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Conserved domains on  [gi|34485553|gb|AAQ73173|]
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polycystic kidney disease 1-like 2 short form [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
 705-824 5.55e-66

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: 218.68  E-value: 5.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  705 YHYLVTVYTGHRRGAATSSKVTVTLYGLDGEREPHHLADPDTPVFERGAVDAFLLSTLFPLGELRSLRLWHDNSGDRPSW 784
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 34485553  785 YVSRVLVYDLVMDRKWYFLCNSWLSINVGDCVLDKVFPVA 824
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
Polycystin_dom super family cl48672
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 1302-1491 7.40e-50

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


The actual alignment was detected with superfamily member pfam20519:

Pssm-ID: 466668  Cd Length: 199  Bit Score: 175.69  E-value: 7.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1302 GFSGVLGFREFFKWANTTLVSNLY-----GHPPGFITDGNSKLVGSAQIRQVRVRESSCPLAQQLQASLNGCRTPYSLDA 1376
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHsnktpSGLPGSFIAYESLLLGVPRLRQLRVRNSSCLVHDKFVREINECHAGYSPPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1377 EDMADYGEGWNA----TTLSAWQYQSQDQRQGYPIWGKLTVYRGGGYVVPLGTDRQSTSRIIRYLFDNTWLDALTRAVFV 1452
Cdd:pfam20519   81 EDRKLYSALPYKpvhyGSKYWFIYTPPGLLMGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 34485553   1453 EFTVYNANVNLFCIVTLTLETSALGTFFTHAALQSLRLY 1491
Cdd:pfam20519  161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel super family cl37568
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1493-1715 1.05e-38

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: 144.73  E-value: 1.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1493 FTDGWHPFVVAAELIYFLFLLYYMGVQGKRMRKETWGYFCSKWNLLELAIILASWSALAVFVKRAVLAERDLQRCRNHRE 1572
Cdd:pfam08016    2 YVTNRSLFILLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1573 EGISFSETAAADAALGYIIAFLVLLSTVKLWHLLRLNPKMNMITAALRRAWGDISGFMIVILTMLLAYSIASNLIFGWKL 1652
Cdd:pfam08016   82 TFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQA 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34485553   1653 RSYKTLFDAAETMVSLQLGIFNYEEVLDYSPVLGSFLIGSCIVFMTFVVLNLFISVILVAFSE 1715
Cdd:pfam08016  162 PNFSNFVKSILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSYVE 224
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 595-634 3.40e-11

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: 59.71  E-value: 3.40e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 34485553     595 SHCVFWDEVQETWDDSGCQVGPRTSpYQTHCLCNHLTFFG 634
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFA 41
REJ super family cl28747
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 38-216 1.51e-08

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


The actual alignment was detected with superfamily member pfam02010:

Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 59.05  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553     38 SLTLLQSNTST------LLLNSSFLQSrGEVIRIRATALTRHAYGEDT---YVISTVPPREVPaCTIAPEEGTVL-TSFA 107
Cdd:pfam02010  255 VLDQLNSQTSTgrsgpyLVIKAGVLQS-GVSYRFTLIVTVYPGLVSGLasiSFITNAPPTGGT-CSVTPTEGTALeTKFT 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553    108 IFCNAST-ALGPLEFCFCL-------ESGSCLHCGPEPALPSVYLPLGEENNDFVLTVVISATNRAGDTQQTQAMAKVAL 179
Cdd:pfam02010  333 VTCQGWTdDDLPLTYQFGDisfreasEEWFLLYEGSSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATSVSLTITVTP 412

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 34485553    180 GDTCVEDVAFQAAVSEKIPTALQGeGGPEQLLQLAKA 216
Cdd:pfam02010  413 PSSSDELLYFLLGTTSDLSALLQS-GDPQQAAQLILA 448
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 705-824 5.55e-66

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: 218.68  E-value: 5.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  705 YHYLVTVYTGHRRGAATSSKVTVTLYGLDGEREPHHLADPDTPVFERGAVDAFLLSTLFPLGELRSLRLWHDNSGDRPSW 784
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 34485553  785 YVSRVLVYDLVMDRKWYFLCNSWLSINVGDCVLDKVFPVA 824
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 1302-1491 7.40e-50

