NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039764126|ref|XP_017175023|]
View 

short transient receptor potential channel 4 isoform X2 [Mus musculus]

Protein Classification

transient-receptor-potential channel protein( domain architecture ID 11489825)

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:0006828|GO:0005262|GO:0070679
PubMed:  20025796|18535090|20861159
SCOP:  4000366
TCDB:  1.A.4

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 17-749 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: 980.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  17 RIPLRIVRA-ESELSPSEKAYLNAVEKGDYASVKKSLEEAEiyfKININCIDPLGRTALLIAIENENLELIELLLSFN-- 93
Cdd:TIGR00870   1 RGPLDIVPAeESPLSDEEKAFLPAAERGDLASVYRDLEEPK---KLNINCPDRLGRSALFVAAIENENLELTELLLNLsc 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  94 -VYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILL-DKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPrp 171
Cdd:TIGR00870  78 rGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELAnDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVP-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 172 heVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDP--FLTAFQLSWELQELSKVENEFKSEYEELSRQCK 249
Cdd:TIGR00870 156 --ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 250 QFAKDLLDQTRSSRELEIILNYRDD--NSLIEEQSGNDLARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWA 327
Cdd:TIGR00870 234 NFALSLLDKLRDSKELEVILNHQGLtpLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 328 VKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDR---SDLNRQGPPPTIVEW 404
Cdd:TIGR00870 314 LELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRptrTDLRVTGLQQTPLEM 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 405 MILPWVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFA 482
Cdd:TIGR00870 394 LIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFA 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 483 IANIFSSLRLISLFTANSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLSCKGI---RCEKQN 558
Cdd:TIGR00870 474 FALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQG 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 559 NAFSTLFETLQSLFWSIFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFA 638
Cdd:TIGR00870 554 NAYSTLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQ 629

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 639 RTKLWMSYFEEGGTLPTPFNVIPSPKSLWYLVKWIWTHLCKK---KMRRKPESFGTIGRRAADNLRRH-HQYQEVMRNLV 714
Cdd:TIGR00870 630 RAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTWERKAETLIEDgLHYQRVMKRLI 709

                         730       740       750
                  ....*....|....*....|....*....|....*
gi 1039764126 715 KRYVAAMIREAKtEEGLTEENVKELKQDISSFRFE 749
Cdd:TIGR00870 710 KRYVLAEQRPRD-DEGTTEEETKELKQDISSLRFE 743
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 17-749 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: 980.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  17 RIPLRIVRA-ESELSPSEKAYLNAVEKGDYASVKKSLEEAEiyfKININCIDPLGRTALLIAIENENLELIELLLSFN-- 93
Cdd:TIGR00870   1 RGPLDIVPAeESPLSDEEKAFLPAAERGDLASVYRDLEEPK---KLNINCPDRLGRSALFVAAIENENLELTELLLNLsc 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  94 -VYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILL-DKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPrp 171
Cdd:TIGR00870  78 rGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELAnDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVP-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 172 heVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDP--FLTAFQLSWELQELSKVENEFKSEYEELSRQCK 249
Cdd:TIGR00870 156 --ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 250 QFAKDLLDQTRSSRELEIILNYRDD--NSLIEEQSGNDLARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWA 327
Cdd:TIGR00870 234 NFALSLLDKLRDSKELEVILNHQGLtpLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 328 VKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDR---SDLNRQGPPPTIVEW 404
Cdd:TIGR00870 314 LELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRptrTDLRVTGLQQTPLEM 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 405 MILPWVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFA 482
Cdd:TIGR00870 394 LIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFA 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 483 IANIFSSLRLISLFTANSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLSCKGI---RCEKQN 558
Cdd:TIGR00870 474 FALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQG 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 559 NAFSTLFETLQSLFWSIFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFA 638
Cdd:TIGR00870 554 NAYSTLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQ 629

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 639 RTKLWMSYFEEGGTLPTPFNVIPSPKSLWYLVKWIWTHLCKK---KMRRKPESFGTIGRRAADNLRRH-HQYQEVMRNLV 714
Cdd:TIGR00870 630 RAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTWERKAETLIEDgLHYQRVMKRLI 709

                         730       740       750
                  ....*....|....*....|....*....|....*
gi 1039764126 715 KRYVAAMIREAKtEEGLTEENVKELKQDISSFRFE 749
Cdd:TIGR00870 710 KRYVLAEQRPRD-DEGTTEEETKELKQDISSLRFE 743
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
 176-235 2.37e-32

Transient receptor ion channel II; This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors. This domain does not tend to appear with the TRP domain (pfam06011) but is often found to the C-terminus of Ankyrin repeats (pfam00023).


