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Conserved domains on  [gi|209863032|ref|NP_001129430|]
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short transient receptor potential channel 4 isoform zeta [Homo sapiens]

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

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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 ...
 17-576 0e+00

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: 678.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032   17 RIPLRIVRA-ESELSPSEKAYLNAVEKGDYASVKKSLEEAEiyfKININCIDPLGRTALLIAIENENLELIELLLSFN-- 93
Cdd:TIGR00870   1 RGPLDIVPAeESPLSDEEKAFLPAAERGDLASVYRDLEEPK---KLNINCPDRLGRSALFVAAIENENLELTELLLNLsc 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032   94 -VYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQ---------------------------------------------- 126
Cdd:TIGR00870  78 rGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSgplelandqytseftpgitalhlaahrqnyeivklllergasvpar 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032      --------------------------------------------------------------------------------
Cdd:TIGR00870 158 acgdffvksqgvdsfyhgesplnaaaclgspsivallsedpadiltadslgntllhllvmenefkaeyeelscqmynfal 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  127 ------------------------------------------------FVAQPNCQQLLASRWYDEFPGWRRRHWAVKMV 158
Cdd:TIGR00870 238 slldklrdskelevilnhqgltplklaakegrivlfrlklaikykqkkFVAWPNGQQLLSLYWLEELDGWRRKQSVLELI 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  159 TCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDR---SDLNRQGPPPTIVEWMILP 235
Cdd:TIGR00870 318 VVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRptrTDLRVTGLQQTPLEMLIVT 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  236 WVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFAIANI 313
Cdd:TIGR00870 398 WVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFAFALV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  314 FSSLRLISLFTANSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGI---RCEKQNNAFS 389
Cdd:TIGR00870 478 LSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQGNAYS 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  390 TLFETLQSLFWSIFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKL 469
Cdd:TIGR00870 558 TLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKL 633

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  470 WMSYFEEGGTLPTPFNVIPSPKSLWYLIKWIWTHLCKK---KMRRKPESFGTIGRRAADNLRRH-HQYQEVMRNLVKRYV 545
Cdd:TIGR00870 634 WMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTWERKAETLIEDgLHYQRVMKRLIKRYV 713

                         730       740       750
                  ....*....|....*....|....*....|.
gi 209863032  546 AAMIRDAKtEEGLTEENFKELKQDISSFRFE 576
Cdd:TIGR00870 714 LAEQRPRD-DEGTTEEETKELKQDISSLRFE 743
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 17-576 0e+00

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: 678.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032   17 RIPLRIVRA-ESELSPSEKAYLNAVEKGDYASVKKSLEEAEiyfKININCIDPLGRTALLIAIENENLELIELLLSFN-- 93
Cdd:TIGR00870   1 RGPLDIVPAeESPLSDEEKAFLPAAERGDLASVYRDLEEPK---KLNINCPDRLGRSALFVAAIENENLELTELLLNLsc 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032   94 -VYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQ---------------------------------------------- 126
Cdd:TIGR00870  78 rGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSgplelandqytseftpgitalhlaahrqnyeivklllergasvpar 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032      --------------------------------------------------------------------------------
Cdd:TIGR00870 158 acgdffvksqgvdsfyhgesplnaaaclgspsivallsedpadiltadslgntllhllvmenefkaeyeelscqmynfal 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  127 ------------------------------------------------FVAQPNCQQLLASRWYDEFPGWRRRHWAVKMV 158
Cdd:TIGR00870 238 slldklrdskelevilnhqgltplklaakegrivlfrlklaikykqkkFVAWPNGQQLLSLYWLEELDGWRRKQSVLELI 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  159 TCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDR---SDLNRQGPPPTIVEWMILP 235
Cdd:TIGR00870 318 VVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRptrTDLRVTGLQQTPLEMLIVT 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  236 WVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFAIANI 313
Cdd:TIGR00870 398 WVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFAFALV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  314 FSSLRLISLFTANSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGI---RCEKQNNAFS 389
Cdd:TIGR00870 478 LSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQGNAYS 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  390 TLFETLQSLFWSIFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKL 469
Cdd:TIGR00870 558 TLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKL 633

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  470 WMSYFEEGGTLPTPFNVIPSPKSLWYLIKWIWTHLCKK---KMRRKPESFGTIGRRAADNLRRH-HQYQEVMRNLVKRYV 545
Cdd:TIGR00870 634 WMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTWERKAETLIEDgLHYQRVMKRLIKRYV 713