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 175.69  E-value: 7.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1302 GFSGVLGFREFFKWANTTLVSNLY-----GHPPGFITDGNSKLVGSAQIRQVRVRESSCPLAQQLQASLNGCRTPYSLDA 1376
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHsnktpSGLPGSFIAYESLLLGVPRLRQLRVRNSSCLVHDKFVREINECHAGYSPPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1377 EDMADYGEGWNA----TTLSAWQYQSQDQRQGYPIWGKLTVYRGGGYVVPLGTDRQSTSRIIRYLFDNTWLDALTRAVFV 1452
Cdd:pfam20519   81 EDRKLYSALPYKpvhyGSKYWFIYTPPGLLMGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 34485553   1453 EFTVYNANVNLFCIVTLTLETSALGTFFTHAALQSLRLY 1491
Cdd:pfam20519  161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1493-1715 1.05e-38

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: 144.73  E-value: 1.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1493 FTDGWHPFVVAAELIYFLFLLYYMGVQGKRMRKETWGYFCSKWNLLELAIILASWSALAVFVKRAVLAERDLQRCRNHRE 1572
Cdd:pfam08016    2 YVTNRSLFILLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1573 EGISFSETAAADAALGYIIAFLVLLSTVKLWHLLRLNPKMNMITAALRRAWGDISGFMIVILTMLLAYSIASNLIFGWKL 1652
Cdd:pfam08016   82 TFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQA 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34485553   1653 RSYKTLFDAAETMVSLQLGIFNYEEVLDYSPVLGSFLIGSCIVFMTFVVLNLFISVILVAFSE 1715
Cdd:pfam08016  162 PNFSNFVKSILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSYVE 224
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 707-809 1.04e-22

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: 94.81  E-value: 1.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553    707 YLVTVYTGHRRGAATSSKVTVTLYGLDGE--REPHHLADPDtpvFERGAVDAFLLSTLFPLGELRSLRLWHDNSGDRPSW 784
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGEsaQLEITLDNPD---FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100
                   ....*....|....*....|....*.
gi 34485553    785 YVSRVLVYDLVMD-RKWYFLCNSWLS 809
Cdd:pfam01477   78 FLKSITVEVPGETgGKYTFPCNSWVY 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
705-809 2.11e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 70.75  E-value: 2.11e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553     705 YHYLVTVYTGHRRGAATSSKVTVTLYGLDGEREPHHLADPDTPVFERGAVDAFLLSTLFPLGELRSLRLWHDNsgDRPSW 784
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEH--RHPEW 78

                            90       100
                    ....*....|....*....|....*
gi 34485553     785 YVSRVLVYDLVMDRKWYFLCNSWLS 809
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVY 103
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 595-634 3.40e-11

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: 59.71  E-value: 3.40e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 34485553     595 SHCVFWDEVQETWDDSGCQVGPRTSpYQTHCLCNHLTFFG 634
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFA 41
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 596-634 7.54e-11

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


Pssm-ID: 460350  Cd Length: 44  Bit Score: 58.47  E-value: 7.54e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 34485553    596 HCVFWDEVQET---WDDSGCQVGPRTSpYQTHCLCNHLTFFG 634
Cdd:pfam01825    2 QCVFWDFTNSTtgrWSTEGCTTVSLND-THTVCSCNHLTSFA 42
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 38-216 1.51e-08

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 59.05  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553     38 SLTLLQSNTST------LLLNSSFLQSrGEVIRIRATALTRHAYGEDT---YVISTVPPREVPaCTIAPEEGTVL-TSFA 107
Cdd:pfam02010  255 VLDQLNSQTSTgrsgpyLVIKAGVLQS-GVSYRFTLIVTVYPGLVSGLasiSFITNAPPTGGT-CSVTPTEGTALeTKFT 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553    108 IFCNAST-ALGPLEFCFCL-------ESGSCLHCGPEPALPSVYLPLGEENNDFVLTVVISATNRAGDTQQTQAMAKVAL 179
Cdd:pfam02010  333 VTCQGWTdDDLPLTYQFGDisfreasEEWFLLYEGSSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATSVSLTITVTP 412