Pssm-ID: 462438  Cd Length: 60  Bit Score: 119.61  E-value: 2.37e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 176 CNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVEN 235
Cdd:pfam08344   1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVEP 60
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 501-639 5.60e-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: 5.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 501 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYfyyEETK-----GLSCKGIRCEKQNNAFSTLFETLQSLFWS 574
Cdd:cd22196   453 QMGIYSVMIQKMILrDICRFLFVYLVFLFGFSAALVTLI---EDGPpkgdvNTSQKECVCKSGYNSYNSLYSTCLELFKF 529

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764126 575 IFGLINLYVT-NVKAQHEFTefvgaTMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 639
Cdd:cd22196   530 TIGMGDLEFTeNYKFKEVFI-----FLLISYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQR 590
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 409-624 1.57e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 55.33  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  409 WVLGFIWGEIKQMWD-----GGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKY-SALNPRESWDMWHpTLVAEALF- 481
Cdd:PLN03223  1185 GAVYSVYEEAMDFGSskktrGSYLAYFLSGWNYVDFASIGLHLATIMMWFVFSWSYaRAFEPDIHYDIYK-NLSASANFt 1263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  482 ---------AIANIFSSLR-LISLFTANSHLGPLQISL--GRML--------------------LDILKFLFIYCLVLLA 529
Cdd:PLN03223  1264 alripnelpEMNDMFLEMKnLVDYFQWYMTLSGINIILllGRILklmdfqprlgvitrtlwlagADLMHFFVIFGMVFVG 1343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  530 FANgLNQLYFYYeetkglsckgircekQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATMFGTYNVISL 609
Cdd:PLN03223  1344 YAF-IGHVIFGN---------------ASVHFSDMTDSINSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVF 1407

                          250
                   ....*....|....*
gi 1039764126  610 VVLLNMLIAMMNNSY 624
Cdd:PLN03223  1408 MILFNFLLAIICDAF 1422
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-168 2.72e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.87  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  35 AYLNAVEKGDYASVKKSLEEaeiyfKININCIDPLGRTALLIAIENENLELIELLLS--FNVYVGD-----ALLHAIRKE 107
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEA-----GADVNARDKDGETPLHLAAYNGNLEIVKLLLEagADVNAQDndgntPLHLAAANG 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039764126 108 VVGAVELLLNHKkpsgekqVPPILLDKQfseftpDITPIILAAHTNNYEIIKLLVQKGVSV 168
Cdd:COG0666   165 NLEIVKLLLEAG-------ADVNARDND------GETPLHLAAENGHLEIVKLLLEAGADV 212
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 17-749 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: 980.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  17 RIPLRIVRA-ESELSPSEKAYLNAVEKGDYASVKKSLEEAEiyfKININCIDPLGRTALLIAIENENLELIELLLSFN-- 93
Cdd:TIGR00870   1 RGPLDIVPAeESPLSDEEKAFLPAAERGDLASVYRDLEEPK---KLNINCPDRLGRSALFVAAIENENLELTELLLNLsc 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  94 -VYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILL-DKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPrp 171
Cdd:TIGR00870  78 rGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELAnDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVP-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 172 heVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDP--FLTAFQLSWELQELSKVENEFKSEYEELSRQCK 249
Cdd:TIGR00870 156 --ARACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 250 QFAKDLLDQTRSSRELEIILNYRDD--NSLIEEQSGNDLARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPGWRRRHWA 327
Cdd:TIGR00870 234 NFALSLLDKLRDSKELEVILNHQGLtpLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 328 VKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIRKPFIKFICHTASYLTFLFLLLLASQHIDR---SDLNRQGPPPTIVEW 404
Cdd:TIGR00870 314 LELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRptrTDLRVTGLQQTPLEM 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 405 MILPWVLGFIWGEIKQMWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFA 482
Cdd:TIGR00870 394 LIVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFA 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 483 IANIFSSLRLISLFTANSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLSCKGI---RCEKQN 558
Cdd:TIGR00870 474 FALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQG 553

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 559 NAFSTLFETLQSLFWSIFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFA 638
Cdd:TIGR00870 554 NAYSTLFETSQELFWAIIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQ 629

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 639 RTKLWMSYFEEGGTLPTPFNVIPSPKSLWYLVKWIWTHLCKK---KMRRKPESFGTIGRRAADNLRRH-HQYQEVMRNLV 714
Cdd:TIGR00870 630 RAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTWERKAETLIEDgLHYQRVMKRLI 709

                         730       740       750
                  ....*....|....*....|....*....|....*
gi 1039764126 715 KRYVAAMIREAKtEEGLTEENVKELKQDISSFRFE 749
Cdd:TIGR00870 710 KRYVLAEQRPRD-DEGTTEEETKELKQDISSLRFE 743
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
 176-235 2.37e-32

Transient receptor ion channel II; This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors. This domain does not tend to appear with the TRP domain (pfam06011) but is often found to the C-terminus of Ankyrin repeats (pfam00023).


