHCFLRREVQDVVKCQMGG 291
AGRB_N pfam19188
Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion ...
38-230 4.24e-82

Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion G-protein coupled receptor B proteins. This region contains 10 cysteine residues that probably form disulphide bonds.


:

Pssm-ID: 465991  Cd Length: 177  Bit Score: 267.04  E-value: 4.24e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524   38 SACSALASGVLYGAFSLQDLFPTIASGCSWTLENPDPTKYSLYLRFNRQEQVCAHFAPRLLPLDHYLVNFTclrpspeea 117
Cdd:pfam19188    1 DPCSTLVQGVLYGSFSLRDLFPTNASGCSWTLENPDPTKYTLYLKFTKPTQSCLPFSPRLLQFDHYLENTT--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  118 vaqaESEVGRPEEEEAeaaagLELCSGSGPFTFLHFDKNFVQLCLSAEPSEAPRLLAPAALAFRFVEVLLINNNNSSQFT 197
Cdd:pfam19188   72 ----RTYLGRESFDEV-----VELCDASSPFSFLEFDKNFVQLCLLAEPRGDPESVVPGPSGDFKVEVLVINNENPSQFT 142
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034560524  198 CGVLCRWSEECGRAA--GRACGFAQPGCSCPGEAG 230
Cdd:pfam19188  143 CGVLCRWLEECLSAStsSRPCGIMQTPCICPGTVP 177
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
614-769 2.11e-36

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


:

Pssm-ID: 465137  Cd Length: 205  Bit Score: 137.01  E-value: 2.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  614 GMSQVVRSLQELLARRTYYSGDLLFSVDILRNVTDTFKRATYVPSADDVQRFFQVVSFMVDAENKEKWDDAQQVSPGSVH 693
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLLATQDATLSNAFLENFVQTVSNLLDPENRESWEDLQQTERGTAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  694 --LLRVVEDFIHLVGDALKAFQSSLIVTDNLVISIQRE--PVSAVSSDITFPMRGRRGmkdwvrHSEDRLFLPKEVLSLS 769
Cdd:pfam16489   81 tkLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLdtHNFKGARFPRFPMKGERP------KDEDSVKLPPKAFKPP 154
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
367-417 3.73e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.08  E-value: 3.73e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   367 WEEWGSWSLCSRSCGRGSRSRMRTCV--PPQHGGKACEGPELQTKLCSMAACP 417
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspPPQNGGGPCTGEDVETRACNEQPCP 53
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
870-923 1.38e-14

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: 69.34  E-value: 1.38e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1034560524   870 TDPHCASWDYSRadassGDWDTENCQTLETQAAHTRCQCQHLSTFAVLAQPPKD 923
Cdd:smart00303    1 FNPICVFWDESS-----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
314-362 2.72e-12

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.99  E-value: 2.72e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034560524   314 EWSPWSVCSLTCGQGLQVRTRSCVSSPY---GTLCSGPLRETRPCNNSAtCP 362
Cdd:smart00209    3 EWSEWSPCSVTCGGGVQTRTRSCCSPPPqngGGPCTGEDVETRACNEQP-CP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
478-528 1.98e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 60.29  E-value: 1.98e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   478 WGPWNAWSLCSKTCDTGWQRRFRMC--QATGTQGYPCEGTGEEVKPCSEKRCP 528
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
422-472 2.98e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 59.91  E-value: 2.98e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   422 WLEWGPWGPCSTSCANGTQQRSRKCSVAGPAW--ATCTGALTDTRECSNLECP 472
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNggGPCTGEDVETRACNEQPCP 53
HormR smart00008
Domain present in hormone receptors;
531-595 8.44e-09

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 53.67  E-value: 8.44e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034560524   531 HEMCRDEYVMLMTWKKAAAGEIIYNKCPPNASG-----SASRRCLLSAQgvayWGL--PSFARCISHEYRYL 595
Cdd:smart00008    2 DLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCTENGG----WSPpfPNYSNCTSNDYEEL 69
 
Name Accession Description Interval E-value
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
929-1186 7.98e-165

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: 498.33  E-value: 7.98e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  929 AGSPSVPLVIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFL 1008
Cdd:cd15988      1 TGSPSVPLMIGCAVSCMALLILLAIYAAFWRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1009 SSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIV 1088
Cdd:cd15988     81 SSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTASYCWLSLEGGLLYAFVGPAAVIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1089 LVNMLIGIIVFNKLMARDGISDKSKKQRAG---------------------------------ASLWSSCVVLPLLALTW 1135
Cdd:cd15988    161 LVNMLIGIIVFNKLMSRDGISDKSKKQRAGseaepcsslllkcskcgvvssaamssatassamASLWSSCVVLPLLALTW 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560524 1136 MSAVLAMTDRRSVLFQALFAVFNSAQGFVITAVHCFLRREVQDVVKCQMGV 1186
Cdd:cd15988    241 MSAVLAMTDRRSILFQVLFAVFNSVQGFVIITVHCFLRREVQDVVKCQMGG 291
AGRB_N pfam19188
Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion ...
38-230 4.24e-82

Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion G-protein coupled receptor B proteins. This region contains 10 cysteine residues that probably form disulphide bonds.


Pssm-ID: 465991  Cd Length: 177  Bit Score: 267.04  E-value: 4.24e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524   38 SACSALASGVLYGAFSLQDLFPTIASGCSWTLENPDPTKYSLYLRFNRQEQVCAHFAPRLLPLDHYLVNFTclrpspeea 117
Cdd:pfam19188    1 DPCSTLVQGVLYGSFSLRDLFPTNASGCSWTLENPDPTKYTLYLKFTKPTQSCLPFSPRLLQFDHYLENTT--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  118 vaqaESEVGRPEEEEAeaaagLELCSGSGPFTFLHFDKNFVQLCLSAEPSEAPRLLAPAALAFRFVEVLLINNNNSSQFT 197
Cdd:pfam19188   72 ----RTYLGRESFDEV-----VELCDASSPFSFLEFDKNFVQLCLLAEPRGDPESVVPGPSGDFKVEVLVINNENPSQFT 142
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034560524  198 CGVLCRWSEECGRAA--GRACGFAQPGCSCPGEAG 230
Cdd:pfam19188  143 CGVLCRWLEECLSAStsSRPCGIMQTPCICPGTVP 177
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
929-1165 6.27e-74

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: 246.42  E-value: 6.27e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  929 AGSPSVPLVIGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKG--------VCTMTA 1000
Cdd:pfam00002    1 ALSLKVIYTVGYSLSLVALLLAIAIFLLF-RKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKQdldhcswvGCKVVA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1001 AFLHFFFLSSFCWVLTEAWQSYLA-VIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYA 1079
Cdd:pfam00002   80 VFLHYFFLANFFWMLVEGLYLYTLlVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVD-PKGYGEDDGCWLSNENGLWWI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1080 FVGPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLW--SSCVVLPLLALTWMSAVLAMTDRR--SVLFQALFA 1155
Cdd:pfam00002  159 IRGPILLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLakSTLLLLPLLGITWVFGLFAFNPENtlRVVFLYLFL 238
                          250
                   ....*....|
gi 1034560524 1156 VFNSAQGFVI 1165
Cdd:pfam00002  239 ILNSFQGFFV 248
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
614-769 2.11e-36

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


Pssm-ID: 465137  Cd Length: 205  Bit Score: 137.01  E-value: 2.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  614 GMSQVVRSLQELLARRTYYSGDLLFSVDILRNVTDTFKRATYVPSADDVQRFFQVVSFMVDAENKEKWDDAQQVSPGSVH 693
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLLATQDATLSNAFLENFVQTVSNLLDPENRESWEDLQQTERGTAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  694 --LLRVVEDFIHLVGDALKAFQSSLIVTDNLVISIQRE--PVSAVSSDITFPMRGRRGmkdwvrHSEDRLFLPKEVLSLS 769
Cdd:pfam16489   81 tkLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLdtHNFKGARFPRFPMKGERP------KDEDSVKLPPKAFKPP 154
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
367-417 3.73e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.08  E-value: 3.73e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   367 WEEWGSWSLCSRSCGRGSRSRMRTCV--PPQHGGKACEGPELQTKLCSMAACP 417
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspPPQNGGGPCTGEDVETRACNEQPCP 53
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
870-923 1.38e-14

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: 69.34  E-value: 1.38e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1034560524   870 TDPHCASWDYSRadassGDWDTENCQTLETQAAHTRCQCQHLSTFAVLAQPPKD 923
Cdd:smart00303    1 FNPICVFWDESS-----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
872-917 2.11e-13

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: 65.79  E-value: 2.11e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034560524  872 PHCASWDYSraDASSGDWDTENCQTLETQAAHTRCQCQHLSTFAVL 917
Cdd:pfam01825    1 PQCVFWDFT--NSTTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
314-362 2.72e-12

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.99  E-value: 2.72e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034560524   314 EWSPWSVCSLTCGQGLQVRTRSCVSSPY---GTLCSGPLRETRPCNNSAtCP 362
Cdd:smart00209    3 EWSEWSPCSVTCGGGVQTRTRSCCSPPPqngGGPCTGEDVETRACNEQP-CP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
369-416 9.61e-12

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 61.14  E-value: 9.61e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034560524  369 EWGSWSLCSRSCGRGSRSRMRT-CVPPQHGGKACeGPELQTKLCSMAAC 416
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRTvIVEPQNGGRPC-PELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
478-528 1.98e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 60.29  E-value: 1.98e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   478 WGPWNAWSLCSKTCDTGWQRRFRMC--QATGTQGYPCEGTGEEVKPCSEKRCP 528
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
422-472 2.98e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 59.91  E-value: 2.98e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   422 WLEWGPWGPCSTSCANGTQQRSRKCSVAGPAW--ATCTGALTDTRECSNLECP 472
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNggGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
314-356 4.89e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 58.97  E-value: 4.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034560524  314 EWSPWSVCSLTCGQGLQVRTRSCVS-SPYGTLCSGPLRETRPCN 356
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSpFPGGEPCTGDDIETQACK 45
TSP_1 pfam00090
Thrombospondin type 1 domain;
424-471 3.28e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 3.28e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034560524  424 EWGPWGPCSTSCANGTQQRSRKCSVAGPAWATCTGALTDTRECSNLEC 471
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
HormR smart00008
Domain present in hormone receptors;
531-595 8.44e-09

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 53.67  E-value: 8.44e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034560524   531 HEMCRDEYVMLMTWKKAAAGEIIYNKCPPNASG-----SASRRCLLSAQgvayWGL--PSFARCISHEYRYL 595
Cdd:smart00008    2 DLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCTENGG----WSPpfPNYSNCTSNDYEEL 69
TSP_1 pfam00090
Thrombospondin type 1 domain;
479-527 1.41e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.04  E-value: 1.41e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034560524  479 GPWNAWSLCSKTCDTGWQRRFRMCQATGTQGYPCEGTGEEVKPCSEKRC 527
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
314-355 6.22e-05

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 46.86  E-value: 6.22e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034560524  314 EWSPWSVCSLTCGQ--GLQVRTRSCVsSPYGTLCSGPLRETRPC 355
Cdd:PTZ00087   235 EWGEWSNCSMECDHpdNVQIRERKCA-HPSGDCFKGDLKETRPC 277
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
359-419 1.16e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.88  E-value: 1.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034560524  359 ATCpvhGVWEEWgswSLCSRSCGRGSRSRMRtcvPPQHGGkaCEgPELQTKlCSMAACPVE 419
Cdd:PTZ00441   238 ASC---GPWDEW---TPCSVTCGKGTHSRSR---PILHEG--CT-THMVEE-CEEEECPVE 285
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
425-472 3.96e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.95  E-value: 3.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034560524  425 WGPWGPCSTSCANGTQQRSRKCSVAGpawatCTGALtdTRECSNLECP 472
Cdd:PTZ00441   243 WDEWTPCSVTCGKGTHSRSRPILHEG-----CTTHM--VEECEEEECP 283
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
531-590 1.66e-03

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 38.51  E-value: 1.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034560524  531 HEMCRDEYVMLMTWKKAAAGEIIYNKCPPNAS-----GSASRRCLLSAQgvayWGLPS---FARCISH 590
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSgfdprGNASRNCTEDGT----WSEHPpsnYSNCTSN 64
 
Name Accession Description Interval E-value
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
929-1186 7.98e-165

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: 498.33  E-value: 7.98e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  929 AGSPSVPLVIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFL 1008
Cdd:cd15988      1 TGSPSVPLMIGCAVSCMALLILLAIYAAFWRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGVCTMTAAFLHFFFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1009 SSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIV 1088
Cdd:cd15988     81 SSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTASYCWLSLEGGLLYAFVGPAAVIV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1089 LVNMLIGIIVFNKLMARDGISDKSKKQRAG---------------------------------ASLWSSCVVLPLLALTW 1135
Cdd:cd15988    161 LVNMLIGIIVFNKLMSRDGISDKSKKQRAGseaepcsslllkcskcgvvssaamssatassamASLWSSCVVLPLLALTW 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560524 1136 MSAVLAMTDRRSVLFQALFAVFNSAQGFVITAVHCFLRREVQDVVKCQMGV 1186
Cdd:cd15988    241 MSAVLAMTDRRSILFQVLFAVFNSVQGFVIITVHCFLRREVQDVVKCQMGG 291
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
929-1186 6.51e-159