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 34485553    180 GDTCVEDVAFQAAVSEKIPTALQGeGGPEQLLQLAKA 216
Cdd:pfam02010  413 PSSSDELLYFLLGTTSDLSALLQS-GDPQQAAQLILA 448
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 1436-1732 2.44e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 56.10  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  1436 YLFD--------NTWLDAL----------TRAVFVEFTVYNANVNLFCIVTLTLETSALGTFFTHAALQSLR--LYPFTD 1495
Cdd:PLN03223 1092 YFFDinlsaaeaQTWLDYMiyglmiddvkTRKVTAQVVVYNAELGYFGNVMVFFEFTDGGKIEVTHRLNTIRveLYETYE 1171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  1496 GWHPFvvAAEL---IYFLFLLYYMGVQ---GKRMRKETWGYFCSKWNLLELAII-----------LASWSALAVF----- 1553
Cdd:PLN03223 1172 DWVRF--AMEIllaIGAVYSVYEEAMDfgsSKKTRGSYLAYFLSGWNYVDFASIglhlatimmwfVFSWSYARAFepdih 1249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  1554 --VKRAVLAERDLQRCRNHREegisFSETAAADAALGYIIAFL----------VLLSTVKLWHLLRLNPKMNMITAALRR 1621
Cdd:PLN03223 1250 ydIYKNLSASANFTALRIPNE----LPEMNDMFLEMKNLVDYFqwymtlsginIILLLGRILKLMDFQPRLGVITRTLWL 1325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  1622 AWGDISGFMIVILTMLLAYSIASNLIFGWKLRSYKTLFDAAETMVSLQLGifNYEEVLDYSPVLG--SFLIG-------S 1692
Cdd:PLN03223 1326 AGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENLLG--DITYFNEDLKNLTglQFVVGmiyfysyN 1403

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 34485553  1693 CIVFMtfVVLNLFISVILVAFSE--EQKYYQLSEEGEIVDLL 1732
Cdd:PLN03223 1404 IFVFM--ILFNFLLAIICDAFGEvkANAAETVSVHTELFPML 1443
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1497-1709 1.49e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1497 WHPFV----VAAELIYFLFLL------YY---------MGVQGKR--MRKETWG------------------YFCSKWNL 1537
Cdd:TIGR00870  346 WKPFIkfifHSASYLYFLYLIiftsvaYYrptrtdlrvTGLQQTPleMLIVTWVdglrlgeekliwlggifeYIHQLWNI 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1538 LE-------LAIILASWSAlAVFVKRAVLAERDLQRCrnhreegisFSETAAADAALgyiiAFLVLLSTVKLWHLLRLNP 1610
Cdd:TIGR00870  426 LDfgmnsfyLATFLDRPFA-ILFVTQAFLVLREHWLR---------FDPTLIEEALF----AFALVLSWLNLLYIFRGNQ 491

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1611 KMNMITAALRRA-WGDISGFMIVILTMLLAYSIASNLIF-------------------GWKLRSYKTLFdaaETMVSLQL 1670
Cdd:TIGR00870  492 HLGPLQIMIGRMiLGDILRFLFIYAVVLFGFACGLNQLYqyydelklnecsnpharscEKQGNAYSTLF---ETSQELFW 568

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 34485553   1671 GIFNYEEVLDYS----PVLGSFLIGSCIVFMTFVVLNLFISVI 1709
Cdd:TIGR00870  569 AIIGLGDLLANEhkftEFVGLLLFGAYNVIMYILLLNMLIAMM 611
 
Name Accession Description Interval E-value
PLAT_polycystin cd01752
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ...
 705-824 5.55e-66

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: 218.68  E-value: 5.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  705 YHYLVTVYTGHRRGAATSSKVTVTLYGLDGEREPHHLADPDTPVFERGAVDAFLLSTLFPLGELRSLRLWHDNSGDRPSW 784
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 34485553  785 YVSRVLVYDLVMDRKWYFLCNSWLSINVGDCVLDKVFPVA 824
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTFPVA 120
Polycystin_dom pfam20519
Polycystin domain; This domain represents the polycystin domain from group II of Transient ...
 1302-1491 7.40e-50

Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other.


