TRPV1_HUMAN
ID TRPV1_HUMAN Reviewed; 839 AA.
AC Q8NER1; A2RUA9; Q3LU47; Q9H0G9; Q9H303; Q9H304; Q9NQ74; Q9NY22;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 1;
DE Short=TrpV1;
DE AltName: Full=Capsaicin receptor;
DE AltName: Full=Osm-9-like TRP channel 1;
DE Short=OTRPC1;
DE AltName: Full=Vanilloid receptor 1;
GN Name=TRPV1; Synonyms=VR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANTS ILE-315 AND VAL-585.
RX PubMed=11050376; DOI=10.1016/s0304-3959(00)00353-5;
RA Hayes P., Meadows H.J., Gunthorpe M., Harries M.H., Duckworth M.D.,
RA Cairns W., Harrison D.C., Clarke C., Ellington K., Prinjha R.K.,
RA Barton A.J., Medhurst A.D., Smith G.D., Topp S., Murdock P., Sanger G.J.,
RA Terrett J., Jenkins O., Benham C.D., Randall A.D., Gloger I.S., Davis J.B.;
RT "Cloning and functional expression of a human orthologue of rat vanilloid
RT receptor-1.";
RL Pain 88:205-215(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANTS SER-91; ILE-315 AND ILE-469.
RC TISSUE=Spinal ganglion;
RX PubMed=11243859; DOI=10.1006/bbrc.2001.4482;
RA Cortright D.N., Crandall M., Sanchez J.F., Zou T., Krause J.E., White G.;
RT "The tissue distribution and functional characterization of human VR1.";
RL Biochem. Biophys. Res. Commun. 281:1183-1189(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT ILE-315.
RC TISSUE=Spinal ganglion;
RX PubMed=11226139; DOI=10.1038/sj.bjp.0703918;
RA McIntyre P., McLatchie L., Chambers A., Phillips E., Clarke M., Savidge J.,
RA Peacock M., Shah K., Winter J., Weerasekera N., Webb M., Rang H., Bevan S.,
RA James I.;
RT "Pharmacological differences between human and rat vanilloid receptor 1
RT (VR1).";
RL Br. J. Pharmacol. 132:1084-1094(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-315.
RC TISSUE=Brain;
RA Lee D., Ha I.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ILE-315 AND VAL-585, AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Pancreas;
RA Lu L., Mansson E.;
RT "Isolation and characterization of a human TRPV1 splice variant.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-315
RP AND ILE-469.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-315.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-315.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TRPV3.
RX PubMed=12077606; DOI=10.1038/nature00894;
RA Smith G.D., Gunthorpe M.J., Kelsell R.E., Hayes P.D., Reilly P., Facer P.,
RA Wright J.E., Jerman J.C., Walhin J.-P., Ooi L., Egerton J., Charles K.J.,
RA Smart D., Randall A.D., Anand P., Davis J.B.;
RT "TRPV3 is a temperature-sensitive vanilloid receptor-like protein.";
RL Nature 418:186-190(2002).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=14987252; DOI=10.1111/j.0906-6705.2004.0178.x;
RA Staender S., Moormann C., Schumacher M., Buddenkotte J., Artuc M.,
RA Shpacovitch V., Brzoska T., Lippert U., Henz B.M., Luger T.A., Metze D.,
RA Steinhoff M.;
RT "Expression of vanilloid receptor subtype 1 in cutaneous sensory nerve
RT fibers, mast cells, and epithelial cells of appendage structures.";
RL Exp. Dermatol. 13:129-139(2004).
RN [12]
RP MUTAGENESIS OF TYR-511 AND THR-550.
RX PubMed=14996838; DOI=10.1074/jbc.m312577200;
RA Gavva N.R., Klionsky L., Qu Y., Shi L., Tamir R., Edenson S., Zhang T.J.,
RA Viswanadhan V.N., Toth A., Pearce L.V., Vanderah T.W., Porreca F.,
RA Blumberg P.M., Lile J., Sun Y., Wild K., Louis J.C., Treanor J.J.;
RT "Molecular determinants of vanilloid sensitivity in TRPV1.";
RL J. Biol. Chem. 279:20283-20295(2004).
RN [13]
RP INTERACTION WITH PACS2.
