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Conserved domains on  [gi|697663146|ref|NP_001289302|]
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short transient receptor potential channel 7 isoform 3 precursor [Mus musculus]

Protein Classification

transient-receptor-potential channel family protein( domain architecture ID 1750128)

transient-receptor-potential ion channel protein conducts cations such as calcium into cells; belongs to the Transient Receptor Family (TC. 1.A.4)

Gene Ontology:  GO:0070588|GO:0005262|GO:0070679
PubMed:  20025796|18535090|20861159
SCOP:  4000366
TCDB:  1.A.4

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 1-437 1.91e-160

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


The actual alignment was detected with superfamily member TIGR00870:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 743  Bit Score: 472.26  E-value: 1.91e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146    1 MKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPnetftdypkqifRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPRE 80
Cdd:TIGR00870 350 IKFIFHSASYLYFLYLIIFTSVAYYRPTRTDL------------RVTGLQQTPLEMLIVTWVDGLRLGEEKLIWLGGIFE 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146   81 YVLHLWNLLDFGMLSIFVASFTARFMAFLKASEAqlyvdqyvqdvtlhnvslppevayFTYARDKWWPSDPQIISEGLYA 160
Cdd:TIGR00870 418 YIHQLWNILDFGMNSFYLATFLDRPFAILFVTQA------------------------FLVLREHWLRFDPTLIEEALFA 473

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  161 IAVVLSFSRIAYILPANESFGPLQISLGRTVK-DIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYN-------------- 225
Cdd:TIGR00870 474 FALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNecsnpharscekqg 553

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  226 PAFTTVEESFKTLFWSIFGLSEVisvvLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFA 305
Cdd:TIGR00870 554 NAYSTLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQ 629

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  306 RAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIKMCLIELCQSKAKRCENDLEMGMLNSKFRKTRyqagmrnsenlta 385
Cdd:TIGR00870 630 RAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKRQRWCRRVEEVNWTTWERKAETLIE------------- 696

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 697663146  386 nstfsKPTRYQKIMKRLIKRYVLKAQVDRENDEVNEGELKEIKQDISSLRYE 437
Cdd:TIGR00870 697 -----DGLHYQRVMKRLIKRYVLAEQRPRDDEGTTEEETKELKQDISSLRFE 743
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-437 1.91e-160

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: 472.26  E-value: 1.91e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146    1 MKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPnetftdypkqifRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPRE 80
Cdd:TIGR00870 350 IKFIFHSASYLYFLYLIIFTSVAYYRPTRTDL------------RVTGLQQTPLEMLIVTWVDGLRLGEEKLIWLGGIFE 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146   81 YVLHLWNLLDFGMLSIFVASFTARFMAFLKASEAqlyvdqyvqdvtlhnvslppevayFTYARDKWWPSDPQIISEGLYA 160
Cdd:TIGR00870 418 YIHQLWNILDFGMNSFYLATFLDRPFAILFVTQA------------------------FLVLREHWLRFDPTLIEEALFA 473

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  161 IAVVLSFSRIAYILPANESFGPLQISLGRTVK-DIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYN-------------- 225
Cdd:TIGR00870 474 FALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNecsnpharscekqg 553

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  226 PAFTTVEESFKTLFWSIFGLSEVisvvLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFA 305
Cdd:TIGR00870 554 NAYSTLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQ 629

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  306 RAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIKMCLIELCQSKAKRCENDLEMGMLNSKFRKTRyqagmrnsenlta 385
Cdd:TIGR00870 630 RAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKRQRWCRRVEEVNWTTWERKAETLIE------------- 696

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 697663146  386 nstfsKPTRYQKIMKRLIKRYVLKAQVDRENDEVNEGELKEIKQDISSLRYE 437
Cdd:TIGR00870 697 -----DGLHYQRVMKRLIKRYVLAEQRPRDDEGTTEEETKELKQDISSLRFE 743
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 52-299 2.62e-14