Pssm-ID: 466668  Cd Length: 199  Bit Score: 175.69  E-value: 7.40e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1302 GFSGVLGFREFFKWANTTLVSNLY-----GHPPGFITDGNSKLVGSAQIRQVRVRESSCPLAQQLQASLNGCRTPYSLDA 1376
Cdd:pfam20519    1 GLLTVTDLDDIWDWLSSVLLPALHsnktpSGLPGSFIAYESLLLGVPRLRQLRVRNSSCLVHDKFVREINECHAGYSPPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1377 EDMADYGEGWNA----TTLSAWQYQSQDQRQGYPIWGKLTVYRGGGYVVPLGTDRQSTSRIIRYLFDNTWLDALTRAVFV 1452
Cdd:pfam20519   81 EDRKLYSALPYKpvhyGSKYWFIYTPPGLLMGYDHWGHLASYPSGGYVVLLPSSREESLKRLAYLQDNNWLDRGTRAVFV 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 34485553   1453 EFTVYNANVNLFCIVTLTLETSALGTFFTHAALQSLRLY 1491
Cdd:pfam20519  161 DFTLYNADINLFCVVTLRVEFPPTGGVLPSPSVQSVKLL 199
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 1493-1715 1.05e-38

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: 144.73  E-value: 1.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1493 FTDGWHPFVVAAELIYFLFLLYYMGVQGKRMRKETWGYFCSKWNLLELAIILASWSALAVFVKRAVLAERDLQRCRNHRE 1572
Cdd:pfam08016    2 YVTNRSLFILLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1573 EGISFSETAAADAALGYIIAFLVLLSTVKLWHLLRLNPKMNMITAALRRAWGDISGFMIVILTMLLAYSIASNLIFGWKL 1652
Cdd:pfam08016   82 TFIDFDRVAQLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQA 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34485553   1653 RSYKTLFDAAETMVSLQLGIFNYEEVLDYSPVLGSFLIGSCIVFMTFVVLNLFISVILVAFSE 1715
Cdd:pfam08016  162 PNFSNFVKSILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSYVE 224
PLAT_repeat cd01756
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ...
 707-824 1.14e-28

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: 111.88  E-value: 1.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  707 YLVTVYTGHRRGAATSSKVTVTLYGLDGEREPHHLADPDTPV-FERGAVDAFLLSTLFpLGELRSLRLWHDNSGDRPSWY 785
Cdd:cd01756    3 YEVTVKTGDVKGAGTDANVFITLYGENGDTGKRKLKKSNNKNkFERGQTDKFTVEAVD-LGKLKKIRIGHDNSGLGAGWF 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 34485553  786 VSRVLVYDLVMDRKWYFLCNSWLSINVGDCVLDKVFPVA 824
Cdd:cd01756   82 LDKVEIREPGTGDEYTFPCNRWLDKDEDDGQIVRELYPS 120
PLAT cd00113
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ...
 705-809 8.04e-23

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: 95.10  E-value: 8.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  705 YHYLVTVYTGHRRGAATSSKVTVTLYGLDGEREPH-HLADPDTpvFERGAVDAFLLSTLFPLGELRSLRLWHDNSGDRPS 783
Cdd:cd00113    1 CRYTVTIKTGDKKGAGTDSNISLALYGENGNSSDIpILDGPGS--FERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDG 78

                         90       100
                 ....*....|....*....|....*.
gi 34485553  784 WYVSRVLVYDLVMDRKWYFLCNSWLS 809
Cdd:cd00113   79 WYCESITVQALGTKKVYTFPVNRWVL 104
PLAT pfam01477
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ...
 707-809 1.04e-22

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: 94.81  E-value: 1.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553    707 YLVTVYTGHRRGAATSSKVTVTLYGLDGE--REPHHLADPDtpvFERGAVDAFLLSTLFPLGELRSLRLWHDNSGDRPSW 784
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGEsaQLEITLDNPD---FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100
                   ....*....|....*....|....*.
gi 34485553    785 YVSRVLVYDLVMD-RKWYFLCNSWLS 809
Cdd:pfam01477   78 FLKSITVEVPGETgGKYTFPCNSWVY 103
LH2 smart00308
Lipoxygenase homology 2 (beta barrel) domain;
705-809 2.11e-14

Lipoxygenase homology 2 (beta barrel) domain;


Pssm-ID: 214608 [Multi-domain]  Cd Length: 105  Bit Score: 70.75  E-value: 2.11e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553     705 YHYLVTVYTGHRRGAATSSKVTVTLYGLDGEREPHHLADPDTPVFERGAVDAFLLSTLFPLGELRSLRLWHDNsgDRPSW 784
Cdd:smart00308    1 GKYKVTVTTGGLDFAGTTASVSLSLVGAEGDGKESKLDYLFKGIFARGSTYEFTFDVDEDFGELGAVKIKNEH--RHPEW 78

