NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2323579483|ref|NP_001400304|]
View 

short transient receptor potential channel 1 isoform 7 [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
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
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
14-676 5.20e-160

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


The actual alignment was detected with superfamily member TIGR00870:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 743  Bit Score: 479.19  E-value: 5.20e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483  14 DALLVAIDSEVVGAVDILLNHRPKRSSRPTIVKLMERIQNPEYstTMDVAPVILAAHRNNYEILTMLLKQDVSLPkphaV 93
Cdd:TIGR00870  83 DTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEF--TPGITALHLAAHRQNYEIVKLLLERGASVP----A 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483  94 GCECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDP--ILRAFELSADLKELSLVEVEFRNDYEELARQCKMFA 171
Cdd:TIGR00870 157 RACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFA 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 172 KDLLAQARNSRELEVILNHtsSDEPLDKRGLLEERMNLSRLKLAIKYNQKEFVSQSNCQQFLNTVWFGQMSGYRRKPTCK 251
Cdd:TIGR00870 237 LSLLDKLRDSKELEVILNH--QGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVL 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 252 KIMTVLTVGIFWPVLSLCYLIAPKSQFGRIIHTPFMKFIIHGASYFTFLLLLNLYSLVYNEDKK---NTMGPALERIDYL 328
Cdd:TIGR00870 315 ELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRtdlRVTGLQQTPLEML 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 329 LILWIIGMIWSDIKRLWYEGLEDFLEESRNQLSFVMNSLYLATFALKVVAHNKFHD--FADRKDWDAFHPTLVAEGLFAF 406
Cdd:TIGR00870 395 IVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQafLVLREHWLRFDPTLIEEALFAF 474
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 407 ANVLSYLRLFFMYTTSSILGPLQISMGQM-LQDFGKFLGMFLLVLFSFTIGLTQLYDKGYTSK--EQKDCVGIFCEQQSN 483
Cdd:TIGR00870 475 ALVLSWLNLLYIFRGNQHLGPLQIMIGRMiLGDILRFLFIYAVVLFGFACGLNQLYQYYDELKlnECSNPHARSCEKQGN 554
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 484 DtFHSFIGTCFALFWYIFSLAHVAifvtrFSYGEELQsFVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWK 563
Cdd:TIGR00870 555 A-YSTLFETSQELFWAIIGLGDLL-----ANEHKFTE-FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWK 627
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 564 FARAKLWLSYFDDKCTLPPPFNIIPSPKTICYMISSLSKWICSHTSKGKVKRQNSL-KEWRNLKQKRDEN---YQKVMCC 639
Cdd:TIGR00870 628 FQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKRQRWCRRVEEVNwTTWERKAETLIEDglhYQRVMKR 707
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 2323579483 640 LVHRYLTSMrQKMQSTDQATVENLNELRQDLSKFRNE 676
Cdd:TIGR00870 708 LIKRYVLAE-QRPRDDEGTTEEETKELKQDISSLRFE 743
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
14-676 5.20e-160

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 479.19  E-value: 5.20e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483  14 DALLVAIDSEVVGAVDILLNHRPKRSSRPTIVKLMERIQNPEYstTMDVAPVILAAHRNNYEILTMLLKQDVSLPkphaV 93
Cdd:TIGR00870  83 DTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEF--TPGITALHLAAHRQNYEIVKLLLERGASVP----A 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483  94 GCECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDP--ILRAFELSADLKELSLVEVEFRNDYEELARQCKMFA 171
Cdd:TIGR00870 157 RACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFA 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 172 KDLLAQARNSRELEVILNHtsSDEPLDKRGLLEERMNLSRLKLAIKYNQKEFVSQSNCQQFLNTVWFGQMSGYRRKPTCK 251
Cdd:TIGR00870 237 LSLLDKLRDSKELEVILNH--QGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVL 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 252 KIMTVLTVGIFWPVLSLCYLIAPKSQFGRIIHTPFMKFIIHGASYFTFLLLLNLYSLVYNEDKK---NTMGPALERIDYL 328
Cdd:TIGR00870 315 ELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRtdlRVTGLQQTPLEML 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 329 LILWIIGMIWSDIKRLWYEGLEDFLEESRNQLSFVMNSLYLATFALKVVAHNKFHD--FADRKDWDAFHPTLVAEGLFAF 406
Cdd:TIGR00870 395 IVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQafLVLREHWLRFDPTLIEEALFAF 474
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 407 ANVLSYLRLFFMYTTSSILGPLQISMGQM-LQDFGKFLGMFLLVLFSFTIGLTQLYDKGYTSK--EQKDCVGIFCEQQSN 483
Cdd:TIGR00870 475 ALVLSWLNLLYIFRGNQHLGPLQIMIGRMiLGDILRFLFIYAVVLFGFACGLNQLYQYYDELKlnECSNPHARSCEKQGN 554
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 484 DtFHSFIGTCFALFWYIFSLAHVAifvtrFSYGEELQsFVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWK 563
Cdd:TIGR00870 555 A-YSTLFETSQELFWAIIGLGDLL-----ANEHKFTE-FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWK 627
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 564 FARAKLWLSYFDDKCTLPPPFNIIPSPKTICYMISSLSKWICSHTSKGKVKRQNSL-KEWRNLKQKRDEN---YQKVMCC 639
Cdd:TIGR00870 628 FQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKRQRWCRRVEEVNwTTWERKAETLIEDglhYQRVMKR 707
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 2323579483 640 LVHRYLTSMrQKMQSTDQATVENLNELRQDLSKFRNE 676
Cdd:TIGR00870 708 LIKRYVLAE-QRPRDDEGTTEEETKELKQDISSLRFE 743
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
95-153 1.19e-27

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: 105.74  E-value: 1.19e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2323579483  95 CECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDPILRAFELSADLKELSLVE 153
Cdd:pfam08344   1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVE 59
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
360-567 1.85e-05

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: 47.88  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 360 LSFVMNSLYLATFALKvvahnkfhdFADRKDWDAFhptLVAEGLFAFANVLSYLRLFFMyttssiLGPLQISMGQM-LQD 438
Cdd:cd22196   407 LFFVQSLFLLASTVLY---------FCGRNEYVAF---MVISLALGWANVLYYTRGFQQ------MGIYSVMIQKMiLRD 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 439 FGKFLGMFLLVLFSFTIGLTQLYDKGYTSKEQKDCVGIFCEQQSNDTFHSFIGTCFALFWYIFSLAHVAiFVTRFSYGEe 518
Cdd:cd22196   469 ICRFLFVYLVFLFGFSAALVTLIEDGPPKGDVNTSQKECVCKSGYNSYNSLYSTCLELFKFTIGMGDLE-FTENYKFKE- 546
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2323579483 519 lqsfVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWKFARA 567
Cdd:cd22196   547 ----VFIFLLISYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQRA 591
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
14-676 5.20e-160

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 479.19  E-value: 5.20e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483  14 DALLVAIDSEVVGAVDILLNHRPKRSSRPTIVKLMERIQNPEYstTMDVAPVILAAHRNNYEILTMLLKQDVSLPkphaV 93
Cdd:TIGR00870  83 DTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEF--TPGITALHLAAHRQNYEIVKLLLERGASVP----A 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483  94 GCECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDP--ILRAFELSADLKELSLVEVEFRNDYEELARQCKMFA 171
Cdd:TIGR00870 157 RACGDFFVKSQGVDSFYHGESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFA 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 172 KDLLAQARNSRELEVILNHtsSDEPLDKRGLLEERMNLSRLKLAIKYNQKEFVSQSNCQQFLNTVWFGQMSGYRRKPTCK 251
Cdd:TIGR00870 237 LSLLDKLRDSKELEVILNH--QGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVL 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 252 KIMTVLTVGIFWPVLSLCYLIAPKSQFGRIIHTPFMKFIIHGASYFTFLLLLNLYSLVYNEDKK---NTMGPALERIDYL 328
Cdd:TIGR00870 315 ELIVVFVIGLKFPELSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPTRtdlRVTGLQQTPLEML 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 329 LILWIIGMIWSDIKRLWYEGLEDFLEESRNQLSFVMNSLYLATFALKVVAHNKFHD--FADRKDWDAFHPTLVAEGLFAF 406
Cdd:TIGR00870 395 IVTWVDGLRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQafLVLREHWLRFDPTLIEEALFAF 474
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 407 ANVLSYLRLFFMYTTSSILGPLQISMGQM-LQDFGKFLGMFLLVLFSFTIGLTQLYDKGYTSK--EQKDCVGIFCEQQSN 483
Cdd:TIGR00870 475 ALVLSWLNLLYIFRGNQHLGPLQIMIGRMiLGDILRFLFIYAVVLFGFACGLNQLYQYYDELKlnECSNPHARSCEKQGN 554
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 484 DtFHSFIGTCFALFWYIFSLAHVAifvtrFSYGEELQsFVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWK 563
Cdd:TIGR00870 555 A-YSTLFETSQELFWAIIGLGDLL-----ANEHKFTE-FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWK 627
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 564 FARAKLWLSYFDDKCTLPPPFNIIPSPKTICYMISSLSKWICSHTSKGKVKRQNSL-KEWRNLKQKRDEN---YQKVMCC 639
Cdd:TIGR00870 628 FQRAKLWMSYEREGGTCPPPFNIIPGPKSFVGLFKRIEKHDGKKRQRWCRRVEEVNwTTWERKAETLIEDglhYQRVMKR 707
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 2323579483 640 LVHRYLTSMrQKMQSTDQATVENLNELRQDLSKFRNE 676
Cdd:TIGR00870 708 LIKRYVLAE-QRPRDDEGTTEEETKELKQDISSLRFE 743
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
95-153 1.19e-27