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: 480.98  E-value: 6.51e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  929 AGSPSVPLVIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFL 1008
Cdd:cd15251      1 AGSPSVTLIVGCGVSCLALLTLLAIYAAFWRYIRSERSIILINFCLSIISSNILILVGQTQTLNKGVCTMTAAFLHFFFL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1009 SSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIV 1088
Cdd:cd15251     81 SSFCWVLTEAWQSYMAVTGRMRTRLIRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAAVV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1089 LVNMLIGIIVFNKLMARDGISDkskkqRAGASLWSSCVVLPLLALTWMSAVLAMTDRRSVLFQALFAVFNSAQGFVITAV 1168
Cdd:cd15251    161 LVNMVIGILVFNKLVSRDGISD-----NAMASLWSSCVVLPLLALTWMSAVLAMTDRRSVLFQILFAVFDSLQGFVIVMV 235
                          250
                   ....*....|....*...
gi 1034560524 1169 HCFLRREVQDVVKCQMGV 1186
Cdd:cd15251    236 HCILRREVQDAVKCRMGV 253
7tmB2_BAI1 cd15990
brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 ...
926-1191 4.32e-117

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: 368.93  E-value: 4.32e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  926 LELAGSPSVPLVIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHF 1005
Cdd:cd15990      1 MEKALLPSVTLIVGCGVSSLTLLLLIIIYVSVWRYIRSERSVILINFCLSIISSNALILIGQTQTRNKVVCTLVAAFLHF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1006 FFLSSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAA 1085
Cdd:cd15990     81 FFLSSFCWVLTEAWQSYMAVTGRLRNRIIRKRFLCLGWGLPALVVAISVGFTKAKGYGTVNYCWLSLEGGLLYAFVGPAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1086 VIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDRRSVLFQALFAVFNSAQGFVI 1165
Cdd:cd15990    161 AVVLVNMVIGILVFNKLVSKDGITDKKLKERAGASLWSSCVVLPLLALTWMSAVLAITDRRSALFQILFAVFDSLEGFVI 240
                          250       260
                   ....*....|....*....|....*.
gi 1034560524 1166 TAVHCFLRREVQDVVKCQMgVCRADE 1191
Cdd:cd15990    241 VMVHCILRREVQDAVKCRV-VDRQEE 265
7tmB2_BAI3 cd15989
brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 ...
927-1184 1.69e-115

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: 365.55  E-value: 1.69e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  927 ELAGSPSVPLVIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFF 1006
Cdd:cd15989      1 ESSGTPSVTLIVGCGLSCLALITLAVVYAALWRYIRSERSIILINFCLSIISSNILILVGQTQTHNKGICTMTTAFLHFF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1007 FLSSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAV 1086
Cdd:cd15989     81 FLASFCWVLTEAWQSYMAVTGKIRTRLIRKRFLCLGWGLPALVVAISMGFTKAKGYGTPHYCWLSLEGGLLYAFVGPAAA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1087 IVLVNMLIGIIVFNKLMARDGISDKSKKQRAG---------------------------------ASLWSSCVVLPLLAL 1133
Cdd:cd15989    161 VVLVNMVIGILVFNKLVSRDGILDKKLKHRAGqmsephsgltlkcakcgvvsttalsattasnamASLWSSCVVLPLLAL 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560524 1134 TWMSAVLAMTDRRSVLFQALFAVFNSAQGFVITAVHCFLRREVQDVVKCQM 1184
Cdd:cd15989    241 TWMSAVLAMTDKRSILFQILFAVFDSLQGFVIVMVHCILRREVQDAFRCRL 291
AGRB_N pfam19188
Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion ...
38-230 4.24e-82

Adhesion GPCR B N-terminal region; This region is found at the N-terminus of various adhesion G-protein coupled receptor B proteins. This region contains 10 cysteine residues that probably form disulphide bonds.


Pssm-ID: 465991  Cd Length: 177  Bit Score: 267.04  E-value: 4.24e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524   38 SACSALASGVLYGAFSLQDLFPTIASGCSWTLENPDPTKYSLYLRFNRQEQVCAHFAPRLLPLDHYLVNFTclrpspeea 117
Cdd:pfam19188    1 DPCSTLVQGVLYGSFSLRDLFPTNASGCSWTLENPDPTKYTLYLKFTKPTQSCLPFSPRLLQFDHYLENTT--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  118 vaqaESEVGRPEEEEAeaaagLELCSGSGPFTFLHFDKNFVQLCLSAEPSEAPRLLAPAALAFRFVEVLLINNNNSSQFT 197
Cdd:pfam19188   72 ----RTYLGRESFDEV-----VELCDASSPFSFLEFDKNFVQLCLLAEPRGDPESVVPGPSGDFKVEVLVINNENPSQFT 142
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034560524  198 CGVLCRWSEECGRAA--GRACGFAQPGCSCPGEAG 230
Cdd:pfam19188  143 CGVLCRWLEECLSAStsSRPCGIMQTPCICPGTVP 177
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
929-1165 6.27e-74

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: 246.42  E-value: 6.27e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  929 AGSPSVPLVIGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKG--------VCTMTA 1000
Cdd:pfam00002    1 ALSLKVIYTVGYSLSLVALLLAIAIFLLF-RKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKQdldhcswvGCKVVA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1001 AFLHFFFLSSFCWVLTEAWQSYLA-VIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYA 1079
Cdd:pfam00002   80 VFLHYFFLANFFWMLVEGLYLYTLlVEVFFSERKYFWWYLLIGWGVPALVVGIWAGVD-PKGYGEDDGCWLSNENGLWWI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1080 FVGPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLW--SSCVVLPLLALTWMSAVLAMTDRR--SVLFQALFA 1155
Cdd:pfam00002  159 IRGPILLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLakSTLLLLPLLGITWVFGLFAFNPENtlRVVFLYLFL 238
                          250
                   ....*....|
gi 1034560524 1156 VFNSAQGFVI 1165
Cdd:pfam00002  239 ILNSFQGFFV 248
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
938-1178 2.45e-72

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: 242.09  E-value: 2.45e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd15040     10 IGCGLSLLGLLLTIITYILFRKLRKRKPTKILLNLCLALLLANLLFLFGINSTDNPVLCTAVAALLHYFLLASFMWMLVE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 AWQSYLAVIGRMRT--RLVRKRFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIG 1095
Cdd:cd15040     90 ALLLYLRLVKVFGTypRHFILKYALIGWGLPLIIVIITLAVDPDSYGNSSGYCWLSNGNGLYYAFLGPVLLIILVNLVIF 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1096 IIVFNKLMARDGISDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDRRSVlFQALFAVFNSAQGFVITAVHCFLRRE 1175
Cdd:cd15040    170 VLVLRKLLRLSAKRNKKKRKKTKAQLRAAVSLFFLLGLTWIFGILAIFGARVV-FQYLFAIFNSLQGFFIFIFHCLRNKE 248

                   ...
gi 1034560524 1176 VQD 1178
Cdd:cd15040    249 VRK 251
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
938-1178 2.39e-50

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: 179.06  E-value: 2.39e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAaFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd15933     10 IGCGISIACLALTLIIFL-VLRVLSSDRFQIHKNLCVALLLAQILLLAGEWAEGNKVACKVVAILLHFFFMAAFSWMLVE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 AWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFtRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGII 1097
Cdd:cd15933     89 GLHLYLMIVKVFNYKSKMRYYYFIGWGLPAIIVAISLAI-LFDDYGSPNVCWLSLDDGLIWAFVGPVIFIITVNTVILIL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1098 V---FNKLMARDGISDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDrRSVLFQALFAVFNSAQGFVITAVHCFLRR 1174
Cdd:cd15933    168 VvkiTVSLSTNDAKKSQGTLAQIKSTAKASVVLLPILGLTWLFGVLVVNS-QTIVFQYIFVILNSLQGLMIFLFHCVLNS 246

                   ....
gi 1034560524 1175 EVQD 1178
Cdd:cd15933    247 EVRS 250
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
937-1177 4.48e-50

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: 178.56  E-value: 4.48e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  937 VIGCAVSCMALLTLLAIYAAFWRFIKSeRSIILLNFCLSILASNILILVGQSRVLSKG--VCTMTAAFLHFFFLSSFCWV 1014
Cdd:cd13952      9 YIGCSLSLVGLLLTIITYLLFPKLRNL-RGKILINLCLSLLLAQLLFLIGQLLTSSDRpvLCKALAILLHYFLLASFFWM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1015 LTEAWQSYLAVIGRMRTRLvRKRFL---CLGWGLPALVVAVSVGFTRT----KGYGTSSYCWLSLEGGLLYAFVGPAAVI 1087
Cdd:cd13952     88 LVEAFDLYRTFVKVFGSSE-RRRFLkysLYGWGLPLLIVIITAIVDFSlygpSPGYGGEYCWLSNGNALLWAFYGPVLLI 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1088 VLVNMLIGIIVFNKLMARDGISDK-SKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDRRSVLFQALFAVFNSAQGFVIT 1166
Cdd:cd13952    167 LLVNLVFFILTVRILLRKLRETPKqSERKSDRKQLRAYLKLFPLMGLTWIFGILAPFVGGSLVFWYLFDILNSLQGFFIF 246
                          250
                   ....*....|.
gi 1034560524 1167 AVHCFLRREVQ 1177
Cdd:cd13952    247 LIFCLKNKEVR 257
7tmB2_latrophilin-like_invertebrate cd15440
invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane ...
938-1177 3.40e-37

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: 141.25  E-value: 3.40e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd15440     10 IGCIISIVCLLLAFITFTCF-RNLQCDRNTIHKNLCLCLLIAEIVFLLGIDQTENRTLCGVIAGLLHYFFLAAFSWMLLE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 AWQSYL---AVIGRMRTRlvRKRFLCLGWGLPALVVAVSVGFTRTkGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVN-ML 1093
Cdd:cd15440     89 GFQLYVmlvEVFEPEKSR--IKWYYLFGYGLPALIVAVSAGVDPT-GYGTEDHCWLSTENGFIWSFVGPVIVVLLANlVF 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1094 IGIIVFnkLMARDGISDKSKKQRAG---ASLW--SSCVVLPLLALTWMSAVLAMtDRRSVLFQALFAVFNSAQGFVITAV 1168
Cdd:cd15440    166 LGMAIY--VMCRHSSRSASKKDASKlknIRGWlkGSIVLVVLLGLTWTFGLLFI-NQESIVMAYIFTILNSLQGLFIFIF 242

                   ....*....
gi 1034560524 1169 HCFLRREVQ 1177
Cdd:cd15440    243 HCVLNEKVR 251
GAIN pfam16489
GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and ...
614-769 2.11e-36

GPCR-Autoproteolysis INducing (GAIN) domain; The GAIN a domain of alpha-helices and beta-strands that is found in cell-adhesion GPCRs and precedes the GPS motif where the autoproteolysis occurs, family, pfam01825. The full GAIN domain, comprises the GPS and the GAIN, in cell-adhesion GPCRs, and is the functional unit for autoproteolysis. The GPS motif at the end of the GAIN domain is an ancient domain that exists in primitive ancestor organizms, and the full GAIN + GPS is conserved in all cell-adhesion GPCRs and all PKD1-related proteins.