Pssm-ID: 462438  Cd Length: 60  Bit Score: 119.61  E-value: 2.37e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 176 CNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVEN 235
Cdd:pfam08344   1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVEP 60
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 395-632 1.15e-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: 106.58  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 395 QGPPPTIVEWMILPWVLGFIWGEIKQMWDGGLQD-YIHDWWNLMDFVMNSLYLATISLKIVAfvkysalnpreswdmwhp 473
Cdd:pfam00520  28 EEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKrYFRSPWNILDFVVVLPSLISLVLSSVG------------------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 474 tlvaeaLFAIANIFSSLRLISLFTANSHLGPLQI---SLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETKGLSCK 550
Cdd:pfam00520  90 ------SLSGLRVLRLLRLLRLLRLIRRLEGLRTlvnSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENPDN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 551 GircekqNNAFSTLFETLQSLFWSIF--GLINLYVTNVKAQHEFtefVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIA 628
Cdd:pfam00520 164 G------RTNFDNFPNAFLWLFQTMTteGWGDIMYDTIDGKGEF---WAYIYFVSFIILGGFLLLNLFIAVIIDNFQELT 234


                  ....
gi 1039764126 629 DHAD 632
Cdd:pfam00520 235 ERTE 238
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 501-639 5.60e-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: 5.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 501 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYfyyEETK-----GLSCKGIRCEKQNNAFSTLFETLQSLFWS 574
Cdd:cd22196   453 QMGIYSVMIQKMILrDICRFLFVYLVFLFGFSAALVTLI---EDGPpkgdvNTSQKECVCKSGYNSYNSLYSTCLELFKF 529

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764126 575 IFGLINLYVT-NVKAQHEFTefvgaTMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 639
Cdd:cd22196   530 TIGMGDLEFTeNYKFKEVFI-----FLLISYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQR 590
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 501-639 1.07e-09

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: 62.20  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 501 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLyfyyeetkglsckgIRCEKQNNA--FSTLFETLQSLFWSIFG 577
Cdd:cd21882   431 MLGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAFVIL--------------FQTEDPNKLgeFRDYPDALLELFKFTIG 496

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764126 578 LINLyvtnvkaqhEFTE-----FVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 639
Cdd:cd21882   497 MGDL---------PFNEnvdfpFVYLILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 502-636 7.45e-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: 7.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 502 LGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLnQLYFYYEETKGLSckgircekqnnAFSTLFETLQSLFWSIFGLIN 580
Cdd:cd22192   447 LGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSAF-YMIFQTEDPDSLG-----------HFYDFPMTLFSTFELFLGLID 514

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764126 581 LYV-TNVKaqhefTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWK 636
Cdd:cd22192   515 GPAnYTVD-----LPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 409-624 1.57e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 55.33  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  409 WVLGFIWGEIKQMWD-----GGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKY-SALNPRESWDMWHpTLVAEALF- 481
Cdd:PLN03223  1185 GAVYSVYEEAMDFGSskktrGSYLAYFLSGWNYVDFASIGLHLATIMMWFVFSWSYaRAFEPDIHYDIYK-NLSASANFt 1263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  482 ---------AIANIFSSLR-LISLFTANSHLGPLQISL--GRML--------------------LDILKFLFIYCLVLLA 529
Cdd:PLN03223  1264 alripnelpEMNDMFLEMKnLVDYFQWYMTLSGINIILllGRILklmdfqprlgvitrtlwlagADLMHFFVIFGMVFVG 1343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  530 FANgLNQLYFYYeetkglsckgircekQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATMFGTYNVISL 609
Cdd:PLN03223  1344 YAF-IGHVIFGN---------------ASVHFSDMTDSINSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVF 1407

                          250
                   ....*....|....*
gi 1039764126  610 VVLLNMLIAMMNNSY 624
Cdd:PLN03223  1408 MILFNFLLAIICDAF 1422
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 395-667 2.68e-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: 54.42  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 395 QGPPP----TIVEWM-------ILPWVLGFIWGEIKQMW---DGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS 460
Cdd:cd22193   334 EPPPPlaktTKMDYMrllgeilVLLGGVYFFVKEIAYFLlrrSDLQSSFSDSYFEILFFVQAVLVILSVVLYLFAYKEYL 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 461 ALnpreswdmwhptLVAEALFAIANIFSSLRlislftANSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLnqlyf 539
Cdd:cd22193   414 AC------------LVLALALGWANMLYYTR------GFQSMGIYSVMIQKVILrDLLRFLFVYLLFLFGFAVAL----- 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 540 yyeetKGLSCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLYVTNvkaQHEFtEFVGATMFGTYNVISLVVLLNMLIAM 619
Cdd:cd22193   471 -----VSLIEKCSSDKKDCSSYGSFSDAVLELFKLTIGMGDLEFQE---NSTY-PAVFLILLLTYVILTFVLLLNMLIAL 541