RX PubMed=29656858; DOI=10.1016/j.ajhg.2018.03.005;
RG DDD Study;
RG C4RCD Research Group;
RA Olson H.E., Jean-Marcais N., Yang E., Heron D., Tatton-Brown K.,
RA van der Zwaag P.A., Bijlsma E.K., Krock B.L., Backer E., Kamsteeg E.J.,
RA Sinnema M., Reijnders M.R.F., Bearden D., Begtrup A., Telegrafi A.,
RA Lunsing R.J., Burglen L., Lesca G., Cho M.T., Smith L.A., Sheidley B.R.,
RA Moufawad El Achkar C., Pearl P.L., Poduri A., Skraban C.M., Tarpinian J.,
RA Nesbitt A.I., Fransen van de Putte D.E., Ruivenkamp C.A.L., Rump P.,
RA Chatron N., Sabatier I., De Bellescize J., Guibaud L., Sweetser D.A.,
RA Waxler J.L., Wierenga K.J., Donadieu J., Narayanan V., Ramsey K.M.,
RA Nava C., Riviere J.B., Vitobello A., Tran Mau-Them F., Philippe C.,
RA Bruel A.L., Duffourd Y., Thomas L., Lelieveld S.H., Schuurs-Hoeijmakers J.,
RA Brunner H.G., Keren B., Thevenon J., Faivre L., Thomas G.,
RA Thauvin-Robinet C.;
RT "A recurrent de novo PACS2 heterozygous missense variant causes neonatal-
RT onset developmental epileptic encephalopathy, facial dysmorphism, and
RT cerebellar dysgenesis.";
RL Am. J. Hum. Genet. 102:995-1007(2018).
CC -!- FUNCTION: Ligand-activated non-selective calcium permeant cation
CC channel involved in detection of noxious chemical and thermal stimuli.
CC Seems to mediate proton influx and may be involved in intracellular
CC acidosis in nociceptive neurons. Involved in mediation of inflammatory
CC pain and hyperalgesia. Sensitized by a phosphatidylinositol second
CC messenger system activated by receptor tyrosine kinases, which involves
CC PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and
CC temperatures higher than 42 degrees Celsius, exhibits a time- and
CC Ca(2+)-dependent outward rectification, followed by a long-lasting
CC refractory state. Mild extracellular acidic pH (6.5) potentiates
CC channel activation by noxious heat and vanilloids, whereas acidic
CC conditions (pH <6) directly activate the channel. Can be activated by
CC endogenous compounds, including 12-hydroperoxytetraenoic acid and
CC bradykinin. Acts as ionotropic endocannabinoid receptor with central
CC neuromodulatory effects. Triggers a form of long-term depression
CC (TRPV1-LTD) mediated by the endocannabinoid anandamine in the
CC hippocampus and nucleus accumbens by affecting AMPA receptors
CC endocytosis. {ECO:0000250|UniProtKB:O35433,
CC ECO:0000269|PubMed:11050376, ECO:0000269|PubMed:11226139,
CC ECO:0000269|PubMed:11243859, ECO:0000269|PubMed:12077606}.
CC -!- ACTIVITY REGULATION: Channel activity is activated via the interaction
CC with PIRT and phosphatidylinositol 4,5-bisphosphate (PIP2). Both PIRT
CC and PIP2 are required to activate channel activity (By similarity). The
CC channel is sensitized by ATP binding. Repeated stimulation with
CC capsaicin gives rise to progressively smaller responses, due to
CC desensitization. This desensitization is triggered by the influx of
CC calcium ions and is inhibited by elevated ATP levels. Ca(2+) and CALM
CC displace ATP from its binding site and trigger a conformation change
CC that leads to a closed, desensitized channel. Intracellular PIP2
CC inhibits desensitization. The double-knot toxin (DkTx) from the Chinese
CC earth tiger tarantula activates the channel and traps it in an open
CC conformation (By similarity). The Scolopendra mutilans RhTx toxin
CC potentiates the heat activation pathway mediated by this channel by
CC binding to the charge-rich outer pore region (in an activated state)
CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q704Y3}.
CC -!- SUBUNIT: Interacts with PIRT (By similarity). Homotetramer (By
CC similarity). Interacts with TRPV3 and may also form a heteromeric
CC channel with TRPV3 (PubMed:12077606). Interacts with CALM, PRKCM and
CC CSK. Interacts with PRKCG and NTRK1, probably by forming a trimeric
CC complex (By similarity). Interacts with the Scolopendra mutilans RhTx
CC toxin (By similarity). Interacts with TMEM100 (By similarity).
CC Interacts with PACS2 (PubMed:29656858). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q704Y3, ECO:0000269|PubMed:12077606,
CC ECO:0000269|PubMed:29656858}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O35433}. Cell projection, dendritic spine
CC membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O35433}. Cell membrane
CC {ECO:0000269|PubMed:11050376, ECO:0000269|PubMed:11243859,
CC ECO:0000269|PubMed:12077606}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O35433}. Note=Mostly, but not exclusively
CC expressed in postsynaptic dendritic spines.
CC {ECO:0000250|UniProtKB:O35433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NER1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NER1-3; Sequence=VSP_056862;
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels. Expression is
CC elevated in dorsal root ganglia. In skin, expressed in cutaneous
CC sensory nerve fibers, mast cells, epidermal keratinocytes, dermal blood
CC vessels, the inner root sheet and the infundibulum of hair follicles,
CC differentiated sebocytes, sweat gland ducts, and the secretory portion
CC of eccrine sweat glands (at protein level).
CC {ECO:0000269|PubMed:11050376, ECO:0000269|PubMed:11243859,
CC ECO:0000269|PubMed:14987252}.
CC -!- DOMAIN: The association domain (AD) is necessary for self-association.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation by PKA reverses capsaicin-induced
CC dephosphorylation at multiple sites, probably including Ser-117 as a
CC major phosphorylation site. Phosphorylation by CAMKII seems to regulate
CC binding to vanilloids. Phosphorylated and modulated by PRKCE, PRKCM and
CC probably PRKCZ. Dephosphorylation by calcineurin seems to lead to
CC receptor desensitization and phosphorylation by CAMKII recovers
CC activity. {ECO:0000250|UniProtKB:O35433}.
CC -!- MISCELLANEOUS: Responses evoked by low pH and heat, and capsaicin can
CC be antagonized by capsazepine.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG43467.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TRPV1ID50368ch17p13.html";
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DR EMBL; AJ277028; CAB95729.1; -; mRNA.
DR EMBL; AF196175; AAG43466.1; -; mRNA.
DR EMBL; AF196176; AAG43467.1; ALT_FRAME; mRNA.
DR EMBL; AJ272063; CAB89866.2; -; mRNA.
DR EMBL; AY131289; AAM89472.1; -; mRNA.
DR EMBL; DQ177332; ABA06605.1; -; mRNA.
DR EMBL; AL136801; CAB66735.1; -; mRNA.
DR EMBL; AC027796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90497.1; -; Genomic_DNA.
DR EMBL; BC132820; AAI32821.1; -; mRNA.
DR EMBL; BC136633; AAI36634.1; -; mRNA.
DR CCDS; CCDS45576.1; -. [Q8NER1-1]
DR PIR; JC7621; JC7621.
DR RefSeq; NP_061197.4; NM_018727.5. [Q8NER1-1]
DR RefSeq; NP_542435.2; NM_080704.3. [Q8NER1-1]
DR RefSeq; NP_542436.2; NM_080705.3. [Q8NER1-1]
DR RefSeq; NP_542437.2; NM_080706.3. [Q8NER1-1]
DR PDB; 6L93; X-ray; 4.47 A; A/B/C/D/E/F=101-365.
DR PDBsum; 6L93; -.
DR AlphaFoldDB; Q8NER1; -.
DR SMR; Q8NER1; -.
DR BioGRID; 113281; 9.
DR STRING; 9606.ENSP00000459962; -.
DR BindingDB; Q8NER1; -.
DR ChEMBL; CHEMBL4794; -.
DR DrugBank; DB11345; (S)-camphor.
DR DrugBank; DB00316; Acetaminophen.
DR DrugBank; DB00132; alpha-Linolenic acid.
DR DrugBank; DB00168; Aspartame.
DR DrugBank; DB01744; Camphor.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB14050; Cannabidivarin.
DR DrugBank; DB06774; Capsaicin.
DR DrugBank; DB11131; Capsicum oleoresin.
DR DrugBank; DB00159; Icosapent.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB11324; Nonivamide.
DR DrugBank; DB09288; Propacetamol.
DR DrugBank; DB06515; Resiniferatoxin.
DR DrugBank; DB02955; Ricinoleic acid.
DR DrugBank; DB00193; Tramadol.
DR DrugBank; DB09120; Zucapsaicin.
DR DrugCentral; Q8NER1; -.
DR GuidetoPHARMACOLOGY; 507; -.
DR TCDB; 1.A.4.2.13; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q8NER1; 1 site.
DR iPTMnet; Q8NER1; -.
DR PhosphoSitePlus; Q8NER1; -.
DR BioMuta; TRPV1; -.
DR DMDM; 296452849; -.
DR MassIVE; Q8NER1; -.
DR PaxDb; Q8NER1; -.
DR PeptideAtlas; Q8NER1; -.
DR PRIDE; Q8NER1; -.
DR ProteomicsDB; 73202; -. [Q8NER1-1]
DR Antibodypedia; 5472; 553 antibodies from 39 providers.
DR DNASU; 7442; -.
DR Ensembl; ENST00000399756.8; ENSP00000382659.4; ENSG00000196689.13. [Q8NER1-1]
DR Ensembl; ENST00000399759.7; ENSP00000382661.3; ENSG00000196689.13. [Q8NER1-1]
DR Ensembl; ENST00000571088.5; ENSP00000461007.1; ENSG00000196689.13. [Q8NER1-1]
DR Ensembl; ENST00000572705.2; ENSP00000459962.1; ENSG00000196689.13. [Q8NER1-1]
DR GeneID; 7442; -.
DR KEGG; hsa:7442; -.
DR MANE-Select; ENST00000572705.2; ENSP00000459962.1; NM_080704.4; NP_542435.2.
DR UCSC; uc010vrr.3; human. [Q8NER1-1]
DR CTD; 7442; -.
DR DisGeNET; 7442; -.
DR GeneCards; TRPV1; -.
DR HGNC; HGNC:12716; TRPV1.
DR HPA; ENSG00000196689; Tissue enhanced (liver).
DR MIM; 602076; gene.
DR neXtProt; NX_Q8NER1; -.
DR OpenTargets; ENSG00000196689; -.
DR PharmGKB; PA37329; -.
DR VEuPathDB; HostDB:ENSG00000196689; -.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000160870; -.
DR HOGENOM; CLU_012795_1_0_1; -.
DR InParanoid; Q8NER1; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; Q8NER1; -.
DR TreeFam; TF314711; -.
DR PathwayCommons; Q8NER1; -.
DR Reactome; R-HSA-3295583; TRP channels.
DR SignaLink; Q8NER1; -.
DR SIGNOR; Q8NER1; -.
DR BioGRID-ORCS; 7442; 12 hits in 1063 CRISPR screens.
DR ChiTaRS; TRPV1; human.
DR GeneWiki; TRPV1; -.
DR GenomeRNAi; 7442; -.
DR Pharos; Q8NER1; Tclin.
DR PRO; PR:Q8NER1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8NER1; protein.
DR Bgee; ENSG00000196689; Expressed in right lobe of liver and 113 other tissues.
DR ExpressionAtlas; Q8NER1; baseline and differential.
DR Genevisible; Q8NER1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0017081; F:chloride channel regulator activity; IEA:Ensembl.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
DR GO; GO:0097603; F:temperature-gated ion channel activity; IEA:Ensembl.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; TAS:Reactome.
DR GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0007635; P:chemosensory behavior; TAS:ProtInc.
DR GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; IEA:Ensembl.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; IEA:Ensembl.
DR GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
DR GO; GO:0001660; P:fever generation; IEA:Ensembl.
DR GO; GO:0014047; P:glutamate secretion; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR GO; GO:0090212; P:negative regulation of establishment of blood-brain barrier; IEA:Ensembl.
DR GO; GO:0010459; P:negative regulation of heart rate; IEA:Ensembl.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IEA:Ensembl.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0002790; P:peptide secretion; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0060454; P:positive regulation of gastric acid secretion; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:1901594; P:response to capsazepine; IMP:UniProtKB.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0050954; P:sensory perception of mechanical stimulus; IEA:Ensembl.
DR GO; GO:0060083; P:smooth muscle contraction involved in micturition; IEA:Ensembl.
DR GO; GO:0050955; P:thermoception; IDA:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR024862; TRPV.
DR InterPro; IPR024863; TRPV1.
DR InterPro; IPR008347; TrpV1-4.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR PANTHER; PTHR10582:SF17; PTHR10582:SF17; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01768; TRPVRECEPTOR.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; ATP-binding; Calcium;
KW Calcium channel; Calcium transport; Calmodulin-binding; Cell membrane;
KW Cell projection; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..839
FT /note="Transient receptor potential cation channel
FT subfamily V member 1"
FT /id="PRO_0000215338"
FT TOPO_DOM 1..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 455..471
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 472..497
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 498..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 532..535
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 557..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 572..599
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 600..658
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 659..687
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 688..839
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT REPEAT 111..153
FT /note="ANK 1"
FT REPEAT 154..200
FT /note="ANK 2"
FT REPEAT 201..247
FT /note="ANK 3"
FT REPEAT 248..283
FT /note="ANK 4"
FT REPEAT 284..332
FT /note="ANK 5"
FT REPEAT 333..359
FT /note="ANK 6"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..713
FT /note="AD"
FT /evidence="ECO:0000250"
FT REGION 768..802
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT REGION 778..793
FT /note="Required for PIP2-mediated channel inhibition"
FT /evidence="ECO:0000250"
FT MOTIF 644..647
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 200..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 211..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 511..512
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 550
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 557
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 647
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT MOD_RES 117
FT /note="Phosphoserine; by PKA and PKD"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 145
FT /note="Phosphothreonine; by PKA; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 371
FT /note="Phosphothreonine; by PKA; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 502
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 705
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 801
FT /note="Phosphoserine; by PKC/PRKCE and PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..150
FT /note="MKKWSSTDLGAAADPLQKDTCPDPLDGDPNSRPPPAKPQLSTAKSRTRLFGK
FT GDSEEAFPVDCPHEEGELDSCPTITVSPVITIQRPGDGPTGARLLSQDSVAASTEKTLR
FT LYDRRSIFEAVAQNNCQDLESLLLFLQKSKKHLTDNEFK -> METLTPGHLQPSPSSP
FT RPRAAPGSLGRVTRRRLSRWIALTRKVSWTPARPSQSALLSPSRGQETAPPVPGCCPRT
FT LSPPAPRRPSGSMIAGVSLKPLLRITARIWRACCSSCRRARSTSQTTSSKVAPALGSGR
FT APALACPDPPLCLS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_056862"
FT VARIANT 91
FT /note="P -> S (in dbSNP:rs222749)"
FT /evidence="ECO:0000269|PubMed:11243859"
FT /id="VAR_057307"
FT VARIANT 315
FT /note="M -> I (in dbSNP:rs222747)"
FT /evidence="ECO:0000269|PubMed:11050376,
FT ECO:0000269|PubMed:11226139, ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:11243859, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.5, ECO:0000269|Ref.8"
FT /id="VAR_071244"
FT VARIANT 469
FT /note="T -> I (in dbSNP:rs224534)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:11243859"
FT /id="VAR_057308"
FT VARIANT 505
FT /note="T -> A (in dbSNP:rs17633288)"
FT /id="VAR_057309"
FT VARIANT 585
FT /note="I -> V (in dbSNP:rs8065080)"
FT /evidence="ECO:0000269|PubMed:11050376, ECO:0000269|Ref.5"
FT /id="VAR_022246"
FT MUTAGEN 511
FT /note="Y->A: Loss of sensitivity to capsaicin."
FT /evidence="ECO:0000269|PubMed:14996838"
FT MUTAGEN 550
FT /note="T->I: Reduces sensitivity to capsaicin 40-fold."
FT /evidence="ECO:0000269|PubMed:14996838"
FT CONFLICT 336
FT /note="T -> M (in Ref. 3; CAB89866)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="M -> V (in Ref. 5; ABA06605)"
FT /evidence="ECO:0000305|Ref.5"
SQ SEQUENCE 839 AA; 94956 MW; 7142F59D428827FB CRC64;
MKKWSSTDLG AAADPLQKDT CPDPLDGDPN SRPPPAKPQL STAKSRTRLF GKGDSEEAFP
VDCPHEEGEL DSCPTITVSP VITIQRPGDG PTGARLLSQD SVAASTEKTL RLYDRRSIFE
AVAQNNCQDL ESLLLFLQKS KKHLTDNEFK DPETGKTCLL KAMLNLHDGQ NTTIPLLLEI
ARQTDSLKEL VNASYTDSYY KGQTALHIAI ERRNMALVTL LVENGADVQA AAHGDFFKKT
KGRPGFYFGE LPLSLAACTN QLGIVKFLLQ NSWQTADISA RDSVGNTVLH ALVEVADNTA
DNTKFVTSMY NEILMLGAKL HPTLKLEELT NKKGMTPLAL AAGTGKIGVL AYILQREIQE
PECRHLSRKF TEWAYGPVHS SLYDLSCIDT CEKNSVLEVI AYSSSETPNR HDMLLVEPLN
RLLQDKWDRF VKRIFYFNFL VYCLYMIIFT MAAYYRPVDG LPPFKMEKTG DYFRVTGEIL
SVLGGVYFFF RGIQYFLQRR PSMKTLFVDS YSEMLFFLQS LFMLATVVLY FSHLKEYVAS
MVFSLALGWT NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYIVFLFG FSTAVVTLIE
DGKNDSLPSE STSHRWRGPA CRPPDSSYNS LYSTCLELFK FTIGMGDLEF TENYDFKAVF
IILLLAYVIL TYILLLNMLI ALMGETVNKI AQESKNIWKL QRAITILDTE KSFLKCMRKA
FRSGKLLQVG YTPDGKDDYR WCFRVDEVNW TTWNTNVGII NEDPGNCEGV KRTLSFSLRS
SRVSGRHWKN FALVPLLREA SARDRQSAQP EEVYLRQFSG SLKPEDAEVF KSPAASGEK