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: 105.74  E-value: 1.19e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2323579483  95 CECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDPILRAFELSADLKELSLVE 153
Cdd:pfam08344   1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVE 59
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
360-567 1.85e-05

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: 47.88  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 360 LSFVMNSLYLATFALKvvahnkfhdFADRKDWDAFhptLVAEGLFAFANVLSYLRLFFMyttssiLGPLQISMGQM-LQD 438
Cdd:cd22196   407 LFFVQSLFLLASTVLY---------FCGRNEYVAF---MVISLALGWANVLYYTRGFQQ------MGIYSVMIQKMiLRD 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 439 FGKFLGMFLLVLFSFTIGLTQLYDKGYTSKEQKDCVGIFCEQQSNDTFHSFIGTCFALFWYIFSLAHVAiFVTRFSYGEe 518
Cdd:cd22196   469 ICRFLFVYLVFLFGFSAALVTLIEDGPPKGDVNTSQKECVCKSGYNSYNSLYSTCLELFKFTIGMGDLE-FTENYKFKE- 546
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2323579483 519 lqsfVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWKFARA 567
Cdd:cd22196   547 ----VFIFLLISYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQRA 591
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
325-559 4.92e-05

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: 45.34  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 325 IDYLLILWIIGMIWSDIKRLWYEGLED-FLEESRNQLSFVMNSLYLATFALKVVahnkfhdfadrkdwdafhptlvaeGL 403
Cdd:pfam00520  35 LEILDYVFTGIFTLEMLLKIIAAGFKKrYFRSPWNILDFVVVLPSLISLVLSSV------------------------GS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 404 FAFANVLSYLRLFFMYTTSSILGPLQI---SMGQMLQDFGKFLGMFLLVLFSFTIGLTQLYDKGYTSKEQkdcvgifcEQ 480
Cdd:pfam00520  91 LSGLRVLRLLRLLRLLRLIRRLEGLRTlvnSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWEN--------PD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 481 QSNDTFHSFIgtcFALFWyifslahvaIFVTRFS--YGEELQ-------SFVGAVIVGTYNVVVVIVLTKLLVAMLHKSF 551
Cdd:pfam00520 163 NGRTNFDNFP---NAFLW---------LFQTMTTegWGDIMYdtidgkgEFWAYIYFVSFIILGGFLLLNLFIAVIIDNF 230

                  ....*...
gi 2323579483 552 QLIANHED 559
Cdd:pfam00520 231 QELTERTE 238
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
396-567 1.80e-03

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: 41.40  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 396 PTLVAEGLFAFANVLSYLRLFFMyttssiLGPLQISMGQM-LQDFGKFLGMFLLVLFSFTIGLTQLYDKGytskeqkdcv 474
Cdd:cd21882   409 VPLVFSLVLGWCNVLYYTRGFQM------LGIYTVMIQKMiLRDLMRFCWVYLVFLFGFASAFVILFQTE---------- 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2323579483 475 gifcEQQSNDTFHSFIGTCFALFWYIFSLAHVAifvtrFSYGEELQsFVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLI 554
Cdd:cd21882   473 ----DPNKLGEFRDYPDALLELFKFTIGMGDLP-----FNENVDFP-FVYLILLLAYVILTYLLLLNMLIALMGETVNRV 542
                         170
                  ....*....|...
gi 2323579483 555 ANHEDKEWKFARA 567
Cdd:cd21882   543 AQESDEIWKLQKA 555
 
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