Pssm-ID: 465137  Cd Length: 205  Bit Score: 137.01  E-value: 2.11e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  614 GMSQVVRSLQELLARRTYYSGDLLFSVDILRNVTDTFKRATYVPSADDVQRFFQVVSFMVDAENKEKWDDAQQVSPGSVH 693
Cdd:pfam16489    1 GAKELARELRNATRHGPLYGGDVLTAVELLSQLFDLLATQDATLSNAFLENFVQTVSNLLDPENRESWEDLQQTERGTAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  694 --LLRVVEDFIHLVGDALKAFQSSLIVTDNLVISIQRE--PVSAVSSDITFPMRGRRGmkdwvrHSEDRLFLPKEVLSLS 769
Cdd:pfam16489   81 tkLLRTLEEYALLLAQNMKYLTPFTIVTPNIVLSVDRLdtHNFKGARFPRFPMKGERP------KDEDSVKLPPKAFKPP 154
7tmB2_CD97 cd15438
CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
938-1188 2.33e-35

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: 136.05  E-value: 2.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLtLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd15438     10 VGLSVSLFCLF-LCILTFLFCRSIRGTRNTIHLHLCLSLFLAHLIFLLGINNTNNQVACAVVAGLLHYFFLAAFCWMSLE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 AWQSYLAVIGRMRTRLVRKRFLCL-GWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGI 1096
Cdd:cd15438     89 GVELYLMVVQVFNTQSLKKRYLLLiGYGVPLVIVAISAAVN-SKGYGTQRHCWLSLERGFLWSFLGPVCLIILVNAIIFV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1097 IVFNKLMAR-DGISDKSKKQRAGASLWSSCVV-LPLLALTWMSAVLAMTDrRSVLFQALFAVFNSAQGFVITAVHCFLRR 1174
Cdd:cd15438    168 ITVWKLAEKfSSINPDMEKLRKIRALTITAIAqLCILGCTWIFGFFQFSD-STLVMSYLFTILNSLQGLFIFLLHCLLSK 246
                          250
                   ....*....|....*
gi 1034560524 1175 EV-QDVVKCQMGVCR 1188
Cdd:cd15438    247 QVrEEYSRWLCAIAR 261
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
938-1176 1.23e-34

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: 133.92  E-value: 1.23e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd15441     10 IGIGISLVLLVIAFLVLSCL-RGLQSNSNSIHKNLVACLLLAELLFLLGINQTENLFPCKLIAILLHYFYLSAFSWLLVE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 AWQSYlavigRMRT--RLVRK---RF-LCLGWGLPALVVAVSVGFtRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVN 1091
Cdd:cd15441     89 SLHLY-----RMLTepRDINHghmRFyYLLGYGIPAIIVGLSVGL-RPDGYGNPDFCWLSVNETLIWSFAGPIAFVIVIT 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1092 MLIGIIVFNKLMARDGISDKSKKQRAGasLWSSCVVLPLLALTWMSAVLAMTDrRSVLFQALFAVFNSAQGFVITAVHCF 1171
Cdd:cd15441    163 LIIFILALRASCTLKRHVLEKASVRTD--LRSSFLLLPLLGATWVFGLLAVNE-DSELLHYLFAGLNFLQGLFIFLFYCI 239

                   ....*
gi 1034560524 1172 LRREV 1176
Cdd:cd15441    240 FNKKV 244
7tmB2_Latrophilin_Adhesion_I cd15252
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of ...
938-1177 5.28e-34

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: 132.24  E-value: 5.28e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLtlLAIYA-AFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLT 1016
Cdd:cd15252     10 VGIIISLVCLA--ICIFTfWFFRGLQSDRTTIHKNLCISLFLAELVFLIGINTTTNKIFCSVIAGLLHYFFLAAFAWMFI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1017 EAWQSYLAVIGRMRTR-LVRKRFLCLGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNML-I 1094
Cdd:cd15252     88 EGIQLYLMLVEVFENEgSRHKNFYIFGYGSPAVIVGVSAALG-YRYYGTTKVCWLSTENYFIWSFIGPATLIILLNLIfL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1095 GIIVFnkLMARDGISDKSKKQRAG---ASLWSSCVVLPLLALTWMSAVLAMtDRRSVLFQALFAVFNSAQGFVITAVHCF 1171
Cdd:cd15252    167 GVAIY--KMFRHTAGLKPEVSCLEnirSWARGAIALLFLLGLTWIFGVLHI-NHASVVMAYLFTVSNSLQGMFIFLFHCV 243

                   ....*.
gi 1034560524 1172 LRREVQ 1177
Cdd:cd15252    244 LSRKVR 249
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
938-1178 4.78e-31

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: 123.61  E-value: 4.78e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVS--CM--ALLTLLaiyaaFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCW 1013
Cdd:cd15439     10 VGLIISllCLflAILTFL-----LCRSIRNTSTSLHLQLSLCLFLADLLFLVGIDRTDNKVLCSIIAGFLHYLFLACFAW 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1014 VLTEAWQSYLAV-----IGRMRTRLVRKRFLCL-GWGLPALVVAVSVGfTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVI 1087
Cdd:cd15439     85 MFLEAVHLFLTVrnlkvVNYFSSHRFKKRFMYPvGYGLPAVIVAISAA-VNPQGYGTPKHCWLSMEKGFIWSFLGPVCVI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1088 VLVNMLIGIIVF----NKLMARDgiSDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDRRSVLfQALFAVFNSAQGF 1163
Cdd:cd15439    164 IVINLVLFCLTLwilrEKLSSLN--AEVSTLKNTRLLTFKAIAQLFILGCTWILGLFQVGPVATVM-AYLFTITNSLQGV 240
                          250
                   ....*....|....*
gi 1034560524 1164 VITAVHCFLRREVQD 1178
Cdd:cd15439    241 FIFLVHCLLNRQVRE 255
7tmB2_GPR133 cd15256
orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G ...
938-1181 1.21e-30

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: 122.34  E-value: 1.21e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRF--IKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVL 1015
Cdd:cd15256     10 VGCSLSIFCLAITLVTFAVLSSVstIRNQRYHIHANLSFAVLVAQILLLISFRFEPGTLPCKIMAILLHFFFLSAFAWML 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1016 TEAWQSYLAVIGRMRTRLVRKRFLC-LGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNmlI 1094
Cdd:cd15256     90 VEGLHLYSMVIKVFGSEESKHFYYYgIGWGSPLLICIISLTSA-LDSYGESDNCWLSLENGAIWAFVAPALFVIVVN--I 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1095 GI-IVFNKLMARdgISDKSKKQRAGASLW-----SSCVVLPLLALTWMSAVLAMtDRRSVLFQALFAVFNSAQGFVITAV 1168
Cdd:cd15256    167 GIlIAVTRVISR--ISADNYKVHGDANAFkltakAVAVLLPILGSSWVFGVLAV-NTHALVFQYMFAIFNSLQGFFIFLF 243
                          250
                   ....*....|...
gi 1034560524 1169 HCFLRREVQDVVK 1181
Cdd:cd15256    244 HCLLNSEVRAAFK 256
7tmB2_GPR116-like_Adhesion_VI cd15932
orphan GPR116 and related proteins, group IV adhesion GPCRs, member of the class B2 family of ...
938-1181 2.33e-29

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: 118.95  E-value: 2.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRFIKSE-----RSIILLNFCLSILASNILILVG---QSRVLSKGVCTMTAAFLHFFFLS 1009
Cdd:cd15932     10 VGLGISILSLVLCLIIEALVWKSVTKNktsymRHVCLVNIALSLLIADIWFIIGaaiSTPPNPSPACTAATFFIHFFYLA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1010 SFCWVLTeawqsyLAVIGRMRTRLV-----RKRFL----CLGWGLPALVVAVSVGFTR-TKGYGTSSYCWLSL-EGGLLY 1078
Cdd:cd15932     90 LFFWMLT------LGLLLFYRLVLVfhdmsKSTMMaiafSLGYGCPLIIAIITVAATApQGGYTRKGVCWLNWdKTKALL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1079 AFVGPAAVIVLVNMLIGIIVFNKLMaRDGISDKSKKQRAGASLW-SSCVVL--PLLALTWMSAVLAMTDRRSVLFQALFA 1155
Cdd:cd15932    164 AFVIPALAIVVVNFIILIVVIFKLL-RPSVGERPSKDEKNALVQiGKSVAIltPLLGLTWGFGLGTMIDPKSLAFHIIFA 242
                          250       260
                   ....*....|....*....|....*.
gi 1034560524 1156 VFNSAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15932    243 ILNSFQGFFILVFGTLLDSKVREALL 268
7tmB2_Latrophilin cd15436
Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
938-1182 8.47e-29

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: 117.20  E-value: 8.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAaFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd15436     10 VGIVISLVCLLICIFTFC-FFRGLQTDRNTIHKNLCINLFIAELLFLIGINRTQYTIACPIFAGLLHFFFLAAFCWLCLE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 AWQSYLAVIGRMRTRLVRKRFLCL-GWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGI 1096
Cdd:cd15436     89 GVQLYLLLVEVFESEYSRRKYFYLcGYSFPALVVAVSAAID-YRSYGTEKACWLRVDNYFIWSFIGPVTFVITLNLVFLV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1097 IVFNKLMARDGISDKSKKQRAGASLWS--SCVVLPLLALTWMSAVLAMtDRRSVLFQALFAVFNSAQGFVITAVHCFLRR 1174
Cdd:cd15436    168 ITLHKMVSHSDLLKPDSSRLDNIKSWAlgAIALLFLLGLTWSFGLMFI-NEESVVMAYLFTIFNAFQGVFIFIFHCALQK 246

                   ....*....
gi 1034560524 1175 EVQ-DVVKC 1182
Cdd:cd15436    247 KVRkEYSKC 255
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
933-1182 2.68e-27

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: 112.71  E-value: 2.68e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  933 SVPLVIGCAVSCMALLTLLAIYAaFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFC 1012
Cdd:cd16007      5 SVITWVGIVISLVCLAICISTFC-FLRGLQTDRNTIHKNLCINLFLAELLFLIGIDKTQYQIACPIFAGLLHFFFLAAFS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 WVLTEAWQSYLAVIGRMRTRLVRKRFLCL-GWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVN 1091
Cdd:cd16007     84 WLCLEGVQLYLMLVEVFESEYSRKKYYYLcGYCFPALVVGISAAID-YRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1092 MLIGIIVFNKLMARDGISDKSKKQRAGASLWS--SCVVLPLLALTWMSAVLaMTDRRSVLFQALFAVFNSAQGFVITAVH 1169
Cdd:cd16007    163 LVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWAlgAITLLFLLGLTWAFGLL-FINKESVVMAYLFTTFNAFQGMFIFIFH 241
                          250
                   ....*....|....
gi 1034560524 1170 CFLRREV-QDVVKC 1182
Cdd:cd16007    242 CALQKKVhKEYSKC 255
7tmB2_EMR_Adhesion_II cd15931
EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of ...
934-1178 2.87e-27

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: 112.61  E-value: 2.87e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  934 VPLVIGCAVSCMALLTLLAIyaafwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCW 1013
Cdd:cd15931     10 VGVIVSLFCLGLAIFTFLLC-----RWIPKINTTAHLHLCLCLSMSHTLFLAGIEYVENELACTVMAGLLHYLFLASFVW 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1014 VLTEAWQSYLAV-----IGRMRTRLVRKRFLCL-GWGLPALVVAVSvGFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVI 1087
Cdd:cd15931     85 MLLEALQLHLLVrrltkVQVIQRDGLPRPLLCLiGYGVPFLIVGVS-ALVYSDGYGEAKMCWLSQERGFNWSFLGPVIAI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1088 VLVNMLIGIIVFNKLMAR--DGISDKSKKQRAGASLWSSCVVLPLLALTWMSAvLAMTDRRSVLFQALFAVFNSAQGFVI 1165
Cdd:cd15931    164 IGINWILFCATLWCLRQTlsNMNSDISQLKDTRLLTFKAVAQLFILGCTWVLG-LFQTNPVALVFQYLFTILNSLQGAFL 242
                          250
                   ....*....|...
gi 1034560524 1166 TAVHCFLRREVQD 1178
Cdd:cd15931    243 FLVHCLLNKEVRE 255
7tmB2_Latrophilin-3 cd16005
Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled ...
938-1177 8.46e-27

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: 111.19  E-value: 8.46e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAaFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd16005     10 VGILLSLVCLLICIFTFC-FFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 AWQSYLAVIGRMRTRLVRKR-FLCLGWGLPALVVAVSVGfTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNML-IG 1095
Cdd:cd16005     89 GVQLYIMLVEVFESEHSRRKyFYLVGYGMPALIVAVSAA-VDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIfLG 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1096 IIVFNK------LMARDGISDKSKKQRAGAslwssCVVLPLLALTWMSAVLAMTDrRSVLFQALFAVFNSAQGFVITAVH 1169
Cdd:cd16005    168 IALYKMfhhtaiLKPESGCLDNIKSWVIGA-----IALLCLLGLTWAFGLMYINE-STVIMAYLFTIFNSLQGMFIFIFH 241

                   ....*...
gi 1034560524 1170 CFLRREVQ 1177
Cdd:cd16005    242 CVLQKKVR 249
7tmB2_ETL cd15437
Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; ...
945-1178 1.08e-26

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: 111.12  E-value: 1.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  945 MALLTLLAIYAAFWRF--IKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTEAWQSY 1022
Cdd:cd15437     14 ISLICLSMCIFTFWFFseIQSTRTTIHKNLCCSLFLAELIFLIGINMNANKLFCSIIAGLLHYFFLAAFAWMCIEGIHLY 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1023 LAVIGRMRTR-LVRKRFLCLGWGLPALVVAVS--VGFtrtKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNML-IGIIV 1098
Cdd:cd15437     94 LIVVGVIYNKgFLHKNFYIFGYGSPAVVVGISaaLGY---KYYGTTKVCWLSTENNFIWSFIGPACLIILVNLLaFGVII 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1099 FNKLMARDGISDK-SKKQRAGASLWSSCVVLPLLALTWMSAVLAMTdRRSVLFQALFAVFNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15437    171 YKVFRHTAMLKPEvSCYENIRSCARGALALLFLLGATWIFGVLHVV-YGSVVTAYLFTISNAFQGMFIFIFLCVLSRKIQ 249

                   .
gi 1034560524 1178 D 1178
Cdd:cd15437    250 E 250
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
938-1182 1.29e-26