                         730       740       750
                  ....*....|....*....|....*....|.
gi 209863032  546 AAMIRDAKtEEGLTEENFKELKQDISSFRFE 576
Cdd:TIGR00870 714 LAEQRPRD-DEGTTEEETKELKQDISSLRFE 743
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 222-459 1.41e-25

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: 106.20  E-value: 1.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  222 QGPPPTIVEWMILPWVLGFIWGEIKQMWDGGLQD-YIHDWWNLMDFVMNSLYLATISLKIVAfvkysalnpreswdmwhp 300
Cdd:pfam00520  28 EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKrYFRSPWNILDFVVVLPSLISLVLSSVG------------------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  301 tlvaeaLFAIANIFSSLRLISLFTANSHLGPLQI---SLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETkgltck 377
Cdd:pfam00520  90 ------SLSGLRVLRLLRLLRLLRLIRRLEGLRTlvnSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKT------ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  378 GIRCEKQNNAFSTLFETLQSLFWSIF--GLINLYVTNVKAQHEFtefVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIA 455
Cdd:pfam00520 158 WENPDNGRTNFDNFPNAFLWLFQTMTteGWGDIMYDTIDGKGEF---WAYIYFVSFIILGGFLLLNLFIAVIIDNFQELT 234


                  ....
gi 209863032  456 DHAD 459
Cdd:pfam00520 235 ERTE 238
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 328-466 5.39e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 62.90  E-value: 5.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 328 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYfyyEETK-----GLTCKGIRCEKQNNAFSTLFETLQSLFWS 401
Cdd:cd22196  453 QMGIYSVMIQKMILrDICRFLFVYLVFLFGFSAALVTLI---EDGPpkgdvNTSQKECVCKSGYNSYNSLYSTCLELFKF 529

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209863032 402 IFGLINLYVT-NVKAQHEFTefvgaTMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 466
Cdd:cd22196  530 TIGMGDLEFTeNYKFKEVFI-----FLLISYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQR 590
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 236-451 1.37e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 55.33  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  236 WVLGFIWGEIKQMWD-----GGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKY-SALNPRESWDMWHpTLVAEALF- 308
Cdd:PLN03223 1185 GAVYSVYEEAMDFGSskktrGSYLAYFLSGWNYVDFASIGLHLATIMMWFVFSWSYaRAFEPDIHYDIYK-NLSASANFt 1263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  309 ---------AIANIFSSLR-LISLFTANSHLGPLQISL--GRML--------------------LDILKFLFIYCLVLLA 356
Cdd:PLN03223 1264 alripnelpEMNDMFLEMKnLVDYFQWYMTLSGINIILllGRILklmdfqprlgvitrtlwlagADLMHFFVIFGMVFVG 1343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  357 FANgLNQLYFYYeetkgltckgircekQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATMFGTYNVISL 436
Cdd:PLN03223 1344 YAF-IGHVIFGN---------------ASVHFSDMTDSINSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVF 1407

                         250
                  ....*....|....*
gi 209863032  437 VVLLNMLIAMMNNSY 451
Cdd:PLN03223 1408 MILFNFLLAIICDAF 1422
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 17-576 0e+00

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: 678.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032   17 RIPLRIVRA-ESELSPSEKAYLNAVEKGDYASVKKSLEEAEiyfKININCIDPLGRTALLIAIENENLELIELLLSFN-- 93
Cdd:TIGR00870   1 RGPLDIVPAeESPLSDEEKAFLPAAERGDLASVYRDLEEPK---KLNINCPDRLGRSALFVAAIENENLELTELLLNLsc 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032   94 -VYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQ---------------------------------------------- 126
Cdd:TIGR00870  78 rGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSgplelandqytseftpgitalhlaahrqnyeivklllergasvpar 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032      --------------------------------------------------------------------------------
Cdd:TIGR00870 158 acgdffvksqgvdsfyhgesplnaaaclgspsivallsedpadiltadslgntllhllvmenefkaeyeelscqmynfal 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  127 ------------------------------------------------FVAQPNCQQLLASRWYDEFPGWRRRHWAVKMV 158
Cdd:TIGR00870 238 slldklrdskelevilnhqgltplklaakegrivlfrlklaikykqkkFVAWPNGQQLLSLYWLEELDGWRRKQSVLELI 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  159 TCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDR---SDLNRQGPPPTIVEWMILP 235
Cdd:TIGR00870 318 VVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRptrTDLRVTGLQQTPLEMLIVT 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  236 WVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFAIANI 313
Cdd:TIGR00870 398 WVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFAFALV 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  314 FSSLRLISLFTANSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGI---RCEKQNNAFS 389
Cdd:TIGR00870 478 LSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQGNAYS 557