                            90       100
                    ....*....|....*....|....*
gi 34485553     785 YVSRVLVYDLVMDRKWYFLCNSWLS 809
Cdd:smart00308   79 FLKSITVKDLPTGGKYHFPCNSWVY 103
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 1528-1721 4.55e-13

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: 70.76  E-value: 4.55e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1528 WGYFCSKWNLLELAIILASWSALAVFVKRAvlaerdlqrcrnhreegisfsetaaadaalGYIIAFLVLLSTVKLWHLLR 1607
Cdd:pfam00520   61 KRYFRSPWNILDFVVVLPSLISLVLSSVGS------------------------------LSGLRVLRLLRLLRLLRLIR 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1608 LNPKMNMITAALRRAWGDISGFMIVILTMLLAYSIASNLIFGWKLR----------SYKTLFDAAETMVSLQLGIfNYEE 1677
Cdd:pfam00520  111 RLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKtwenpdngrtNFDNFPNAFLWLFQTMTTE-GWGD 189

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 34485553   1678 VLD-----YSPVLGSFLIGSCIVFMTFVVLNLFISVILVAFSEEQKYYQ 1721
Cdd:pfam00520  190 IMYdtidgKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
GPS smart00303
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ...
 595-634 3.40e-11

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: 59.71  E-value: 3.40e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 34485553     595 SHCVFWDEVQETWDDSGCQVGPRTSpYQTHCLCNHLTFFG 634
Cdd:smart00303    3 PICVFWDESSGEWSTRGCELLETNG-THTTCSCNHLTTFA 41
GPS pfam01825
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ...
 596-634 7.54e-11

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


Pssm-ID: 460350  Cd Length: 44  Bit Score: 58.47  E-value: 7.54e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 34485553    596 HCVFWDEVQET---WDDSGCQVGPRTSpYQTHCLCNHLTFFG 634
Cdd:pfam01825    2 QCVFWDFTNSTtgrWSTEGCTTVSLND-THTVCSCNHLTSFA 42
PLAT_plant_stress cd01754
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ...
 707-811 5.08e-09

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: 56.01  E-value: 5.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  707 YLVTVYTGHRRGAATSSKVTVTLYGLDGE-------REPHHLADPDTPVFERGAVDAFLLSTLFPLGELRSLRLWHDNSG 779
Cdd:cd01754    3 YTIYVQTGSIWKAGTDSRISLQIYDADGPglrianlEAWGGLMGAGHDYFERGNLDRFSGRGPCLPSPPCWMNLTSDGTG 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 34485553  780 DRPSWYVSRVLVYDL-----VMDRKWYFlcNSWLSIN 811
Cdd:cd01754   83 NHPGWYVNYVEVTQAgqhapCMQHLFAV--EQWLATD 117
REJ pfam02010
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...
 38-216 1.51e-08

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.


Pssm-ID: 366875 [Multi-domain]  Cd Length: 448  Bit Score: 59.05  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553     38 SLTLLQSNTST------LLLNSSFLQSrGEVIRIRATALTRHAYGEDT---YVISTVPPREVPaCTIAPEEGTVL-TSFA 107
Cdd:pfam02010  255 VLDQLNSQTSTgrsgpyLVIKAGVLQS-GVSYRFTLIVTVYPGLVSGLasiSFITNAPPTGGT-CSVTPTEGTALeTKFT 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553    108 IFCNAST-ALGPLEFCFCL-------ESGSCLHCGPEPALPSVYLPLGEENNDFVLTVVISATNRAGDTQQTQAMAKVAL 179
Cdd:pfam02010  333 VTCQGWTdDDLPLTYQFGDisfreasEEWFLLYEGSSQISISTFLPPGLPANDYQVTVVVVVYDSLGAATSVSLTITVTP 412