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: 110.78  E-value: 1.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAaFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd16006     10 VGIVISLVCLAICIFTFC-FFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTEYKIACPIFAGLLHFFFLAAFAWMCLE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 AWQSYLAVIGRMRTRLVRKRFLCL-GWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGI 1096
Cdd:cd16006     89 GVQLYLMLVEVFESEYSRKKYYYVaGYLFPATVVGVSAAID-YKSYGTEKACWLRVDNYFIWSFIGPVTFIILLNLIFLV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1097 IVFNKLMARDGISDKSKKQRAGASLWSS--CVVLPLLALTWMSAVLAMTDrRSVLFQALFAVFNSAQGFVITAVHCFLRR 1174
Cdd:cd16006    168 ITLCKMVKHSNTLKPDSSRLENIKSWVLgaFALLCLLGLTWSFGLLFINE-ETIVMAYLFTIFNAFQGMFIFIFHCALQK 246

                   ....*....
gi 1034560524 1175 EV-QDVVKC 1182
Cdd:cd16006    247 KVrKEYSKC 255
7tmB2_GPR113 cd15253
orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G ...
938-1178 5.17e-26

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: 109.46  E-value: 5.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRF-----IKSERSIILLNFCLSILASNILILvGQSRVLSKG---VCTMTAAFLHFFFLS 1009
Cdd:cd15253     10 VGLGASILALLLCLGIYRLVWRSvvrnkISYFRHMTLVNIAFSLLLADTCFL-GATFLSAGHespLCLAAAFLCHFFYLA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1010 SFCWVLTEA---WQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKG-YGTSSYCWLSLEGGLLYAFVGPAA 1085
Cdd:cd15253     89 TFFWMLVQAlmlFHQLLFVFHQLAKRSVLPLMVTLGYLCPLLIAAATVAYYYPKRqYLHEGACWLNGESGAIYAFSIPVL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1086 VIVLVNMLIGIIVFNKLMaRDGISD--KSKKQRAGASLWSSCVVL-PLLALTWMSAVLAMTDRRSVLFQALFAVFNSAQG 1162
Cdd:cd15253    169 AIVLVNLLVLFVVLMKLM-RPSVSEgpPPEERKALLSIFKALLVLtPVFGLTWGLGVATLTGESSQVSHYGFAILNAFQG 247
                          250
                   ....*....|....*.
gi 1034560524 1163 FVITAVHCFLRREVQD 1178
Cdd:cd15253    248 VFILLFGCLMDKKVRE 263
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
941-1181 1.40e-22

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: 98.77  E-value: 1.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  941 AVSCMALLtLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTEAWQ 1020
Cdd:cd15991     13 SLSLVALL-ITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGINQTENPFVCTVVAILLHYFYMSTFAWMFVEGLH 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1021 SYlavigRMRTRlVRK------RFL-CLGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNML 1093
Cdd:cd15991     92 IY-----RMLTE-VRNintghmRFYyVVGWGIPAIITGLAVGLD-PQGYGNPDFCWLSVQDTLIWSFAGPIGIVVIINTV 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1094 IGIIVFNKLMARDGISDksKKQRAGASLWSSCVVLPLLALTWMSAVLAMtDRRSVLFQALFAVFNSAQGFVITAVHCFLR 1173
Cdd:cd15991    165 IFVLAAKASCGRRQRYF--EKSGVISMLRTAFLLLLLISATWLLGLMAV-NSDTLSFHYLFAIFSCLQGIFIFFFHCIFN 241

                   ....*...
gi 1034560524 1174 REVQDVVK 1181
Cdd:cd15991    242 KEVRKHLK 249
7tmB2_GPR112 cd15997
Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane ...
938-1184 1.48e-22

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: 99.35  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQ--SRVLSKGVCTMTAAFLHFFFLSSFCWVL 1015
Cdd:cd15997     10 LGCGISSIFLGITLVTYLAFEKLRRDYPSKILINLCTALLMLNLVFLLNSwlSSFNNYGLCITVAAFLHYFLLASFTWMG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1016 TEAWQSYLAVIgRMRTRLVRK---RFLCLGWGLPALVVAVsVGFTRTKGYGTSS----------YCWLSLEGGLLYAFVG 1082
Cdd:cd15997     90 LEAVHMYFALV-KVFNIYIPNyilKFCIAGWGIPAVVVAL-VLAINKDFYGNELssdslhpstpFCWIQDDVVFYISVVA 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1083 PAAVIVLVNMLIGIIVFNKLMardgiSDKSKKQRAGAS------LWSSCVVLPLLALTWMSAVLAMTDRRsVLFQALFAV 1156
Cdd:cd15997    168 YFCLIFLCNISMFITVLIQIR-----SMKAKKPSRNWKqgflhdLKSVASLTFLLGLTWGFAFFAWGPVR-IFFLYLFSI 241
                          250       260
                   ....*....|....*....|....*...
gi 1034560524 1157 FNSAQGFVITAVHCFLRREVQDvvKCQM 1184
Cdd:cd15997    242 CNTLQGFFIFVFHCLMKENVRK--QWRI 267
7tmB2_GPR126-like_Adhesion_VIII cd15258
orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family ...
938-1177 1.19e-21

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: 96.33  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSK--GVCTMTAAFLHFFFLSSFCWVL 1015
Cdd:cd15258     10 VGCGISAIFLAITILTYIAFRKLRRDYPSKIHMNLCAALLLLNLAFLLSSWIASFGsdGLCIAVAVALHYFLLACLTWMG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1016 TEAWQSYLAViGRMRTRLVRKRFL---CLGWGLPALVVAVsVGFTRTKGYGTSSY-----------CWLSLEGGLLYAFV 1081
Cdd:cd15258     90 LEAFHLYLLL-VKVFNTYIRRYILklcLVGWGLPALLVTL-VLSVRSDNYGPITIpngegfqndsfCWIRDPVVFYITVV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1082 GPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDRRsVLFQALFAVFNSAQ 1161
Cdd:cd15258    168 GYFGLTFLFNMVMLATVLVQICRLREKAQATPRKRALHDLLTLLGLTFLLGLTWGLAFFAWGPFN-LPFLYLFAIFNSLQ 246
                          250
                   ....*....|....*.
gi 1034560524 1162 GFVITAVHCFLRREVQ 1177
Cdd:cd15258    247 GFFIFIWYCSMKENVR 262
7tmB2_GPR128 cd15257
orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G ...
938-1165 3.87e-21

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: 95.71  E-value: 3.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVScMALLTLLAIYAAFWRFIKSER-SIILLNFCLSILASNILILVGQSRV-------------------------L 991
Cdd:cd15257     10 IGCVLS-IAGLVITIIFHLHTRKLRKSSvTWVLLNLCSSLLLFNIIFTSGVENTnndyeistvpdretntvllseeyveP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  992 SKGVCTMTAAFLHFFFLSSFCWVLTEAWQSYLAVIgRMRTRLVRKRFL---CLGWGLPALVVAVSVGFT---------RT 1059
Cdd:cd15257     89 DTDVCTAVAALLHYFLLVTFMWNAVYSAQLYLLLI-RMMKPLPEMFILqasAIGWGIPAVVVAITLGATyrfptslpvFT 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1060 KGYGTSSYCWL-------SLEGGLLYAFVGPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLWSSCVVLPLLA 1132
Cdd:cd15257    168 RTYRQEEFCWLaaldknfDIKKPLLWGFLLPVGLILITNVILFIMTSQKVLKKNNKKLTTKKRSYMKKIYITVSVAVVFG 247
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1034560524 1133 LTWMSA--VLAMTDRRSVLFQALFAVFNSAQGFVI 1165
Cdd:cd15257    248 ITWILGylMLVNNDLSKLVFSYIFCITNTTQGVQI 282
7tmB2_CELSR2 cd15992
Cadherin EGF LAG seven-pass G-type receptor 2, member of the class B2 family of ...
945-1181 5.75e-21

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: 94.12  E-value: 5.75e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  945 MALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTEAWQSYLA 1024
Cdd:cd15992     16 LGFLLLTFLFLLCLRALRSNKTSIRKNGATALFLSELVFILGINQADNPFACTVIAILLHFFYLCTFSWLFLEGLHIYRM 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1025 V-------IGRMRTrlvrkrFLCLGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGII 1097
Cdd:cd15992     96 LsevrdinYGPMRF------YYLIGWGVPAFITGLAVGLD-PEGYGNPDFCWLSIYDTLIWSFAGPVAFAVSMNVFLYIL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1098 VFNKLMARDGISDKSKKQRAgASLWSSCVVLPLLALTWMSAVLAMtDRRSVLFQALFAVFNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15992    169 SSRASCSAQQQSFEKKKGPV-SGLRTAFTVLLLVSVTCLLALLSV-NSDVILFHYLFAGFNCLQGPFIFLSHVVLLKEVR 246

                   ....
gi 1034560524 1178 DVVK 1181
Cdd:cd15992    247 KALK 250
7tmB2_GPR64 cd15444
orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B ...
938-1177 1.12e-20

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: 93.74  E-value: 1.12e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSK---GVCTMTAAFLHFFFLSSFCWV 1014
Cdd:cd15444     10 IGCGLSAIFLSVTLVTYIAFEKIRRDYPSKILIQLCVALLLLNLVFLLDSWIALYKdivGLCISVAVFLHYFLLVSFTWM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1015 LTEAWQSYLAVIGRMRTrLVRK---RFLCLGWGLPALVVAVSVGFTRTKgYGTSSY-----------CWLSLEGGLLYAF 1080
Cdd:cd15444     90 GLEAFHMYLALVKVFNT-YIRKyilKFCIVGWGVPAVVVAIVLAVSKDN-YGLGSYgkspngstddfCWINNNIVFYITV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1081 VGPAAVIVLVNMLIGIIVF---------NKLMARDGISDKSKKQRAGASLwsscvvlpLLALTWMSAVLAMTDrRSVLFQ 1151
Cdd:cd15444    168 VGYFCVIFLLNISMFIVVLvqlcrikkqKQLGAQRKTSLQDLRSVAGITF--------LLGITWGFAFFAWGP-VNLAFM 238
                          250       260
                   ....*....|....*....|....*.
gi 1034560524 1152 ALFAVFNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15444    239 YLFAIFNTLQGFFIFIFYCVAKENVR 264
7tmB2_GPR126 cd15996
orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G ...
938-1177 1.24e-20

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: 93.80  E-value: 1.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQ--SRVLSKGVCTMTAAFLHFFFLSSFCWVL 1015
Cdd:cd15996     10 IGCGISAIFSAATLLTYIAFEKLRRDYPSKILMNLSTALLFLNLVFLLDGwiASFEIDELCITVAVLLHFFLLATFTWMG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1016 TEAWQSYLAVIGRMRTRLVRK--RFLCLGWGLPALVVAVSVGFTRT-----------KGYGTSSYCWLSLEGGLLYAFVG 1082
Cdd:cd15996     90 LEAIHMYIALVKVFNTYIRRYilKFCIIGWGLPALIVSIVLASTNDnygygyygkdkDGQGGDEFCWIKNPVVFYVTCAA 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1083 PAAVIVLVNMLIGIIVFNKLMARDGI-SDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDrRSVLFQALFAVFNSAQ 1161
Cdd:cd15996    170 YFGIMFLMNVAMFIVVMVQICGRNGKrSNRTLREEILRNLRSVVSLTFLLGMTWGFAFFAWGP-VNLAFMYLFTIFNSLQ 248
                          250
                   ....*....|....*.
gi 1034560524 1162 GFVITAVHCFLRREVQ 1177
Cdd:cd15996    249 GLFIFVFHCALKENVQ 264
7tmB2_GPR116_Ig-Hepta cd15254
The immunoglobulin-repeat-containing receptor Ig-hepta/GPR116, member of the class B2 family ...
938-1178 3.61e-20

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: 92.17  E-value: 3.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRFIKSERS-----IILLNFCLSILASNILILV-----GQSRVLSKGVCTMTAAFLHFFF 1007
Cdd:cd15254     10 IGLSISILSLAICIVIESLVWKSVTKNRTsymrhVCILNIAVSLLIADIWFIVvaaiqDQNYAVNGNVCVAATFFIHFFY 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1008 LSSFCWVLTEAWQSY--LAVIGRMRTRLVRKRF-LCLGWGLPALVVAVSVGFTRTK-GYGTSSYCWLSLEGG-LLYAFVG 1082
Cdd:cd15254     90 LCVFFWMLALGLMLFyrLVFILHDTSKTIQKAVaFCLGYGCPLIISVITIAVTLPRdSYTRKKVCWLNWEDSkALLAFVI 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1083 PAAVIVLVNMLIGIIVFNKLMaRDGISDKSKKQRAgASLW----SSCVVLPLLALTWMSAVLAMTDRRSVLFQALFAVFN 1158
Cdd:cd15254    170 PALIIVAVNSIITVVVIVKIL-RPSIGEKPSKQER-SSLFqiikSIGVLTPLLGLTWGFGLATVIKGSSIVFHILFTLLN 247
                          250       260
                   ....*....|....*....|
gi 1034560524 1159 SAQGFVITAVHCFLRREVQD 1178
Cdd:cd15254    248 AFQGLFILVFGTLWDKKVQE 267
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
945-1181 4.69e-20