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  390 TLFETLQSLFWSIFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKL 469
Cdd:TIGR00870 558 TLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKL 633

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  470 WMSYFEEGGTLPTPFNVIPSPKSLWYLIKWIWTHLCKK---KMRRKPESFGTIGRRAADNLRRH-HQYQEVMRNLVKRYV 545
Cdd:TIGR00870 634 WMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTWERKAETLIEDgLHYQRVMKRLIKRYV 713

                         730       740       750
                  ....*....|....*....|....*....|.
gi 209863032  546 AAMIRDAKtEEGLTEENFKELKQDISSFRFE 576
Cdd:TIGR00870 714 LAEQRPRD-DEGTTEEETKELKQDISSLRFE 743
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 222-459 1.41e-25

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: 106.20  E-value: 1.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  222 QGPPPTIVEWMILPWVLGFIWGEIKQMWDGGLQD-YIHDWWNLMDFVMNSLYLATISLKIVAfvkysalnpreswdmwhp 300
Cdd:pfam00520  28 EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKrYFRSPWNILDFVVVLPSLISLVLSSVG------------------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  301 tlvaeaLFAIANIFSSLRLISLFTANSHLGPLQI---SLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETkgltck 377
Cdd:pfam00520  90 ------SLSGLRVLRLLRLLRLLRLIRRLEGLRTlvnSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKT------ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  378 GIRCEKQNNAFSTLFETLQSLFWSIF--GLINLYVTNVKAQHEFtefVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIA 455
Cdd:pfam00520 158 WENPDNGRTNFDNFPNAFLWLFQTMTteGWGDIMYDTIDGKGEF---WAYIYFVSFIILGGFLLLNLFIAVIIDNFQELT 234


                  ....
gi 209863032  456 DHAD 459
Cdd:pfam00520 235 ERTE 238
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 328-466 5.39e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 62.90  E-value: 5.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 328 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYfyyEETK-----GLTCKGIRCEKQNNAFSTLFETLQSLFWS 401
Cdd:cd22196  453 QMGIYSVMIQKMILrDICRFLFVYLVFLFGFSAALVTLI---EDGPpkgdvNTSQKECVCKSGYNSYNSLYSTCLELFKF 529

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209863032 402 IFGLINLYVT-NVKAQHEFTefvgaTMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 466
Cdd:cd22196  530 TIGMGDLEFTeNYKFKEVFI-----FLLISYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQR 590
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 328-466 6.61e-10

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: 62.59  E-value: 6.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 328 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLyfyyeetkgltckgIRCEKQNNA--FSTLFETLQSLFWSIFG 404
Cdd:cd21882  431 MLGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAFVIL--------------FQTEDPNKLgeFRDYPDALLELFKFTIG 496

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 209863032 405 LINLyvtnvkaqhEFTE-----FVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 466
Cdd:cd21882  497 MGDL---------PFNEnvdfpFVYLILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 329-463 5.97e-08

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: 56.17  E-value: 5.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 329 LGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLnQLYFYYEEtkgltckgircEKQNNAFSTLFETLQSLFWSIFGLIN 407
Cdd:cd22192  447 LGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSAF-YMIFQTED-----------PDSLGHFYDFPMTLFSTFELFLGLID 514

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 209863032 408 LYV-TNVKaqhefTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWK 463
Cdd:cd22192  515 GPAnYTVD-----LPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 236-451 1.37e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 55.33  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  236 WVLGFIWGEIKQMWD-----GGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKY-SALNPRESWDMWHpTLVAEALF- 308
Cdd:PLN03223 1185 GAVYSVYEEAMDFGSskktrGSYLAYFLSGWNYVDFASIGLHLATIMMWFVFSWSYaRAFEPDIHYDIYK-NLSASANFt 1263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  309 ---------AIANIFSSLR-LISLFTANSHLGPLQISL--GRML--------------------LDILKFLFIYCLVLLA 356
Cdd:PLN03223 1264 alripnelpEMNDMFLEMKnLVDYFQWYMTLSGINIILllGRILklmdfqprlgvitrtlwlagADLMHFFVIFGMVFVG 1343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  357 FANgLNQLYFYYeetkgltckgircekQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATMFGTYNVISL 436
Cdd:PLN03223 1344 YAF-IGHVIFGN---------------ASVHFSDMTDSINSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVF 1407

                         250
                  ....*....|....*
gi 209863032  437 VVLLNMLIAMMNNSY 451
Cdd:PLN03223 1408 MILFNFLLAIICDAF 1422
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 222-494 2.69e-07

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: 54.03  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 222 QGPPP----TIVEWM-------ILPWVLGFIWGEIKQMW---DGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS 287
Cdd:cd22193  334 EPPPPlaktTKMDYMrllgeilVLLGGVYFFVKEIAYFLlrrSDLQSSFSDSYFEILFFVQAVLVILSVVLYLFAYKEYL 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 288 ALnpreswdmwhptLVAEALFAIANIFSSLRlislftANSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLnqlyf 366
Cdd:cd22193  414 AC------------LVLALALGWANMLYYTR------GFQSMGIYSVMIQKVILrDLLRFLFVYLLFLFGFAVAL----- 470

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 367 yyeetKGLTCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLYVTNvkaQHEFtEFVGATMFGTYNVISLVVLLNMLIAM 446
Cdd:cd22193  471 -----VSLIEKCSSDKKDCSSYGSFSDAVLELFKLTIGMGDLEFQE---NSTY-PAVFLILLLTYVILTFVLLLNMLIAL 541

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 209863032 447 MNNSYQLIADHADIEWKF--ARTKL--------WM-SYFEEGGTLPTPFNVIPSPKSLW 494
Cdd:cd22193  542 MGETVNNVSKESKRIWKLqrAITILefeksfpeCMrKAFRSGRLLKVGLCKDGTPDFRW 600
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 339-469 6.48e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs 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: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.76  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 339 MLLDILKFLFIYCLVLLAFANGLNQLYfyyeetkgLTCK-GIRCEKQNNAFSTLFEtlqsLFWSIFGLINLYVTnvkaQH 417
Cdd:cd22194  509 ILNDVLKFLLVYILFLLGFGVALASLI--------EDCPdDSECSSYGSFSDAVLE----LFKLTIGLGDLEIQ----QN 572

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 209863032 418 EFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKF--ARTKL 469
Cdd:cd22194  573 SKYPILFLLLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLqrARTIL 626
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 237-451 1.20e-04

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: 44.19  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  237 VLGFIWGEIKQMWDGGLQdYIHDWWNLMDFVMNSLYLATISLKIVAFVKYSAL------NPRESWDMWHPTLVAEALF-- 308
Cdd:pfam08016  21 FLYFVVEEILKIRKHRPS-YLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLiksveaSPVTFIDFDRVAQLDNLYRii 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032  309 -AIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFAnglnQLyfyyeetkGLTCKGircekqNNA 387
Cdd:pfam08016 100 lAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYA----QF--------GYLLFG------TQA 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 209863032  388 --FSTLFETLQSLFWSIFGLINLYvtnvkAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSY 451
Cdd:pfam08016 162 pnFSNFVKSILTLFRTILGDFGYN-----EIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 330-464 4.21e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs 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 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.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 44.07  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 330 GPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGIRCE-------KQNNAFSTLfetLQSLFWS 401
Cdd:cd22195  499 GTYSIMIQKILFkDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTvptypscRDSNTFSKF---LLDLFKL 575

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209863032 402 IFGLINLYVTNvKAQHEFtefVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKF 464
Cdd:cd22195  576 TIGMGDLEMLN-SAKYPA---VFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKL 634
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 339-466 1.15e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.53  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 209863032 339 MLLDILKFLFIYCLVLLAFANGLNQLY-----FYYEETKGLTCKGIRCEKQNNA---FSTLFETLQSLFWSIFGLINLyv 410
Cdd:cd22197  463 ILRDLLRFLLVYLVFLFGFAVALVSLSreapsPKAPEDNNSTVTEQPTVGQEEEpapYRSILDASLELFKFTIGMGEL-- 540

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 209863032 411 tnvkAQHEFTEFVGATMFG--TYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 466
Cdd:cd22197  541 ----AFQEQLRFRGVVLLLllAYVLLTYVLLLNMLIALMSETVNHVADNSWSIWKLQK 594
 
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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