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 24-JAN-2024, entry version 178. 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="https://atlasgeneticsoncology.org/gene/50368/TRPV1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8GF8; EM; 2.90 A; A/B/C/D=2-839. DR PDB; 8GF9; EM; 2.58 A; A/B/C/D=2-839. DR PDB; 8GFA; EM; 2.29 A; A/B/C/D=2-839. DR PDBsum; 6L93; -. DR PDBsum; 8GF8; -. DR PDBsum; 8GF9; -. DR PDBsum; 8GFA; -. DR AlphaFoldDB; Q8NER1; -. DR SMR; Q8NER1; -. DR BioGRID; 113281; 10. 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 ca2+/cation channel (trp-cc) family. DR GlyCosmos; Q8NER1; 1 site, No reported glycans. DR GlyGen; Q8NER1; 1 site. DR iPTMnet; Q8NER1; -. DR PhosphoSitePlus; Q8NER1; -. DR BioMuta; TRPV1; -. DR DMDM; 296452849; -. DR MassIVE; Q8NER1; -. DR PaxDb; 9606-ENSP00000459962; -. DR PeptideAtlas; Q8NER1; -. DR ProteomicsDB; 73202; -. [Q8NER1-1] DR Antibodypedia; 5472; 616 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 AGR; HGNC:12716; -. 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; 1003028at2759; -. 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; 13 hits in 1148 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 115 other cell types or tissues. DR ExpressionAtlas; Q8NER1; baseline and differential. 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:0016020; C:membrane; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. 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; TAS:Reactome. 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 monoatomic ion channel activity; ISS:UniProtKB. DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. 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: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 CDD; cd22196; TRPV1; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 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; IPR008347; TrpV1-4. DR NCBIfam; TIGR00870; trp; 1. DR PANTHER; PTHR10582:SF17; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V MEMBER 1; 1. DR PANTHER; PTHR10582; TRANSIENT RECEPTOR POTENTIAL ION CHANNEL PROTEIN; 1. DR Pfam; PF00023; Ank; 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; Ankyrin repeat; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR Genevisible; Q8NER1; HS. 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 //