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: 91.44  E-value: 4.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  945 MALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTEAWQSYla 1024
Cdd:cd15993     16 LAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLLGINRTENQFLCTVVAILLHYFFLSTFAWLFVQGLHIY-- 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1025 vigRMRT------RLVRKRFLCLGWGLPALVVAVSVGFTrTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGIIV 1098
Cdd:cd15993     94 ---RMQTearnvnFGAMRFYYAIGWGVPAIITGLAVGLD-PEGYGNPDFCWISIHDKLVWSFAGPIVVVIVMNGVMFLLV 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1099 FNklMARDGISDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDrrSVL-FQALFAVFNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15993    170 AR--MSCSPGQKETKKTSVLMTLRSSFLLLLLISATWLFGLLAVNN--SVLaFHYLHAILCCLQGLAVLLLFCVLNEEVQ 245

                   ....
gi 1034560524 1178 DVVK 1181
Cdd:cd15993    246 EAWK 249
7tmB2_GPR144 cd15255
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
938-1181 5.22e-19

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: 88.75  E-value: 5.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVLTE 1017
Cdd:cd15255     10 IGCGVSLCALIVTFILFLAV-GVPKSERTTVHKNLIFALAAAEFLLMFSEWAKGNQVACWAVTALLHLFFLAAFSWMLVE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1018 A---WQSYLAVigRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKgYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMli 1094
Cdd:cd15255     89 GlllWSKVVAV--NMSEDRRMKFYYVTGWGLPVVIVAVTLATSFNK-YVADQHCWLNVQTDIIWAFVGPVLFVLTVNT-- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1095 gIIVFNKLM---------ARDGISDKSKKQRAGASLWSSC----VVLPLLALTWMSAVLAmtdRRSVLFQALFAVFNSAQ 1161
Cdd:cd15255    164 -FVLFRVVMvtvssarrrAKMLTPSSDLEKQIGIQIWATAkpvlVLLPVLGLTWLCGVLV---HLSDVWAYVFITLNSFQ 239
                          250       260
                   ....*....|....*....|
gi 1034560524 1162 GFVITAVHCFLRREVQDVVK 1181
Cdd:cd15255    240 GLYIFLVYAIYNSEVRNAIQ 259
7tmB3_Methuselah-like cd15039
Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G ...
937-1174 1.51e-18

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: 87.28  E-value: 1.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  937 VIGCAVSCMALLTLLAIYAafwrFIKSERSI---ILLNFCLSILASNILILVGQ-SRVLSKGVCTMTAAFLHFFFLSSFC 1012
Cdd:cd15039      9 LIGLIISLVFLLLTLAVYA----LLPELRNLhgkCLMCLVLSLFVAYLLLLIGQlLSSGDSTLCVALGILLHFFFLAAFF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 WVLTEAWQSYLAVIGRMRTRL---VRKRFL---CLGWGLPALVVAVSVGFTRTK-------GYGTsSYCWLSLEGGLLYA 1079
Cdd:cd15039     85 WLNVMSFDIWRTFRGKRSSSSrskERKRFLrysLYAWGVPLLLVAVTIIVDFSPntdslrpGYGE-GSCWISNPWALLLY 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1080 FVGPAAVIVLVNMLIGIIVFNKLMAR----DGISDKSKKQRAGASLwssCVVLPLL-ALTWMSAVLA-MTDRRSVLFQaL 1153
Cdd:cd15039    164 FYGPVALLLLFNIILFILTAIRIRKVkketAKVQSRLRSDKQRFRL---YLKLFVImGVTWILEIISwFVGGSSVLWY-I 239
                          250       260
                   ....*....|....*....|.
gi 1034560524 1154 FAVFNSAQGFVITAVHCFLRR 1174
Cdd:cd15039    240 FDILNGLQGVFIFLIFVCKRR 260
7tmB1_CRF-R cd15264
corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane ...
937-1181 2.97e-18

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: 86.32  E-value: 2.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  937 VIGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSrVLSK-------GVCTMTAAFLHFFFLS 1009
Cdd:cd15264      9 YLGFSISLVALAVALIIFLYF-RSLRCLRNNIHCNLIVTFILRNVTWFIMQN-TLTEihhqsnqWVCRLIVTVYNYFQVT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1010 SFCWVLTEAWQSYLAVIGRMRTRLVRK-RFLCLGWGLPA-LVVAVSVGftrtKGYGTSSYCWLSLEGGLLYAFV--GPAA 1085
Cdd:cd15264     87 NFFWMFVEGLYLHTMIVWAYSADKIRFwYYIVIGWCIPCpFVLAWAIV----KLLYENEHCWLPKSENSYYDYIyqGPIL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1086 VIVLVNML----IGIIVFNKLMArdgiSDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDRRSVlfQALFAVFN--- 1158
Cdd:cd15264    163 LVLLINFIflfnIVWVLITKLRA----SNTLETIQYRKAVKATLVLLPLLGITYMLFFINPGDDKTS--RLVFIYFNtfl 236
                          250       260
                   ....*....|....*....|....
gi 1034560524 1159 -SAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15264    237 qSFQGLFVAVFYCFLNGEVRSAIR 260
7tmB2_GPR111_115 cd15994
orphan adhesion receptors GPR111 and GPR115, member of the class B2 family of ...
938-1181 5.06e-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: 85.66  E-value: 5.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFW-RFIKSE----RSIILLNFCLSILASNILILVG---QSRVLSKGVCTMTAAFLHFFFLS 1009
Cdd:cd15994     10 IGLGLSIFSLALCLTIEAVVWsHVTKTEitymRHVCIVNIATSLLIADVWFILAsivHNTALNYPLCVAATFFLHFFYLS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1010 SFCWVLTEAW---QSYLAVIGRM-RTRLVRKRFlCLGWGLPALVVAVSVGFTR-TKGYGTSSYCWLSL-EGGLLYAFVGP 1083
Cdd:cd15994     90 LFFWMLTKALlilYGILLVFFKItKSVFIATAF-SIGYGCPLVIAVLTVAITEpKKGYLRPEACWLNWdETKALLAFIIP 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1084 AAVIVLVNMLIGIIVFNKlMARDGISDkSKKQRAGASLWSS---CVVLPLLALTWMSAVLAMTDRRSVLFQALFAVFNSA 1160
Cdd:cd15994    169 ALSIVVVNLIVVGVVVVK-TQRSSIGE-SCKQDVSNIIRISknvAILTPLLGLTWGFGLATIIDSRSLPFHIIFALLNAF 246
                          250       260
                   ....*....|....*....|.
gi 1034560524 1161 QGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15994    247 QGFFILLFGTILDRKIRIALY 267
7tmB2_GPR124-like_Adhesion_III cd15259
orphan GPR124 and related proteins, group III adhesion GPCRs, member of class B2 family of ...
935-1176 5.52e-17

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: 82.42  E-value: 5.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  935 PLV-IGCAVSCMALLTLLAIYAAFWRFIKSERSI--ILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSF 1011
Cdd:cd15259      6 PVVyAGAALCLLCLLATIITYIVFHRLIRISRKGrhMLVNLCLHLLLTCVVFVGGINRTANQLVCQAVGILLHYSTLCTL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1012 CWV----------LTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGfTRTKGYGTSSYCWLSLEGGLLyAFV 1081
Cdd:cd15259     86 LWVgvtarnmykqVTKTAKPPQDEDQPPRPPKPMLRFYLIGWGIPLIICGITAA-VNLDNYSTYDYCWLAWDPSLG-AFY 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1082 GPAAVIVLVNMLIGIIVFNKLmardgisdKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDRR--SVLFQALFAVFNS 1159
Cdd:cd15259    164 GPAALIVLVNCIYFLRIYCQL--------KGAPVSFQSQLRGAVITLFLYVAMWACGALAVSQRYflDLVFSCLYGATCS 235
                          250
                   ....*....|....*..
gi 1034560524 1160 AQGFVITAVHCFLRREV 1176
Cdd:cd15259    236 SLGLFVLIHHCLSREDV 252
7tmB1_CRF-R1 cd15445
corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane ...
934-1181 6.01e-17

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: 82.68  E-value: 6.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  934 VPLVIGCAVSCMALLTLLAIYAAFWRF--IKSERSIILLNFCLSILASNILILVGQSRVLSK------GVCTMTAAFLHF 1005
Cdd:cd15445      3 IAVIINYLGHCISLVALLVAFVLFLRLrsIRCLRNIIHWNLITAFILRNATWFVVQLTMSPEvhqsnvVWCRLVTAAYNY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1006 FFLSSFCWVLTEAWQSYLAVIGRMRTRLVRK-RFLCLGWGLP-ALVVAVSVGftrtKGYGTSSYCWLSLEGGLL--YAFV 1081
Cdd:cd15445     83 FHVTNFFWMFGEGCYLHTAIVLTYSTDKLRKwMFICIGWCIPfPIIVAWAIG----KLYYDNEKCWFGKRAGVYtdYIYQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1082 GPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLWSSCVVLPLLALTWMSA-VLAMTDRRS-VLFQALFAVFNS 1159
Cdd:cd15445    159 GPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFfVNPGEDEISrIVFIYFNSFLES 238
                          250       260
                   ....*....|....*....|..
gi 1034560524 1160 AQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15445    239 FQGFFVSVFYCFLNSEVRSAVR 260
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
367-417 3.73e-15

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 71.08  E-value: 3.73e-15
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   367 WEEWGSWSLCSRSCGRGSRSRMRTCV--PPQHGGKACEGPELQTKLCSMAACP 417
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCspPPQNGGGPCTGEDVETRACNEQPCP 53
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
870-923 1.38e-14

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: 69.34  E-value: 1.38e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1034560524   870 TDPHCASWDYSRadassGDWDTENCQTLETQAAHTRCQCQHLSTFAVLAQPPKD 923
Cdd:smart00303    1 FNPICVFWDESS-----GEWSTRGCELLETNGTHTTCSCNHLTTFAVLMDVPPI 49
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
872-917 2.11e-13

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: 65.79  E-value: 2.11e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034560524  872 PHCASWDYSraDASSGDWDTENCQTLETQAAHTRCQCQHLSTFAVL 917
Cdd:pfam01825    1 PQCVFWDFT--NSTTGRWSTEGCTTVSLNDTHTVCSCNHLTSFAVL 44
7tmB1_CRF-R2 cd15446
corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane ...
934-1181 9.98e-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: 69.99  E-value: 9.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  934 VPLVIGCAVSCMALLTLLAIYAAFW--RFIKSERSIILLNFCLSILASNI----LILVGQSRVLSKGV-CTMTAAFLHFF 1006
Cdd:cd15446      3 IALIINYLGHCISVGALVVAFLLFLclRSIRCLRNIIHWNLITTFILRNVmwflLQMIDHNIHESNEVwCRCITTIYNYF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1007 FLSSFCWVLTEAWQSYLAVIGRMRTRLVRK-RFLCLGWGLPA-LVVAVSVGftrtKGYGTSSYCWLSLEGGLL--YAFVG 1082
Cdd:cd15446     83 VVTNFFWMFVEGCYLHTAIVMTYSTDKLRKwVFLFIGWCIPCpIIVAWAIG----KLYYENEQCWFGKEPGKYidYIYQG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1083 PAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLWSSCVVLPLLALTWMsaVLAMTDRRSVLFQALFAVFN---- 1158
Cdd:cd15446    159 PVILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYM--LFFVNPGEDDISQIVFIYFNsflq 236
                          250       260
                   ....*....|....*....|...
gi 1034560524 1159 SAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15446    237 SFQGFFVSVFYCFLNGEVRSAAR 259
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
314-362 2.72e-12

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 62.99  E-value: 2.72e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1034560524   314 EWSPWSVCSLTCGQGLQVRTRSCVSSPY---GTLCSGPLRETRPCNNSAtCP 362
Cdd:smart00209    3 EWSEWSPCSVTCGGGVQTRTRSCCSPPPqngGGPCTGEDVETRACNEQP-CP 53
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
369-416 9.61e-12

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 61.14  E-value: 9.61e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034560524  369 EWGSWSLCSRSCGRGSRSRMRT-CVPPQHGGKACeGPELQTKLCSMAAC 416
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRTvIVEPQNGGRPC-PELLERRPCNLPPC 52
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
478-528 1.98e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 60.29  E-value: 1.98e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   478 WGPWNAWSLCSKTCDTGWQRRFRMC--QATGTQGYPCEGTGEEVKPCSEKRCP 528
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCcsPPPQNGGGPCTGEDVETRACNEQPCP 53
7tmB1_GHRHR2 cd15271
growth-hormone-releasing hormone receptor type 2, member of the class B family of ...
939-1185 2.01e-11

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: 66.29  E-value: 2.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  939 GCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVgQSRVL----SKGVCTM-TAAFLHFFFLSSFC- 1012
Cdd:cd15271     11 GYGTSLTSLITAVLIFCTF-RKLHCTRNYIHINLFVSFILRALAVFI-KDAVLfadeSVDHCTMsTVACKAAVTFFQFCv 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 -----WVLTEAWqsYLAVIGRMRTRLVRKRFLC---LGWGLPALVVAVsvgFTRTKGYGTSSYCWLSLEGGLLYAFVGPA 1084
Cdd:cd15271     89 lanffWLLVEGM--YLQTLLLLTFTSDRKYFWWyilIGWGAPSVTVTV---WVLTRLQYDNRGCWDDLESRIWWIIKTPI 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1085 AVIVLVNMLIGI----IVFNKLMARD-GISDKSKKQRAGASlwsSCVVLPLLALTWMsaVLAM----TDRRSVLFQALfa 1155
Cdd:cd15271    164 LLSVFVNFLIFInvirILVQKLKSPDvGGNDTSHYMRLAKS---TLLLIPLFGVHYV--VFAFfpehVGVEARLYFEL-- 236
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034560524 1156 VFNSAQGFVITAVHCFLRREVQDVVKCQMG 1185
Cdd:cd15271    237 VLGSFQGFIVALLYCFLNGEVQAEIKKRLG 266
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
422-472 2.98e-11

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 59.91  E-value: 2.98e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1034560524   422 WLEWGPWGPCSTSCANGTQQRSRKCSVAGPAW--ATCTGALTDTRECSNLECP 472
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPPPQNggGPCTGEDVETRACNEQPCP 53
TSP_1 pfam00090
Thrombospondin type 1 domain;
314-356 4.89e-11

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 58.97  E-value: 4.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034560524  314 EWSPWSVCSLTCGQGLQVRTRSCVS-SPYGTLCSGPLRETRPCN 356
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSpFPGGEPCTGDDIETQACK 45
TSP_1 pfam00090
Thrombospondin type 1 domain;
369-416 1.69e-10

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 57.43  E-value: 1.69e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034560524  369 EWGSWSLCSRSCGRGSRSRMRTCVPPQHGGKACEGPELQTKLCSMAAC 416
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
7tmB1_hormone_R cd15041
The subfamily B1 of hormone receptors (secretin-like), member of the class B family ...
937-1181 6.82e-10

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: 61.86  E-value: 6.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  937 VIGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGVcTMTAAFLHFFFLSSFCWVLT 1016
Cdd:cd15041      9 LVGYSLSLVALLPAIVIFLYF-RSLRCTRIRLHINLFLSFILRAVFWIIWDLLVVYDRL-TSSGVETVLMQNPVGCKLLS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1017 EAWQ-SYLAVIGRM-------RTRLVR---------KRFLCLGWGLPALVV---AVSVGFTRTKGygtssyCWLSL-EGG 1075
Cdd:cd15041     87 VLKRyFKSANYFWMlceglylHRLIVVaffsepsslKLYYAIGWGLPLVIVviwAIVRALLSNES------CWISYnNGH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1076 LLYAFVGPAAVIVLVNM--LIGI--IVFNKLMARDGISDKSKKQRAGASLwsscVVLPLLALTWMsavLAM-----TDRR 1146
Cdd:cd15041    161 YEWILYGPNLLALLVNLffLINIlrILLTKLRSHPNAEPSNYRKAVKATL----ILIPLFGIQYL---LTIyrppdGSEG 233
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1034560524 1147 SVLFQALFAVFNSAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15041    234 ELVYEYFNAILNSSQGFFVAVIYCFLNGEVQSELK 268
7tmB1_secretin cd15275
secretin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
938-1177 9.81e-10

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: 61.30  E-value: 9.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVgQSRVLSK-----------GVCTMTAAFLHFF 1006
Cdd:cd15275     10 VGYSVSLVSLAIALAILCSF-RRLHCTRNYIHMQLFLSFILRAISIFI-KDAVLFSseddnhcdiytVGCKVAMVFSNYC 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1007 FLSSFCWVLTEAWqsYLAVIGRMRTRLVRKR---FLCLGWGLPALVVAvsvgftrtkGYGTSSY------CW-LSLEGGL 1076
Cdd:cd15275     88 IMANYSWLLVEGL--YLHSLLSISFFSERKHlwwYIALGWGSPLIFII---------SWAIARYlhenegCWdTRRNAWI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1077 LYAFVGPAAVIVLVNML--IGI--IVFNKLMARDGISDKSKKQRAGASlwSSCVVLPLLALTWMSAVLAMTDRRSVLF-- 1150
Cdd:cd15275    157 WWIIRGPVILSIFVNFIlfLNIlrILMRKLRAPDMRGNEFSQYKRLAK--STLLLIPLFGLHYILFAFFPEDVSSGTMei 234
                          250       260
                   ....*....|....*....|....*...
gi 1034560524 1151 QALFAV-FNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15275    235 WLFFELaLGSFQGFVVAVLYCFLNGEVQ 262
7tmB2_GPR114 cd15443
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
937-1184 1.13e-09

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: 60.92  E-value: 1.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  937 VIGCAVSCMALLTLLAIYAAFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKG--VCTMTAAFLHFFFLSSFCWV 1014
Cdd:cd15443      9 IVGCSISAAASLLTILLHFFSRKQPKDSTTRIHMNLLGSLFLLNGSFLLSPPLATSQStwLCRAAAALLHYSLLCCLTWM 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1015 LTEAWQSYLaVIGRMRTRLVRKRF--LC-LGWGLPALVVAVSVGFTR----------TKGYGTSSYCWLSLEGGLLYAFV 1081
Cdd:cd15443     89 AIEGFHLYL-LLVKVYNIYIRRYVlkLCvLGWGLPALIVLLVLIFKReaygphtiptGTGYQNASMCWITSSKVHYVLVL 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1082 GPAAVIVLVNMLIGIIVFNklMARDGISDKSKKQRAGASLWSSCVVLP-LLALTWMSAVLAMTDrrSVLFQA-LFAVFNS 1159
Cdd:cd15443    168 GYAGLTSLFNLVVLAWVVR--MLRRLRSRKQELGERARRDWVTVLGLTcLLGTTWALAFFSFGV--FLIPQLfLFTIINS 243
                          250       260
                   ....*....|....*....|....*
gi 1034560524 1160 AQGFVITAVHCFLRREVQDVVKCQM 1184
Cdd:cd15443    244 LYGFFICLWYCTQRRRSDASAKSST 268
7tmB2_GPR97 cd15442
orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G ...
938-1165 1.45e-09

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: 60.97  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVScMALLTLLAIYAAFWRF----IKSERSI-ILLNFCLSILASNI--LILVGQSRVLSKGVCTMTAAFLHFFFLSS 1010
Cdd:cd15442     10 AGCGVS-MVFLIFTIILYFFLRFtyqkFKSEDAPkIHVNLSSSLLLLNLafLLNSGVSSRAHPGLCKALGGVTHYFLLCC 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1011 FCWVLTEAWQSYLAVIGRMRTrLVRKRF--LCL-GWGLPALVVAV-----SVG-FT-RTKGYGTS-SYCWLSlEGGLLYA 1079
Cdd:cd15442     89 FTWMAIEAFHLYLLAIKVFNT-YIHHYFakLCLvGWGFPALVVTItgsinSYGaYTiMDMANRTTlHLCWIN-SKHLTVH 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1080 FV---GPAAVIVLVNMLIGIIVFNKLMARDGIS---DKSKKQRAG-ASLWSSCvvlpLLALTWMSAVLAMTDrRSVLFQA 1152
Cdd:cd15442    167 YItvcGYFGLTFLFNTVVLGLVAWKIFHLQSATagkEKCQAWKGGlTVLGLSC----LLGVTWGLAFFTYGS-MSVPTVY 241
                          250
                   ....*....|...
gi 1034560524 1153 LFAVFNSAQGFVI 1165
Cdd:cd15442    242 IFALLNSLQGLFI 254
7tmB1_PDFR cd15261
The pigment dispersing factor receptor, member of the class B seven-transmembrane G ...
937-1184 2.64e-09

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: 60.07  E-value: 2.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  937 VIGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILV---GQSRVLSKGVCTMTAAFLHF-------- 1005
Cdd:cd15261      9 IVGLCLSLVSLIISLFIFSYF-RTLRNHRTRIHKNLFLAILLQVIIRLVlyiDQAITRSRGSHTNAATTEGRtinstpil 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1006 ----------FFLSSFCWVLTEAWqsYL---AVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGFTRTKgYGTSSyCWLSl 1072
Cdd:cd15261     88 cegfyvlleyAKTVMFMWMFIEGL--YLhniIVVSVFSGKPNYLFYYILGWGIPIVHTSAWAIVTLIK-MKVNR-CWFG- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1073 eggllYAFV-------GPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLWSSCVVLPLLALT-WMSAVLAMTD 1144
Cdd:cd15261    163 -----YYLTpyywileGPRLAVILINLFFLLNIIRVLVSKLRESHSREIEQVRKAVKAAIVLLPLLGITnILQMIPPPLT 237
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1034560524 1145 RRSVLFqALFA----VFNSAQGFVITAVHCFLRREVQDVVKCQM 1184
Cdd:cd15261    238 SVIVGF-AVWSysthFLTSFQGFFVALIYCFLNGEVKNVLKKFW 280
7tmB2_GPR123 cd16000
G protein-coupled receptor 123, member of the class B2 family of seven-transmembrane G ...
943-1187 3.05e-09

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: 59.97  E-value: 3.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  943 SCMALLtLLAIYAAFWRFIKSERSI--------ILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWV 1014
Cdd:cd16000     10 ACTAVM-LLCLFASIITYIVHHSTIrisrkgwhMLLNFCFHTALTFAVFAGGINRTKYPIICQAVGIVLHYSTLSTMLWI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1015 LTEAWQSYLAVIGRMRT----------RLVRKRFLCLGWGLPALVVAVSVGfTRTKGYGTSS----YCWLSLEGGlLYAF 1080
Cdd:cd16000     89 GVTARNIYKQVTKKPHLcqdtdqppypKQPLLRFYLVSGGVPFIICGITAA-TNINNYGTEDedtpYCWMAWEPS-LGAF 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1081 VGPAAVIVLVNMLIGIIVFNKLMARDGISDKSKKQRA-GASLWSSCVVLPLLALTWMSAVLAMTDRR--SVLFQALFAVF 1157
Cdd:cd16000    167 YGPVAFIVLVTCIYFLCTYVQLRRHPERKYELKNEHSfKAQLRAAAFTLFLFTATWAFGALAVSQGHflDMIFSCLYGAF 246
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034560524 1158 NSAQGFVITAVHCFLRrevQDVVKCQMGVC 1187
Cdd:cd16000    247 CVTLGLFILIHHCAKR---DDVWHCWWSCC 273
TSP_1 pfam00090
Thrombospondin type 1 domain;
424-471 3.28e-09

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 53.96  E-value: 3.28e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034560524  424 EWGPWGPCSTSCANGTQQRSRKCSVAGPAWATCTGALTDTRECSNLEC 471
Cdd:pfam00090    2 PWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
HormR smart00008
Domain present in hormone receptors;
531-595 8.44e-09

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 53.67  E-value: 8.44e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034560524   531 HEMCRDEYVMLMTWKKAAAGEIIYNKCPPNASG-----SASRRCLLSAQgvayWGL--PSFARCISHEYRYL 595
Cdd:smart00008    2 DLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGfsyktGASRNCTENGG----WSPpfPNYSNCTSNDYEEL 69
7tmB1_PTH3R cd15983
parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G ...
1041-1181 1.01e-08

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: 58.40  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1041 LGWGLPALVVAVsvgFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGIIVFNKLMARDGISDKSK---KQRA 1117
Cdd:cd15983    136 IGWGLPAVFVSV---WASVRVSLADTQCWDLSAGNLKWIYQVPILAAILVNFFLFLNIVRVLASKLWETNTGKldpRQQY 212
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034560524 1118 GASLWSSCVVLPLLALTWMsAVLAM--TDRRSVLFQALF---AVFNSAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15983    213 RKLLKSTLVLMPLFGVHYV-LFMAMpyTDVTGLLWQIQMhyeMLFNSSQGFFVAFIYCFCNGEVQAEIK 280
7tmB1_calcitonin_R cd15274
calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
937-1183 1.19e-08

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: 57.86  E-value: 1.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  937 VIGCAVSCMALLTLLAIYAaFWRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGV--------CTMTAAFLHFFFL 1008
Cdd:cd15274      9 IVGHSLSIATLLISLGIFF-FFRSLSCQRVTLHKNLFLSYILNSIIIIIHLVAVVPNGElvarnpvsCKILHFIHQYMMG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1009 SSFCWVLTEA-WQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVgFTRTKGYGTSsyCWLSLEGGLLYAFVGPAAVI 1087
Cdd:cd15274     88 CNYFWMLCEGiYLHTLIVVAVFAEKQRLMWYYLLGWGFPLIPTTIHA-ITRAVYYNDN--CWLSSETHLLYIIHGPIMAA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1088 VLVNMLIGIIVFNKLMARDGISDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDRRSV-LFQALFAVFNSAQGFVIT 1166
Cdd:cd15274    165 LVVNFFFLLNIVRVLVTKLRETHEAESHMYLKAVKATLILVPLLGIQFVLFPWRPSGKILGkIYDYVMHSLIHFQGFFVA 244
                          250
                   ....*....|....*..
gi 1034560524 1167 AVHCFLRREVQDVVKCQ 1183
Cdd:cd15274    245 TIFCFCNGEVQATLKRQ 261
7tmB1_DH_R cd15263
insect diuretic hormone receptors, member of the class B family of seven-transmembrane G ...
1013-1181 1.29e-08