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: 72.30  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146   52 SWTEMLIMKWVLGMIWSECKEIWEEgPREYVLHLWNLLDFGMLSIFVASFTARFMAFlkaseaqlyvdqyvqdvtlhnvs 131
Cdd:pfam00520   2 RYFELFILLLILLNTIFLALETYFQ-PEEPLTTVLEILDYVFTGIFTLEMLLKIIAA----------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  132 lPPEVAYFtyaRDKWW--------PSDPQIISEGLYAIAV--VLSFSRIAYILPANESFGPLQI---SLGRTVKDIFKFM 198
Cdd:pfam00520  58 -GFKKRYF---RSPWNildfvvvlPSLISLVLSSVGSLSGlrVLRLLRLLRLLRLIRRLEGLRTlvnSLIRSLKSLGNLL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  199 VIFIMVFVAFMIGMFNLYSYYRGAKYNPA-----FTTVEESFKTLFWSIF--GLSEVISVVLKYDHKFIeniGYVLYGVY 271
Cdd:pfam00520 134 LLLLLFLFIFAIIGYQLFGGKLKTWENPDngrtnFDNFPNAFLWLFQTMTteGWGDIMYDTIDGKGEFW---AYIYFVSF 210

                         250       260
                  ....*....|....*....|....*...
gi 697663146  272 NVTMVVVLLNMLIAMINNSYQEIEEDAD 299
Cdd:pfam00520 211 IILGGFLLLNLFIAVIIDNFQELTERTE 238
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 158-298 4.93e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 52.64  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  158 LYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAF-MIG--MFNLYSyyrgakynPAFTTVEES 234
Cdd:PLN03223 1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYaFIGhvIFGNAS--------VHFSDMTDS 1365

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697663146  235 FKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDA 298
Cdd:PLN03223 1366 INSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFGEVKANA 1429
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 160-303 3.09e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146 160 AIAVVLSFSRIAYILPANESFGPLQISLGRTV-KDIFKFMVIFIMVFVAFMIGMFNLYsYYRGAKYNPAFTtveeSFKTL 238
Cdd:cd22192  427 SLALVLGWCNVMYFARGFQMLGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIF-QTEDPDSLGHFY----DFPMT 501

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697663146 239 FWSIFGLS-EVISVVLKYDHKfIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWK 303
Cdd:cd22192  502 LFSTFELFlGLIDGPANYTVD-LPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-437 1.91e-160

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: 472.26  E-value: 1.91e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146    1 MKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPnetftdypkqifRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPRE 80
Cdd:TIGR00870 350 IKFIFHSASYLYFLYLIIFTSVAYYRPTRTDL------------RVTGLQQTPLEMLIVTWVDGLRLGEEKLIWLGGIFE 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146   81 YVLHLWNLLDFGMLSIFVASFTARFMAFLKASEAqlyvdqyvqdvtlhnvslppevayFTYARDKWWPSDPQIISEGLYA 160
Cdd:TIGR00870 418 YIHQLWNILDFGMNSFYLATFLDRPFAILFVTQA------------------------FLVLREHWLRFDPTLIEEALFA 473

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  161 IAVVLSFSRIAYILPANESFGPLQISLGRTVK-DIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYN-------------- 225
Cdd:TIGR00870 474 FALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNecsnpharscekqg 553

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  226 PAFTTVEESFKTLFWSIFGLSEVisvvLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFA 305
Cdd:TIGR00870 554 NAYSTLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQ 629

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  306 RAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIKMCLIELCQSKAKRCENDLEMGMLNSKFRKTRyqagmrnsenlta 385
Cdd:TIGR00870 630 RAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKRQRWCRRVEEVNWTTWERKAETLIE------------- 696

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 697663146  386 nstfsKPTRYQKIMKRLIKRYVLKAQVDRENDEVNEGELKEIKQDISSLRYE 437
Cdd:TIGR00870 697 -----DGLHYQRVMKRLIKRYVLAEQRPRDDEGTTEEETKELKQDISSLRFE 743
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 52-299 2.62e-14

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: 72.30  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146   52 SWTEMLIMKWVLGMIWSECKEIWEEgPREYVLHLWNLLDFGMLSIFVASFTARFMAFlkaseaqlyvdqyvqdvtlhnvs 131
Cdd:pfam00520   2 RYFELFILLLILLNTIFLALETYFQ-PEEPLTTVLEILDYVFTGIFTLEMLLKIIAA----------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  132 lPPEVAYFtyaRDKWW--------PSDPQIISEGLYAIAV--VLSFSRIAYILPANESFGPLQI---SLGRTVKDIFKFM 198
Cdd:pfam00520  58 -GFKKRYF---RSPWNildfvvvlPSLISLVLSSVGSLSGlrVLRLLRLLRLLRLIRRLEGLRTlvnSLIRSLKSLGNLL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  199 VIFIMVFVAFMIGMFNLYSYYRGAKYNPA-----FTTVEESFKTLFWSIF--GLSEVISVVLKYDHKFIeniGYVLYGVY 271
Cdd:pfam00520 134 LLLLLFLFIFAIIGYQLFGGKLKTWENPDngrtnFDNFPNAFLWLFQTMTteGWGDIMYDTIDGKGEFW---AYIYFVSF 210

                         250       260
                  ....*....|....*....|....*...
gi 697663146  272 NVTMVVVLLNMLIAMINNSYQEIEEDAD 299
Cdd:pfam00520 211 IILGGFLLLNLFIAVIIDNFQELTERTE 238
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 49-294 2.42e-09

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: 57.29  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146   49 TQFSWTEMLIMKWVLGMI----WSECKEIWEEGPReYVLHLWNLLDFGMLSIFVASFTARFM-AFLKASEAQLYVDQYVQ 123
Cdd:pfam08016   4 TNRSLFILLCEIVFVVFFlyfvVEEILKIRKHRPS-YLRSVWNLLDLAIVILSVVLIVLNIYrDFLADRLIKSVEASPVT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  124 DVTLHNVSlppevayftyardKWwpsdpQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIM 203
Cdd:pfam08016  83 FIDFDRVA-------------QL-----DNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  204 VFVAFMIGMFNLYSyyrgaKYNPAFTTVEESFKTLF---WSIFGLSEVISVVlkydhkfiENIGYVLYGVYNVTMVVVLL 280
Cdd:pfam08016 145 FFFAYAQFGYLLFG-----TQAPNFSNFVKSILTLFrtiLGDFGYNEIFSGN--------RVLGPLLFLTFVFLVIFILL 211

                         250
                  ....*....|....
gi 697663146  281 NMLIAMINNSYQEI 294
Cdd:pfam08016 212 NLFLAIINDSYVEV 225
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 158-298 4.93e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 52.64  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146  158 LYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAF-MIG--MFNLYSyyrgakynPAFTTVEES 234
Cdd:PLN03223 1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYaFIGhvIFGNAS--------VHFSDMTDS 1365

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 697663146  235 FKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDA 298
Cdd:PLN03223 1366 INSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFGEVKANA 1429
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 160-303 3.09e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146 160 AIAVVLSFSRIAYILPANESFGPLQISLGRTV-KDIFKFMVIFIMVFVAFMIGMFNLYsYYRGAKYNPAFTtveeSFKTL 238
Cdd:cd22192  427 SLALVLGWCNVMYFARGFQMLGPFTIMIQKIIfGDLMKFCWLMFVVILGFSSAFYMIF-QTEDPDSLGHFY----DFPMT 501

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 697663146 239 FWSIFGLS-EVISVVLKYDHKfIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWK 303
Cdd:cd22192  502 LFSTFELFlGLIDGPANYTVD-LPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 162-307 4.24e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146 162 AVVLSFSRIAYILPANESFGPLQISLGRTV-KDIFKFMVIFIMVFVAFMIGmfnLYSYYRGAKYN--PAFTTVEESFKTL 238
Cdd:cd21882  414 SLVLGWCNVLYYTRGFQMLGIYTVMIQKMIlRDLMRFCWVYLVFLFGFASA---FVILFQTEDPNklGEFRDYPDALLEL 490

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697663146 239 FWSIFGLSEvISVVLKYDHKFIENIgyvLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARA 307
Cdd:cd21882  491 FKFTIGMGD-LPFNENVDFPFVYLI---LLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQKA 555
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 192-330 4.87e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.39  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697663146 192 KDIFKFMVIFIMVFVAFMIGmfnLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISvvlkyDHKFIENIGY-----V 266
Cdd:cd22193  450 RDLLRFLFVYLLFLFGFAVA---LVSLIEKCSSDKKDCSSYGSFSDAVLELFKLTIGMG-----DLEFQENSTYpavflI 521

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 697663146 267 LYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWL-----------SYFDEGRTLPAPFNLVPSP 330
Cdd:cd22193  522 LLLTYVILTFVLLLNMLIALMGETVNNVSKESKRIWKLQRAITILefeksfpecmrKAFRSGRLLKVGLCKDGTP 596
 
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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