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039764126 620 MNNSYQLIADHADIEWKF--ARTKL--------WM-SYFEEGGTLPTPFNVIPSPKSLW 667
Cdd:cd22193   542 MGETVNNVSKESKRIWKLqrAITILefeksfpeCMrKAFRSGRLLKVGLCKDGTPDFRW 600
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 512-642 1.65e-05

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: 48.60  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 512 MLLDILKFLFIYCLVLLAFANGLNQLYfyyeETkglsCK-GIRCEKQNNAFSTLFEtlqsLFWSIFGLINLYVTnvkaQH 590
Cdd:cd22194   509 ILNDVLKFLLVYILFLLGFGVALASLI----ED----CPdDSECSSYGSFSDAVLE----LFKLTIGLGDLEIQ----QN 572

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039764126 591 EFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKF--ARTKL 642
Cdd:cd22194   573 SKYPILFLLLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLqrARTIL 626
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-168 2.72e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.87  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  35 AYLNAVEKGDYASVKKSLEEaeiyfKININCIDPLGRTALLIAIENENLELIELLLS--FNVYVGD-----ALLHAIRKE 107
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEA-----GADVNARDKDGETPLHLAAYNGNLEIVKLLLEagADVNAQDndgntPLHLAAANG 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039764126 108 VVGAVELLLNHKkpsgekqVPPILLDKQfseftpDITPIILAAHTNNYEIIKLLVQKGVSV 168
Cdd:COG0666   165 NLEIVKLLLEAG-------ADVNARDND------GETPLHLAAENGHLEIVKLLLEAGADV 212
Ank_2 pfam12796
Ankyrin repeats (3 copies);
39-168 3.11e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126  39 AVEKGDYASVKKSLEEaeiyfKININCIDPLGRTALLIAienenlelielllsfnvyvgdallhaIRKEVVGAVELLLNH 118
Cdd:pfam12796   4 AAKNGNLELVKLLLEN-----GADANLQDKNGRTALHLA--------------------------AKNGHLEIVKLLLEH 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039764126 119 KkpsgekqvppilldkQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSV 168
Cdd:pfam12796  53 A---------------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 410-624 3.04e-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: 43.03  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 410 VLGFIWGEIKQMWDGGLQdYIHDWWNLMDFVMNSLYLATISLKIVAFVKYSAL------NPRESWDMWHPTLVAEALF-- 481
Cdd:pfam08016  21 FLYFVVEEILKIRKHRPS-YLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLiksveaSPVTFIDFDRVAQLDNLYRii 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 482 -AIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETkglsckgircekqnna 560
Cdd:pfam08016 100 lAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPN---------------- 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039764126 561 FSTLFETLQSLFWSIFGLINLYvtnvkAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSY 624
Cdd:pfam08016 164 FSNFVKSILTLFRTILGDFGYN-----EIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 503-637 6.27e-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: 43.69  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 503 GPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLSCKGIRCE-------KQNNAFSTLfetLQSLFWS 574
Cdd:cd22195   499 GTYSIMIQKILFkDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTvptypscRDSNTFSKF---LLDLFKL 575

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039764126 575 IFGLINLYVTNvKAQHEFtefVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKF 637
Cdd:cd22195   576 TIGMGDLEMLN-SAKYPA---VFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKL 634
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-168 7.59e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.63  E-value: 7.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039764126  98 DALLHAIRKEVVGAVELLLNHKkpsgekqVPPILLDKQfseftpDITPIILAAHTNNYEIIKLLVQKGVSV 168
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAG-------ADVNARDKD------GETPLHLAAYNGNLEIVKLLLEAGADV 146
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 512-639 2.91e-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: 41.38  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764126 512 MLLDILKFLFIYCLVLLAFANGLNQLYFYYEETK--------GLSCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLyv 583
Cdd:cd22197   463 ILRDLLRFLLVYLVFLFGFAVALVSLSREAPSPKapednnstVTEQPTVGQEEEPAPYRSILDASLELFKFTIGMGEL-- 540

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039764126 584 tnvkAQHEFTEFVGATMFG--TYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 639
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH