[1]
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NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT VAL-585.
DOI=10.1016/S0304-3959(00)00353-5; PubMed=11050376 [NCBI, ExPASy, EBI, Israel, Japan]
Hayes P.,
Meadows H.J.,
Gunthorpe M.,
Harries M.H.,
Duckworth M.D.,
Cairns W.,
Harrison D.C.,
Clarke C.,
Ellington K.,
Prinjha R.K.,
Barton A.J.,
Medhurst A.D.,
Smith G.D.,
Topp S.,
Murdock P.,
Sanger G.J.,
Terrett J.,
Jenkins O.,
Benham C.D., ![]()
Randall A.D.,
Gloger I.S.,
Davis J.B.;
"Cloning and functional expression of a human orthologue of rat vanilloid receptor-1.";
Pain 88:205-215(2000).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Spinal ganglion;
DOI=10.1006/bbrc.2001.4482; PubMed=11243859 [NCBI, ExPASy, EBI, Israel, Japan]
Cortright D.N.,
Crandall M.,
Sanchez J.F.,
Zou T.,
Krause J.E.,
White G.;
"The tissue distribution and functional characterization of human VR1.";
Biochem. Biophys. Res. Commun. 281:1183-1189(2001).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Spinal ganglion;
DOI=10.1038/sj.bjp.0703918; PubMed=11226139 [NCBI, ExPASy, EBI, Israel, Japan]
McIntyre P.,
McLatchie L.,
Chambers A.,
Phillips E.,
Clarke M.,
Savidge J.,
Peacock M.,
Shah K.,
Winter J.,
Weerasekera N.,
Webb M.,
Rang H.,
Bevan S.,
James I.;
"Pharmacological differences between human and rat vanilloid receptor 1 (VR1).";
Br. J. Pharmacol. 132:1084-1094(2001).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Lee D.,
Ha I.;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan]
Wiemann S.,
Weil B.,
Wellenreuther R.,
Gassenhuber J.,
Glassl S.,
Ansorge W.,
Boecher M.,
Bloecker H.,
Bauersachs S.,
Blum H.,
Lauber J.,
Duesterhoeft A.,
Beyer A.,
Koehrer K.,
Strack N.,
Mewes H.-W.,
Ottenwaelder B.,
Obermaier B.,
Tampe J., ![]()
Heubner D.,
Wambutt R.,
Korn B.,
Klein M.,
Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
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[6]
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INTERACTION WITH TRPV3.
DOI=10.1038/nature00894; PubMed=12077606 [NCBI, ExPASy, EBI, Israel, Japan]
Smith G.D.,
Gunthorpe M.J.,
Kelsell R.E.,
Hayes P.D.,
Reilly P.,
Facer P.,
Wright J.E.,
Jerman J.C.,
Walhin J.-P.,
Ooi L.,
Egerton J.,
Charles K.J.,
Smart D.,
Randall A.D.,
Anand P.,
Davis J.B.;
"TRPV3 is a temperature-sensitive vanilloid receptor-like protein.";
Nature 418:186-190(2002).
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[7]
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TISSUE SPECIFICITY.
DOI=10.1111/j.0906-6705.2004.0178.x; PubMed=14987252 [NCBI, ExPASy, EBI, Israel, Japan]
Staender S.,
Moormann C.,
Schumacher M.,
Buddenkotte J.,
Artuc M.,
Shpacovitch V.,
Brzoska T.,
Lippert U.,
Henz B.M.,
Luger T.A.,
Metze D.,
Steinhoff M.;
"Expression of vanilloid receptor subtype 1 in cutaneous sensory nerve fibers, mast cells, and epithelial cells of appendage structures.";
Exp. Dermatol. 13:129-139(2004).
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[8]
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MUTAGENESIS OF TYR-511 AND THR-550.
DOI=10.1074/jbc.M312577200; PubMed=14996838 [NCBI, ExPASy, EBI, Israel, Japan]
Gavva N.R.,
Klionsky L.,
Qu Y.,
Shi L.,
Tamir R.,
Edenson S.,
Zhang T.J.,
Viswanadhan V.N.,
Toth A.,
Pearce L.V.,
Vanderah T.W.,
Porreca F.,
Blumberg P.M.,
Lile J.,
Sun Y.,
Wild K.,
Louis J.C.,
Treanor J.J.;
"Molecular determinants of vanilloid sensitivity in TRPV1.";
J. Biol. Chem. 279:20283-20295(2004).
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- FUNCTION: Receptor-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. May be involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL.
- ENZYME REGULATION: Channel activity is activated via the interaction with PIRT and phosphatidylinositol-4,5-bisphosphate (PIP2). Both PIRT and PIP2 are required to activate channel activity (By similarity).
- SUBUNIT: Self-associates. Probably homotetramer. May also form a heteromeric channel with TRPV3. Interacts with calmodulin, PIRT, PRKCM and CSK. Interacts with PRKCG and NTRK1, probably by forming a trimeric complex (By similarity).
- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (By similarity).
- TISSUE SPECIFICITY: Widely expressed at low levels. Expression is elevated in dorsal root ganglia. In skin, expressed in cutaneous sensory nerve fibers, mast cells, epidermal keratinocytes, dermal blood vessels, the inner root sheet and the infundibulum of hair follicles, differentiated sebocytes, sweat gland ducts, and the secretory portion of eccrine sweat glands (at protein level).
- DOMAIN: The association domain (AD) is necessary for self-association (By similarity).
- PTM: Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-117 as a major phosphorylation site. Phoshphorylation by CAMKII seems to regulate binding to vanilloids. Phosphorylated and modulated by PKCM and probably PKCZ. Dephosphorylation by calcineurin seems to lead to receptor desensitization and phosphorylation by CAMKII recovers activity (By similarity).
- MISCELLANEOUS: Responses evoked by low pH and heat, and capsaicin can be antagonized by capsazepine.
- SIMILARITY: Belongs to the transient receptor family. TrpV subfamily.
- SIMILARITY: Contains 6 ANK repeats.
- SEQUENCE CAUTION:
- Sequence=AAG43467.1; Type=Frameshift; Positions=498;
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