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: 57.76  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 WVLTEAWQSYLAVIGRMRTRLVRKR-FLCLGWGLPALVVAV-----SVGFTRTKGYGTSS----YCWLSLEGGLLYAFVG 1082
Cdd:cd15263     88 WMFVEGLYLYMLVVETFSGENIKLRvYAFIGWGIPAVVIVIwaivkALAPTAPNTALDPNgllkHCPWMAEHIVDWIFQG 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1083 PAAVIVLVNM--LIGI--IVFNKLMARDGISDKSKKQRAGASLwsscVVLPLLALTWMSAVLAMTDRRS-VLFQALFAVF 1157
Cdd:cd15263    168 PAILVLAVNLvfLVRImwVLITKLRSANTVETQQYRKAAKALL----VLIPLLGITYILVIAGPTEGIAaNIFEYVRAVL 243
                          170       180
                   ....*....|....*....|....
gi 1034560524 1158 NSAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15263    244 LSTQGFTVALFYCFLNTEVRNTLR 267
TSP_1 pfam00090
Thrombospondin type 1 domain;
479-527 1.41e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.04  E-value: 1.41e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034560524  479 GPWNAWSLCSKTCDTGWQRRFRMCQATGTQGYPCEGTGEEVKPCSEKRC 527
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRTCKSPFPGGEPCTGDDIETQACKMDKC 49
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
314-356 2.58e-08

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 51.51  E-value: 2.58e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034560524  314 EWSPWSVCSLTCGQGLQVRTRSCVSSPY--GTLCsGPLRETRPCN 356
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTRTVIVEPQngGRPC-PELLERRPCN 48
7tmB1_PTH-R_related cd15272
invertebrate parathyroid hormone-related receptors, member of the class B family of ...
1013-1181 2.87e-08

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: 57.01  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 WVLTEAWqsYLAVIGRMRTRLVRKR---FLCLGWGLPALVVAVSVGFTRTKgygTSSYCW-LSLEGGLLYAFVGPAAVIV 1088
Cdd:cd15272    107 WIFVEGL--YLHMLIFVAVFSENSRvkwYILLGWLSPLLFVLPWVFVRATL---EDTLCWnTNTNKGYFWIIRGPIVISI 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1089 LVNMLIGI----IVFNKLMArdGISDKSKKQRAGASLWSSCVVLPLLALTWMSAVlAMTDRRS-------VLFQALFavF 1157
Cdd:cd15272    182 AINFLFFInivrVLFTKLKA--SNTQESRPFRYRKLAKSTLVLIPLFGVHYMVFV-VLPDSMSsdeaelvWLYFEMF--F 256
                          170       180
                   ....*....|....*....|....
gi 1034560524 1158 NSAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15272    257 NSFQGFIVALLFCFLNGEVQSEIK 280
7tmB1_Secretin_R-like cd15930
secretin receptor-like group of hormone receptors, member of the class B family of ...
938-1181 6.34e-08

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: 55.90  E-value: 6.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKG---VCTM-TAAFLHFFFLSSFC- 1012
Cdd:cd15930     10 VGYSLSLTSLTTAMIILCLF-RKLHCTRNYIHMNLFVSFILRAIAVFIKDAVLFSSEdvdHCFVsTVGCKASMVFFQYCv 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 -----WVLTEA-WQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVsvgFTRTKGYGTSSYCW-LSLEGGLLYAFVGPAA 1085
Cdd:cd15930     89 manffWLLVEGlYLHTLLVISFFSERRYFWWYVLIGWGAPTVFVTV---WIVARLYFEDTGCWdINDESPYWWIIKGPIL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1086 VIVLVNMLIGI----IVFNKLMARD-GISDKSKKQRAGASlwsSCVVLPLLALTWMsaVLAMT-DRRSVLFQALFA-VFN 1158
Cdd:cd15930    166 ISILVNFVLFIniirILLQKLRSPDiGGNESSQYKRLARS---TLLLIPLFGIHYI--VFAFFpENISLGIRLYFElCLG 240
                          250       260
                   ....*....|....*....|...
gi 1034560524 1159 SAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15930    241 SFQGFVVAVLYCFLNGEVQAEIK 263
7tmB1_NPR_B4_insect-like cd15260
insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of ...
937-1184 7.68e-08

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: 55.36  E-value: 7.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  937 VIGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILIL------VGQSRVL--SKGVCTMTAAFLHFFFL 1008
Cdd:cd15260      9 IGGYSVSLIALIISLAIFFSF-RSLRCTRITIHMNLFISFALNNLLWIvwyklvVDNPEVLleNPIWCQALHVLLQYFMV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1009 SSFCWVLTEAWQSYLA--VIGRMRTRLVRKrFLCLGWGLPALVVAVSVGFTRTKGYGTSsYCWLSlEGGLLYAFVGPAAV 1086
Cdd:cd15260     88 CNYFWMFCEGLYLHTVlvVAFISEKSLMRW-FIAIGWGVPLVITAIYAGVRASLPDDTE-RCWME-ESSYQWILIVPVVL 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1087 IVLVNM--LIGII--VFNKLMARDGISDKSKKQRAgasLWSSCVVLPLLALTWmsavLAMTDRR------SVLFQALFAV 1156
Cdd:cd15260    165 SLLINLifLINIVrvLLTKLRATSPNPAPAGLRKA---VRATLILIPLLGLQF----LLIPFRPepgaplETIYQYVSAL 237
                          250       260
                   ....*....|....*....|....*...
gi 1034560524 1157 FNSAQGFVITAVHCFLRREVQDVVKCQM 1184
Cdd:cd15260    238 LTSLQGLCVAVLFCFCNGEVIAAIKRKW 265
7tmB1_PTH1R cd15984
parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G ...
1038-1181 1.87e-07

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: 54.57  E-value: 1.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1038 FLCLGWGLPALVVAVsvgFTRTKGYGTSSYCWLSLEGGLLYAFVGPAAVIVLVNMLIGIIVFNKLMARDGISDKSK---K 1114
Cdd:cd15984    138 FTLFGWGLPAVFVTI---WASVRATLADTGCWDLSAGNLKWIIQVPILAAIVVNFILFINIVRVLATKLRETNAGRcdtR 214
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034560524 1115 QRAGASLWSSCVVLPLLALTWMsAVLAM--TDRRSVLFQALF---AVFNSAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15984    215 QQYRKLLKSTLVLMPLFGVHYI-VFMAMpyTEVSGILWQVQMhyeMLFNSFQGFFVAIIYCFCNGEVQAEIK 285
7tmB1_VIP-R2 cd15986
vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of ...
938-1181 2.11e-07

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: 54.04  E-value: 2.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILVGQSRVLSKGV------------CTMTAAFLHF 1005
Cdd:cd15986     10 LGHSVSLIALTTGSTILCLF-RKLHCTRNYIHLNLFFSFILRAISVLVKDDILYSSSNtehctvppsligCKVSLVILQY 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1006 FFLSSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVavsVGFTRTKGYGTSSYCWLSLEGGLLYAFVG-PA 1084
Cdd:cd15986     89 CIMANFYWLLVEGLYLHTLLVVIFSENRHFIVYLLIGWGIPTVFI---IAWIVARIYLEDTGCWDTNDHSVPWWVIRiPI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1085 AVIVLVNMLIGI----IVFNKLMARD-GISDKSKKQRAGASlwsSCVVLPLLALTWMSAVLaMTDRRSVLFQALFAV-FN 1158
Cdd:cd15986    166 IISIILNFILFIsiirILLQKLRSPDvGGNDQSQYKRLAKS---TLLLIPLFGVHYIVFVY-FPDSSSSNYQIFFELcLG 241
                          250       260
                   ....*....|....*....|...
gi 1034560524 1159 SAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15986    242 SFQGLVVAILYCFLNSEVQGELK 264
7tmB1_GlucagonR-like_1 cd15985
uncharacterized group of glucagon receptor-like proteins, member of the class B family of ...
1013-1183 2.77e-07

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: 53.78  E-value: 2.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 WVLTEAWQSYLAVIGRMRTRLVRKR-FLCLGWGLPALVVavsVGFTRTKGYGTSSYCWlSLEGGLLYAFV--GPAAVIVL 1089
Cdd:cd15985    104 WFFVEAVYLYKLLIGAVFSEKNYYLlYLYLGWGTPVLFV---VPWMLAKYLKENKECW-ALNENMAYWWIirIPILLASL 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1090 VNMLIGI----IVFNKLMARDGISDKSKKQRAGASLwsscVVLPLLALTWMSAVLAMTDRRSVLF---QALFAVF-NSAQ 1161
Cdd:cd15985    180 INLLIFMrilkVILSKLRANQKGYADYKLRLAKATL----TLIPLFGIHEVVFIFATDEQTTGILryiKVFFTLFlNSFQ 255
                          170       180
                   ....*....|....*....|..
gi 1034560524 1162 GFVITAVHCFLRREVQDVVKCQ 1183
Cdd:cd15985    256 GFLVAVLYCFANKEVKSELLKK 277
7tmB1_GCGR cd15267
glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled ...
930-1177 1.27e-06

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: 51.75  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  930 GSPSVPLVIGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNF-------CLSILASNILI----------LVGQSRVLS 992
Cdd:cd15267      4 SSFQVMYTVGYSLSLGALLLALAILGGF-SKLHCMRNAIHMNLfasfilkASSVLVIDGLLrtrysqkiedDLSSTWLSD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  993 KGV--CTMTAAFLHFFFLSSFCWVLTEAWQSY-LAVIGRMRTRLVRKRFLCLGWGLPALVVavsVGFTRTKGYGTSSYCW 1069
Cdd:cd15267     83 EAVagCRVAAVFMQYGIVANYCWLLVEGIYLHnLLVLAVFPERSYFSLYLCIGWGAPALFV---VPWVVVKCLYENVQCW 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1070 -LSLEGGLLYAFVGPAAVIVLVNMLIGI----IVFNKLMARDGISDKSKKQRAGASLwsscVVLPLLALTWMsAVLAMTD 1144
Cdd:cd15267    160 tSNDNMGFWWILRFPVFLAILINFFIFVriiqILVSKLRARQMHYTDYKFRLAKSTL----TLIPLLGIHEV-VFAFVTD 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1034560524 1145 -------RRSVLFQALFavFNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15267    235 ehaqgtlRSAKLFFDLF--LSSFQGLLVAVLYCFLNKEVQ 272
7tmB1_PTHR cd15265
parathyroid hormone receptors, member of the class B family of seven-transmembrane G ...
1037-1181 1.48e-06

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: 51.61  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1037 RFLCLGWGLPALVVAVSVgFTRTKGYGTSsyCWLSLEGGLLYAFVGPAAVIVLVNMLIGI----IVFNKL-MARDGISDK 1111
Cdd:cd15265    137 GFTLIGWGFPAVFVIPWA-SVRATLADTR--CWDLSAGNYKWIYQVPILAAIVVNFILFLnivrVLATKLrETNAGRCDT 213
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034560524 1112 SKKQRAGASlwSSCVVLPLLALTWMSAVLAMTDRRSVLFQA-----LFavFNSAQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15265    214 RQQYRKLAK--STLVLIPLFGVHYIVFMGMPYTEVGLLWQIrmhyeLF--FNSFQGFFVAIIYCFCNGEVQAEIK 284
7tmB1_NPR_B7_insect-like cd15273
insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of ...
1041-1177 2.23e-06

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: 51.22  E-value: 2.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1041 LGWGLPALVVA----VSVGFTrtkgygtSSYCWLSLEGGLLYAFV-GPAAVIVLVN----MLIGIIVFNKLmaRDGISDK 1111
Cdd:cd15273    137 LGWGLPLIFVVpwivARILFE-------NSLCWTTNSNLLNFLIIrIPIMISVLINfilfLNIVRVLLVKL--RSSVNED 207
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034560524 1112 SKKQRAGASlwSSCVVLPLLAL--TWMSAV-LAMTDRRSVLFQALF--AVFNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15273    208 SRRYKKWAK--STLVLVPLFGVhyTIFLILsYLDDTNEAVELIWLFcdQLFASFQGFFVALLYCFLNGEVR 276
7tmB1_GlucagonR-like cd15929
glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G ...
1012-1177 6.51e-06

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: 49.74  E-value: 6.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1012 CWVLTEAWQSY-LAVIGRMRTRLVRKRFLCLGWGLPALVVavsVGFTRTKGYGTSSYCWLSLEG-GLLYAFVGPAAVIVL 1089
Cdd:cd15929    102 YWLLVEGLYLHtLLVLAVFSERSIFRLYLLLGWGAPVLFV---VPWGIVKYLYENTGCWTRNDNmAYWWIIRLPILLAIL 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1090 VNMLIGI----IVFNKLMARDGISDKSKKQRAGASLwsscVVLPLLALTWMSAVLAMTD------RRSVLFQALFavFNS 1159
Cdd:cd15929    179 INFFIFVrilkILVSKLRANQMCKTDYKFRLAKSTL----TLIPLLGVHEVVFAFVTDEqargtlRFIKLFFELF--LSS 252
                          170
                   ....*....|....*...
gi 1034560524 1160 AQGFVITAVHCFLRREVQ 1177
Cdd:cd15929    253 FQGLLVAVLYCFANKEVQ 270
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
424-471 1.72e-05

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 43.42  E-value: 1.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560524  424 EWGPWGPCSTSCANGTQQRSRkcSVAGPA---WATCtGALTDTRECSNLEC 471
Cdd:pfam19028    5 EWSEWSECSVTCGGGVQTRTR--TVIVEPqngGRPC-PELLERRPCNLPPC 52
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
479-527 1.99e-05

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 43.42  E-value: 1.99e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560524  479 GPWNAWSLCSKTCDTGWQRRFRMC--QATGtQGYPCeGTGEEVKPCSEKRC 527
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTVivEPQN-GGRPC-PELLERRPCNLPPC 52
7tmB2_GPR124 cd15998
G protein-coupled receptor 124, member of the class B2 family of seven-transmembrane G ...
944-1177 2.55e-05

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: 47.64  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  944 CMALLtLLAIYAAFWRFIKSERSI--------ILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSFCWVL 1015
Cdd:cd15998     11 CTALL-LLCLFSTIITYILNHSSIhvsrkgwhMLLNLCFHIAMTSAVFAGGITLTNYQMVCQAVGITLHYSSLSTLLWMG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1016 TEA--------WQSYLAVIGRMRTRLVRK--RFLCLGWGLPALVVAVSVGFTRTKGYGTSSYCWLSLEGGlLYAFVGPAA 1085
Cdd:cd15998     90 VKArvlhkeltWRAPPPQEGDPALPTPRPmlRFYLIAGGIPLIICGITAAVNIHNYRDHSPYCWLVWRPS-LGAFYIPVA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1086 VIVLVNMLIGIIVFNKLmaRDGISDKSKKQRAGASLWSSCVVLPLLALTWMSAVLAMTDR--RSVLFQALFAVFNSAQGF 1163
Cdd:cd15998    169 LILLVTWIYFLCAGLHL--RGPSADGDSVYSPGVQLGALVTTHFLYLAMWACGALAVSQRwlPRVVCSCLYGVAASALGL 246
                          250
                   ....*....|....
gi 1034560524 1164 VITAVHCFLRREVQ 1177
Cdd:cd15998    247 FVFTHHCARRRDVR 260
7tmB1_VIP-R1 cd15269
vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of ...
938-1181 3.68e-05

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: 47.16  E-value: 3.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFwRFIKSERSIILLNFCLSILASNILILV--------GQSRVLSKGV--CTMTAAFLHFFF 1007
Cdd:cd15269     10 IGHSLSLISLTAAMIILCLF-RKLHCTRNYIHMHLFMSFILRAIAVFIkdavlfesGEEDHCSVASvgCKAAMVFFQYCI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1008 LSSFCWVLTEAWQSY-LAVIGRMRTRLVRKRFLCLGWGLPALVVAVsvgFTRTKGYGTSSYCWLSLEGGLLYAFV-GPAA 1085
Cdd:cd15269     89 MANFFWLLVEGLYLHtLLAVSFFSERKYFWWYILIGWGAPSVFITA---WSVARIYFEDVGCWDTIIESLLWWIIkTPIL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1086 VIVLVNMLIGI----IVFNKLMARD-GISDKSKKQRAGASlwsSCVVLPLLALTWMSAVLAMTDRRSVLFQALFAVFNSA 1160
Cdd:cd15269    166 VSILVNFILFIciirILVQKLHSPDiGRNESSQYSRLAKS---TLLLIPLFGIHYIMFAFFPDNFKAEVKLVFELILGSF 242
                          250       260
                   ....*....|....*....|.
gi 1034560524 1161 QGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15269    243 QGFVVAVLYCFLNGEVQAELK 263
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
317-357 4.31e-05

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 42.44  E-value: 4.31e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034560524  317 PWSVCSLTCGQGLQVRTRSCVSSPYGTL-----CSGPLR--ETRPCNN 357
Cdd:pfam19030    5 PWGECSVTCGGGVQTRLVQCVQKGGGSIvpdseCSAQKKppETQSCNL 52
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
481-527 4.57e-05

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 42.44  E-value: 4.57e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034560524  481 WNA--WSLCSKTCDTGWQRRFRMCQATGTQ----GYPCEGTG--EEVKPCSEKRC 527
Cdd:pfam19030    1 WVAgpWGECSVTCGGGVQTRLVQCVQKGGGsivpDSECSAQKkpPETQSCNLKPC 55
PTZ00087 PTZ00087
thrombosponding-related protein; Provisional
314-355 6.22e-05

thrombosponding-related protein; Provisional


Pssm-ID: 185438  Cd Length: 340  Bit Score: 46.86  E-value: 6.22e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1034560524  314 EWSPWSVCSLTCGQ--GLQVRTRSCVsSPYGTLCSGPLRETRPC 355
Cdd:PTZ00087   235 EWGEWSNCSMECDHpdNVQIRERKCA-HPSGDCFKGDLKETRPC 277
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
426-471 9.93e-05

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 41.67  E-value: 9.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034560524  426 GPWGPCSTSCANGTQQRSRKC------SVAGPAWATCTGALTDTRECSNLEC 471
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCvqkgggSIVPDSECSAQKKPPETQSCNLKPC 55
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
359-419 1.16e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 46.88  E-value: 1.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034560524  359 ATCpvhGVWEEWgswSLCSRSCGRGSRSRMRtcvPPQHGGkaCEgPELQTKlCSMAACPVE 419
Cdd:PTZ00441   238 ASC---GPWDEW---TPCSVTCGKGTHSRSR---PILHEG--CT-THMVEE-CEEEECPVE 285
7tmB1_GLP1R cd15268
glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G ...
1013-1177 2.90e-04

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: 44.56  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 WVLTEAWQSY-LAVIGRMRTRLVRKRFLCLGWGLPALVVAVsvgftrtkgYGTSSY------CWlSLEGGLLYAFV--GP 1083
Cdd:cd15268    103 WLLVEGVYLYtLLAFSVFSEQRIFRLYLSIGWGVPLLFVIP---------WGIVKYlyedegCW-TRNSNMNYWLIirLP 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1084 AAVIVLVNMLIGI----IVFNKLMARDGISDKSKKQRAGASLwsscVVLPLLALTWMSAVLAMTD--RRSVLFQALFA-- 1155
Cdd:cd15268    173 ILFAIGVNFLIFIrvicIVVSKLKANLMCKTDIKCRLAKSTL----TLIPLLGTHEVIFAFVMDEhaRGTLRFVKLFTel 248
                          170       180
                   ....*....|....*....|..
gi 1034560524 1156 VFNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15268    249 SFTSFQGLMVAILYCFVNNEVQ 270
7tmB1_GLP2R cd15266
glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G ...
996-1177 3.64e-04

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: 44.35  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  996 CTMTAAFLHFFFLSSFCWVLTEAWQSY-LAVIGRMRTRLVRKRFLCLGWGLPALVVavsVGFTRTKGYGTSSYCWLSLEG 1074
Cdd:cd15266     87 CRVAQVFMHYFVGANYFWLLVEGLYLHtLLVTAVLSERRLLKKYMLIGWGTPVLFV---VPWGVAKILLENTGCWGRNEN 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1075 -GLLYAFVGPAAVIVLVNMLIGI----IVFNKLMARDGISDKSKKQRAGASLwsscVVLPLLALTWMsAVLAMTD----- 1144
Cdd:cd15266    164 mGIWWIIRGPILLCITVNFYIFLkilkLLLSKLKAQQMRFTDYKYRLARSTL----VLIPLLGIHEV-VFSFITDeqveg 238
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034560524 1145 --RRSVLFQALfaVFNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15266    239 fsRHIRLFIQL--TLSSFQGFLVAVLYCFANGEVK 271
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
425-472 3.96e-04

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 44.95  E-value: 3.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1034560524  425 WGPWGPCSTSCANGTQQRSRKCSVAGpawatCTGALtdTRECSNLECP 472
Cdd:PTZ00441   243 WDEWTPCSVTCGKGTHSRSRPILHEG-----CTTHM--VEECEEEECP 283
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
371-421 6.44e-04

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 39.36  E-value: 6.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034560524  371 GSWSLCSRSCGRGSRSRMRTCVPPqhGGKACEGPElqtkLCSMAACPVEGQ 421
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLVQCVQK--GGGSIVPDS----ECSAQKKPPETQ 48
7tmB1_GHRHR cd15270
growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane ...
938-1177 7.34e-04

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: 43.25  E-value: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  938 IGCAVSCMALLTLLAIYAAFWRfIKSERSIILLNFCLSILASNILILVGQSRVLSKGV---CTM-TAAFLHFFFLSSFC- 1012
Cdd:cd15270     10 VGYSISIVSLCVAVAILVAFRR-LHCPRNYIHIQLFFTFILKAIAVFIKDAALFQEDDtdhCSMsTVLCKVSVVFCHYCv 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1013 -----WVLTEAwqSYLAVIgRMRTRLVRKR----FLCLGWGLPALVVAVSVGftrTKGYGTSSYCW-LSLEGGLLYAFVG 1082
Cdd:cd15270     89 mtnffWLLVEA--VYLNCL-LASSFPRGKRyfwwLVLLGWGLPTLCTGTWIL---CKLYFEDTECWdINNDSPYWWIIKG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1083 PAAVIVLVNMLIGI----IVFNKLMARDGISDKSKKQRAGASlwSSCVVLPLLALTWMSAVL----AMTDRRSVLFQALf 1154
Cdd:cd15270    163 PIVISVGVNFLLFLniirILLKKLDPRQINFNNSAQYRRLSK--STLLLIPLFGTHYIIFNFlpdyAGLGIRLYLELCL- 239
                          250       260
                   ....*....|....*....|...
gi 1034560524 1155 avfNSAQGFVITAVHCFLRREVQ 1177
Cdd:cd15270    240 ---GSFQGFIVAVLYCFLNQEVQ 259
7tmB2_GPR125 cd15999
G protein-coupled receptor 125, member of the class B2 family of seven-transmembrane G ...
935-1102 1.62e-03

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: 42.54  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524  935 PLVIGCAVSC-MALLTLLAIYAAFWRFIKSERSI--ILLNFCLSILASNILILVGQSRVLSKGVCTMTAAFLHFFFLSSF 1011
Cdd:cd15999      6 PVVYATAVVLlLCLLTIIVSYIYHHSLVRISRKSwhMLVNLCFHIFLTCAVFVGGINQTRNASVCQAVGIILHYSTLATV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1012 CWVLTEAWQSYLAVigrmrTRLVRK---------------RFLCLGWGLPALVVAVSVGfTRTKGYGT---SSYCWLSLE 1073
Cdd:cd15999     86 LWVGVTARNIYKQV-----TRKAKRcqdpdeppppprpmlRFYLIGGGIPIIVCGITAA-ANIKNYGSrpnAPYCWMAWE 159
                          170       180
                   ....*....|....*....|....*....
gi 1034560524 1074 GGlLYAFVGPAAVIVLVNMLIGIIVFNKL 1102
Cdd:cd15999    160 PS-LGAFYGPAGFIIFVNCMYFLSIFIQL 187
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
531-590 1.66e-03

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 38.51  E-value: 1.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034560524  531 HEMCRDEYVMLMTWKKAAAGEIIYNKCPPNAS-----GSASRRCLLSAQgvayWGLPS---FARCISH 590
Cdd:pfam02793    1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSgfdprGNASRNCTEDGT----WSEHPpsnYSNCTSN 64
7tmB1_PACAP-R1 cd15987
pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B ...
1038-1181 2.93e-03

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: 41.49  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034560524 1038 FLCLGWGLPALVVAVsvgFTRTKGYGTSSYCW-LSLEGGLLYAFVGPAAVIVLVN--MLIGIIVF--NKLMARD-GISDK 1111
Cdd:cd15987    120 YTIIGWGTPTICVTV---WAVLRLHFDDTGCWdMNDNTALWWVIKGPVVGSIMINfvLFIGIIIIlvQKLQSPDiGGNES 196
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034560524 1112 SKKQRAGASlwsSCVVLPLLALTWMSAVLA---MTDRRSVLFQALFAVFnsaQGFVITAVHCFLRREVQDVVK 1181
Cdd:cd15987    197 SIYLRLARS---TLLLIPLFGIHYTVFAFSpenVSKRERLVFELGLGSF---QGFVVAVLYCFLNGEVQSEIK 263
 
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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