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 34485553    180 GDTCVEDVAFQAAVSEKIPTALQGeGGPEQLLQLAKA 216
Cdd:pfam02010  413 PSSSDELLYFLLGTTSDLSALLQS-GDPQQAAQLILA 448
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 1436-1732 2.44e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 56.10  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  1436 YLFD--------NTWLDAL----------TRAVFVEFTVYNANVNLFCIVTLTLETSALGTFFTHAALQSLR--LYPFTD 1495
Cdd:PLN03223 1092 YFFDinlsaaeaQTWLDYMiyglmiddvkTRKVTAQVVVYNAELGYFGNVMVFFEFTDGGKIEVTHRLNTIRveLYETYE 1171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  1496 GWHPFvvAAEL---IYFLFLLYYMGVQ---GKRMRKETWGYFCSKWNLLELAII-----------LASWSALAVF----- 1553
Cdd:PLN03223 1172 DWVRF--AMEIllaIGAVYSVYEEAMDfgsSKKTRGSYLAYFLSGWNYVDFASIglhlatimmwfVFSWSYARAFepdih 1249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  1554 --VKRAVLAERDLQRCRNHREegisFSETAAADAALGYIIAFL----------VLLSTVKLWHLLRLNPKMNMITAALRR 1621
Cdd:PLN03223 1250 ydIYKNLSASANFTALRIPNE----LPEMNDMFLEMKNLVDYFqwymtlsginIILLLGRILKLMDFQPRLGVITRTLWL 1325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  1622 AWGDISGFMIVILTMLLAYSIASNLIFGWKLRSYKTLFDAAETMVSLQLGifNYEEVLDYSPVLG--SFLIG-------S 1692
Cdd:PLN03223 1326 AGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENLLG--DITYFNEDLKNLTglQFVVGmiyfysyN 1403

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 34485553  1693 CIVFMtfVVLNLFISVILVAFSE--EQKYYQLSEEGEIVDLL 1732
Cdd:PLN03223 1404 IFVFM--ILFNFLLAIICDAFGEvkANAAETVSVHTELFPML 1443
PLAT_LOX cd01753
PLAT domain of 12/15-lipoxygenase. As a unique subfamily of the mammalian lipoxygenases, they ...
 707-817 3.26e-06

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: 47.69  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553  707 YLVTVYTGHRRGAATSSKVTVTLYGLDGEREPHHLADPdTPVFERGAVDAFLLSTLFPLGELRSLRLWHDNSGDRPSWYV 786
Cdd:cd01753    3 YKVTVATGSSLFAGTDDYIYLTLVGTAGESEKQLLDRP-GYDFERGAVDEYKVKVPEDLGELLLVRLRKRKYLLFDAWFC 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 34485553  787 SRVLVYDLVMDRKWyFLCNSWLsinVGDCVL 817
Cdd:cd01753   82 NYITVTGPGGDEYH-FPCYRWI---EGYGTL 108
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1497-1709 1.49e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1497 WHPFV----VAAELIYFLFLL------YY---------MGVQGKR--MRKETWG------------------YFCSKWNL 1537
Cdd:TIGR00870  346 WKPFIkfifHSASYLYFLYLIiftsvaYYrptrtdlrvTGLQQTPleMLIVTWVdglrlgeekliwlggifeYIHQLWNI 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1538 LE-------LAIILASWSAlAVFVKRAVLAERDLQRCrnhreegisFSETAAADAALgyiiAFLVLLSTVKLWHLLRLNP 1610
Cdd:TIGR00870  426 LDfgmnsfyLATFLDRPFA-ILFVTQAFLVLREHWLR---------FDPTLIEEALF----AFALVLSWLNLLYIFRGNQ 491

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34485553   1611 KMNMITAALRRA-WGDISGFMIVILTMLLAYSIASNLIF-------------------GWKLRSYKTLFdaaETMVSLQL 1670
Cdd:TIGR00870  492 HLGPLQIMIGRMiLGDILRFLFIYAVVLFGFACGLNQLYqyydelklnecsnpharscEKQGNAYSTLF---ETSQELFW 568

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 34485553   1671 GIFNYEEVLDYS----PVLGSFLIGSCIVFMTFVVLNLFISVI 1709
Cdd:TIGR00870  569 AIIGLGDLLANEhkftEFVGLLLFGAYNVIMYILLLNMLIAMM 611
PLAT_RAB6IP1 cd01757
PLAT/LH2 domain present in RAB6 interacting protein 1 (Rab6IP1)_like family. PLAT/LH2 domains ...
 765-818 3.39e-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: 39.06  E-value: 3.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 34485553  765 LGELRSLRLWHDNSGDRPSWYVSRVLVYDLVMDRKWYFLCNSWLSINVGDCVLD 818
Cdd:cd01757   52 LGKLTTVQIGHDNSGLLAKWLVEYVMVRNEITGHTYKFPCGRWLGEGVDDGNGE 105
 
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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