NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1370468401|ref|XP_024306028|]
View 

polycystin-1-like protein 3 isoform X6 [Homo sapiens]

Protein Classification

polycystin family protein( domain architecture ID 13062566)

polycystin family protein similar to Homo sapiens polycystic kidney disease 2-like 2 protein that may function as a subunit of a cation channel and play a role in fertilization

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 507-623 3.82e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


:

Pssm-ID: 238850  Cd Length: 120  Bit Score: 193.26  E-value: 3.82e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  507 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 586
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370468401  587 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 623
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
PKD_channel super family cl37568
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1231-1442 3.87e-29

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


The actual alignment was detected with superfamily member pfam08016:

Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 116.99  E-value: 3.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1231 IISQVIYYLLVCYYAFIQGCQLKQQKWRFFTGKRNILDTSIILISFILLGLDMKSISLHKKNMARYRDDQDRFISFYEAV 1310
Cdd:pfam08016   11 LLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPVTFIDFDRVA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1311 KVNSAATHLVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSS 1390
Cdd:pfam08016   91 QLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPNFSNFVKS 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370468401 1391 AVTVVGLLMGISHQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAF 1442
Cdd:pfam08016  171 ILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
GPS super family cl02559
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 397-436 9.96e-08

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.


The actual alignment was detected with superfamily member smart00303:

Pssm-ID: 470616  Cd Length: 49  Bit Score: 49.69  E-value: 9.96e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370468401   397 TQCYYWEIHNQTWSSAGCQVGP-QSTilRTQCLCNHLTFFA 436
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLEtNGT--HTTCSCNHLTTFA 41
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 507-623 3.82e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 193.26  E-value: 3.82e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  507 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 586
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370468401  587 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 623
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1231-1442 3.87e-29

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 116.99  E-value: 3.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1231 IISQVIYYLLVCYYAFIQGCQLKQQKWRFFTGKRNILDTSIILISFILLGLDMKSISLHKKNMARYRDDQDRFISFYEAV 1310
Cdd:pfam08016   11 LLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPVTFIDFDRVA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1311 KVNSAATHLVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSS 1390
Cdd:pfam08016   91 QLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPNFSNFVKS 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370468401 1391 AVTVVGLLMGISHQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAF 1442
Cdd:pfam08016  171 ILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 509-623 1.65e-21

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 91.34  E-value: 1.65e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  509 YLIQVYTGYRRSAATTAKVVITLYGSEGRS--EPHHLCDPQktvFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 586
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESaqLEITLDNPD---FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1370468401  587 YVSQVIVC-DMAVKRKWHFLCNCWLAVDLgDCELDRVF 623
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVYGSK-KYKETRVF 114
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
507-613 1.19e-13

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 68.44  E-value: 1.19e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401   507 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSgvSPSW 586
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78

                            90       100
                    ....*....|....*....|....*..
gi 1370468401   587 YVSQVIVCDMAVKRKWHFLCNCWLAVD 613
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 397-436 9.96e-08

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: 49.69  E-value: 9.96e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370468401   397 TQCYYWEIHNQTWSSAGCQVGP-QSTilRTQCLCNHLTFFA 436
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLEtNGT--HTTCSCNHLTTFA 41
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 398-436 1.14e-07

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: 49.23  E-value: 1.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1370468401  398 QCYYWEIHNQT---WSSAGCQVGpQSTILRTQCLCNHLTFFA 436
Cdd:pfam01825    2 QCVFWDFTNSTtgrWSTEGCTTV-SLNDTHTVCSCNHLTSFA 42
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 1319-1471 3.64e-06

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 51.87  E-value: 3.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1319 LVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSSAVTVVGLL 1398
Cdd:PLN03223  1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENL 1373

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468401 1399 MG-ISHQEEVF----ALDPVLGTFLILTSVILMVLVVINLFVSAILMAFGkERKSLKKEAALIDTllqKLSNLLGISW 1471
Cdd:PLN03223  1374 LGdITYFNEDLknltGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFG-EVKANAAETVSVHT---ELFPMLRDKW 1447
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 507-623 3.82e-57

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238850  Cd Length: 120  Bit Score: 193.26  E-value: 3.82e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  507 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 586
Cdd:cd01752      1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1370468401  587 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 623
Cdd:cd01752     81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 509-626 2.15e-31

PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238854  Cd Length: 120  Bit Score: 119.58  E-value: 2.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  509 YLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTV-FERGGLDVFLLTTwTSLGNLHSLRLWHDNSGVSPSWY 587
Cdd:cd01756      3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNkFERGQTDKFTVEA-VDLGKLKKIRIGHDNSGLGAGWF 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1370468401  588 VSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVFIPV 626
Cdd:cd01756     82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1231-1442 3.87e-29

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 116.99  E-value: 3.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1231 IISQVIYYLLVCYYAFIQGCQLKQQKWRFFTGKRNILDTSIILISFILLGLDMKSISLHKKNMARYRDDQDRFISFYEAV 1310
Cdd:pfam08016   11 LLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPVTFIDFDRVA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1311 KVNSAATHLVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSS 1390
Cdd:pfam08016   91 QLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPNFSNFVKS 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1370468401 1391 AVTVVGLLMGISHQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAF 1442
Cdd:pfam08016  171 ILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 509-623 1.65e-21

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.


Pssm-ID: 396180  Cd Length: 115  Bit Score: 91.34  E-value: 1.65e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  509 YLIQVYTGYRRSAATTAKVVITLYGSEGRS--EPHHLCDPQktvFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 586
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESaqLEITLDNPD---FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1370468401  587 YVSQVIVC-DMAVKRKWHFLCNCWLAVDLgDCELDRVF 623
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVYGSK-KYKETRVF 114
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 508-610 1.36e-16

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.


Pssm-ID: 238061  Cd Length: 116  Bit Score: 76.99  E-value: 1.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  508 HYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHhLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSWY 587
Cdd:cd00113      2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDI-PILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWY 80

                           90       100
                   ....*....|....*....|...
gi 1370468401  588 VSQVIVCDMAVKRKWHFLCNCWL 610
Cdd:cd00113     81 CESITVQALGTKKVYTFPVNRWV 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
507-613 1.19e-13

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 68.44  E-value: 1.19e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401   507 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSgvSPSW 586
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEHR--HPEW 78

                            90       100
                    ....*....|....*....|....*..
gi 1370468401   587 YVSQVIVCDMAVKRKWHFLCNCWLAVD 613
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVYPD 105
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 397-436 9.96e-08

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: 49.69  E-value: 9.96e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1370468401   397 TQCYYWEIHNQTWSSAGCQVGP-QSTilRTQCLCNHLTFFA 436
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLEtNGT--HTTCSCNHLTTFA 41
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 398-436 1.14e-07

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: 49.23  E-value: 1.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1370468401  398 QCYYWEIHNQT---WSSAGCQVGpQSTILRTQCLCNHLTFFA 436
Cdd:pfam01825    2 QCVFWDFTNSTtgrWSTEGCTTV-SLNDTHTVCSCNHLTSFA 42
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 509-613 1.57e-07

PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins.


Pssm-ID: 238852  Cd Length: 129  Bit Score: 51.77  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  509 YLIQVYTGYRRSAATTAKVVITLYGSEGR-------SEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSG 581
Cdd:cd01754      3 YTIYVQTGSIWKAGTDSRISLQIYDADGPglrianlEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1370468401  582 VSPSWYVSQVIVCDMAVKR---KWHFLCNCWLAVD 613
Cdd:cd01754     83 NHPGWYVNYVEVTQAGQHApcmQHLFAVEQWLATD 117
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 1319-1471 3.64e-06

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 51.87  E-value: 3.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1319 LVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSSAVTVVGLL 1398
Cdd:PLN03223  1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENL 1373

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370468401 1399 MG-ISHQEEVF----ALDPVLGTFLILTSVILMVLVVINLFVSAILMAFGkERKSLKKEAALIDTllqKLSNLLGISW 1471
Cdd:PLN03223  1374 LGdITYFNEDLknltGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFG-EVKANAAETVSVHT---ELFPMLRDKW 1447
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 509-619 1.11e-04

PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Both types of enzymes are cytosolic but need this domain to access their sequestered membrane or micelle bound substrates.


Pssm-ID: 238851  Cd Length: 113  Bit Score: 43.07  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401  509 YLIQVYTGYRRSAATTAKVVITLYGSEGRSEPhHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSWYV 588
Cdd:cd01753      3 YKVTVATGSSLFAGTDDYIYLTLVGTAGESEK-QLLDRPGYDFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLFDAWFC 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1370468401  589 SQVIVCDMAvKRKWHFLCNCWLAvdlGDCEL 619
Cdd:cd01753     82 NYITVTGPG-GDEYHFPCYRWIE---GYGTL 108
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 1256-1450 1.92e-03

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 41.48  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1256 KWRFFTGKRNILDTSIILISFILLGLDMKSISLhkknmaryrddqdrfisfyeAVKVNSAathlvgFPVLLatvqLWNLL 1335
Cdd:pfam00520   60 KKRYFRSPWNILDFVVVLPSLISLVLSSVGSLS--------------------GLRVLRL------LRLLR----LLRLI 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468401 1336 RHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCS----------ISDYRTFFSSAVTVVGLLMGIS--- 1402
Cdd:pfam00520  110 RRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKlktwenpdngRTNFDNFPNAFLWLFQTMTTEGwgd 189

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1370468401 1403 -HQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAFGKERKSLK 1450
Cdd:pfam00520  190 iMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 567-624 5.81e-03

PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains consists of an eight stranded beta-barrel. In RabIP1 this domain may participate in lipid-mediated modulation of Rab6IP1's function via it's generally proposed function of mediating interaction with lipids or membrane bound proteins.


Pssm-ID: 238855  Cd Length: 114  Bit Score: 38.29  E-value: 5.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370468401  567 LGNLHSLRLWHDNSGVSPSWYVSQVIVCDMAVKRKWHFLCNCWL--AVDLGDCE---LDRVFI 624
Cdd:cd01757     52 LGKLTTVQIGHDNSGLLAKWLVEYVMVRNEITGHTYKFPCGRWLgeGVDDGNGEdgsLERVLV 114
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH