Transient receptor potential cation channel subfamily V member 1

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Reviewed, UniProtKB/Swiss-Prot Q8NER1 (TRPV1_HUMAN)

Last modified July 7, 2009. Version 57. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Transient receptor potential cation channel subfamily V member 1
      Short name=TrpV1
Alternative name(s):
    Osm-9-like TRP channel 1
      Short name=OTRPC1
    Vanilloid receptor 1
    Capsaicin receptor

Gene names

Name:	TRPV1
Synonyms:	VR1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	839 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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. Ref.1 Ref.2 Ref.3
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 structure	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). Ref.1 Ref.2 Ref.7
Domain	The association domain (AD) is necessary for self-association By similarity.
Post-translational modification	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.
Sequence similarities	Belongs to the transient receptor family. TrpV subfamily. Contains 6 ANK repeats.
Sequence caution	The sequence AAG43467.1 differs from that shown. Reason: Frameshift at position 498.

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Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat Transmembrane
Ligand	ATP-binding Calcium Calmodulin-binding Nucleotide-binding
Molecular function	Calcium channel Ionic channel
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW cell surface receptor linked signal transduction Traceable author statement. Source: ProtInc chemosensory behavior Traceable author statement. Source: ProtInc thermoception Inferred from direct assay. Source: MGI
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium channel activity Traceable author statement. Source: ProtInc calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 839

839

Transient receptor potential cation channel subfamily V member 1

PRO_0000215338

Regions

Topological domain

1 – 433

433

Cytoplasmic Potential

Transmembrane

434 – 454

Potential

Topological domain

455 – 476

Extracellular Potential

Transmembrane

477 – 497

Potential

Topological domain

498 – 513

Cytoplasmic Potential

Transmembrane

514 – 534

Potential

Topological domain

535

Extracellular Potential

Transmembrane

536 – 556

Potential

Topological domain

557 – 579

Cytoplasmic Potential

Transmembrane

580 – 600

Potential

Topological domain

601 – 659

Pore forming Probable

Transmembrane

660 – 680

Potential

Topological domain

681 – 839

159

Cytoplasmic Potential

Repeat

111 – 153

ANK 1

Repeat

154 – 200

ANK 2

Repeat

201 – 247

ANK 3

Repeat

248 – 283

ANK 4

Repeat

284 – 332

ANK 5

Repeat

333 – 359

ANK 6

Region

685 – 713

AD By similarity

Region

768 – 802

Interaction with calmodulin By similarity

Region

778 – 793

Required for PIP2-mediated channel inhibition By similarity

Amino acid modifications

Modified residue

117

Phosphoserine By similarity

Modified residue

145

Phosphothreonine By similarity

Modified residue

371

Phosphothreonine By similarity

Modified residue

502

Phosphoserine By similarity

Modified residue

705

Phosphothreonine By similarity

Modified residue

775

Phosphoserine By similarity

Modified residue

801

Phosphoserine By similarity

Modified residue

821

Phosphoserine By similarity

Glycosylation

604

N-linked (GlcNAc...) By similarity

Natural variations

Natural variant

P → S: dbSNP rs222749.

VAR_057307

Natural variant

469

T → I: dbSNP rs224534.

VAR_057308

Natural variant

505

T → A: dbSNP rs17633288.

VAR_057309

Natural variant

585

I → V Ref.1

VAR_022246

Experimental info

Mutagenesis

511

Y → A: Loss of sensitivity to capsaicin. Ref.8

Mutagenesis

550

T → I: Reduces sensitivity to capsaicin 40-fold. Ref.8

Sequence conflict

315

I → M in AAG43466. Ref.2

Sequence conflict

336

T → M in CAB89866. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8NER1-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 7142F59D4318996F
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FASTA

839

94,938

        10         20         30         40         50         60 
MKKWSSTDLG AAADPLQKDT CPDPLDGDPN SRPPPAKPQL STAKSRTRLF GKGDSEEAFP 

        70         80         90        100        110        120 
VDCPHEEGEL DSCPTITVSP VITIQRPGDG PTGARLLSQD SVAASTEKTL RLYDRRSIFE 

       130        140        150        160        170        180 
AVAQNNCQDL ESLLLFLQKS KKHLTDNEFK DPETGKTCLL KAMLNLHDGQ NTTIPLLLEI 

       190        200        210        220        230        240 
ARQTDSLKEL VNASYTDSYY KGQTALHIAI ERRNMALVTL LVENGADVQA AAHGDFFKKT 

       250        260        270        280        290        300 
KGRPGFYFGE LPLSLAACTN QLGIVKFLLQ NSWQTADISA RDSVGNTVLH ALVEVADNTA 

       310        320        330        340        350        360 
DNTKFVTSMY NEILILGAKL HPTLKLEELT NKKGMTPLAL AAGTGKIGVL AYILQREIQE 

       370        380        390        400        410        420 
PECRHLSRKF TEWAYGPVHS SLYDLSCIDT CEKNSVLEVI AYSSSETPNR HDMLLVEPLN 

       430        440        450        460        470        480 
RLLQDKWDRF VKRIFYFNFL VYCLYMIIFT MAAYYRPVDG LPPFKMEKTG DYFRVTGEIL 

       490        500        510        520        530        540 
SVLGGVYFFF RGIQYFLQRR PSMKTLFVDS YSEMLFFLQS LFMLATVVLY FSHLKEYVAS 

       550        560        570        580        590        600 
MVFSLALGWT NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYIVFLFG FSTAVVTLIE 

       610        620        630        640        650        660 
DGKNDSLPSE STSHRWRGPA CRPPDSSYNS LYSTCLELFK FTIGMGDLEF TENYDFKAVF 

       670        680        690        700        710        720 
IILLLAYVIL TYILLLNMLI ALMGETVNKI AQESKNIWKL QRAITILDTE KSFLKCMRKA 

       730        740        750        760        770        780 
FRSGKLLQVG YTPDGKDDYR WCFRVDEVNW TTWNTNVGII NEDPGNCEGV KRTLSFSLRS 

       790        800        810        820        830 
SRVSGRHWKN FALVPLLREA SARDRQSAQP EEVYLRQFSG SLKPEDAEVF KSPAASGEK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional expression of a human orthologue of rat vanilloid receptor-1." 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. Davis J.B. Pain 88:205-215(2000) [PubMed: 11050376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT VAL-585.
[2]	"The tissue distribution and functional characterization of human VR1." Cortright D.N., Crandall M., Sanchez J.F., Zou T., Krause J.E., White G. Biochem. Biophys. Res. Commun. 281:1183-1189(2001) [PubMed: 11243859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANTS SER-91 AND ILE-469. Tissue: Spinal ganglion.
[3]	"Pharmacological differences between human and rat vanilloid receptor 1 (VR1)." 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. Br. J. Pharmacol. 132:1084-1094(2001) [PubMed: 11226139] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: Spinal ganglion.
[4]	Lee D., Ha I. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[5]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." 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. Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-469. Tissue: Testis.
[6]	"TRPV3 is a temperature-sensitive vanilloid receptor-like protein." 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. Nature 418:186-190(2002) [PubMed: 12077606] [Abstract] Cited for: INTERACTION WITH TRPV3.
[7]	"Expression of vanilloid receptor subtype 1 in cutaneous sensory nerve fibers, mast cells, and epithelial cells of appendage structures." 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. Exp. Dermatol. 13:129-139(2004) [PubMed: 14987252] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Molecular determinants of vanilloid sensitivity in TRPV1." 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. J. Biol. Chem. 279:20283-20295(2004) [PubMed: 14996838] [Abstract] Cited for: MUTAGENESIS OF TYR-511 AND THR-550.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AJ277028 mRNA. Translation: CAB95729.1. AF196175 mRNA. Translation: AAG43466.1. AF196176 mRNA. Translation: AAG43467.1. Frameshift. AJ272063 mRNA. Translation: CAB89866.2. AY131289 mRNA. Translation: AAM89472.1. AL136801 mRNA. Translation: CAB66735.1.
IPI	IPI00874241.
PIR	JC7621.
RefSeq	NP_061197.4. NP_542435.2. NP_542436.2. NP_542437.2.
UniGene	Hs.579217 Hs.655380
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q8NER1.
Proteomic databases
PRIDE	Q8NER1.
Genome annotation databases
Ensembl	ENSG00000196689. Homo sapiens. [Contig view]
GeneID	7442.
KEGG	hsa:7442.
Organism-specific databases
GeneCards	GC17M003415.
H-InvDB	HIX0013428. HIX0079948.
HGNC	HGNC:12716. TRPV1.
MIM	602076. gene.
PharmGKB	PA37329.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q8NER1.
Enzyme and pathway databases
Pathway_Interaction_DB	pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma. mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.
Gene expression databases
ArrayExpress	Q8NER1.
Bgee	Q8NER1.
CleanEx	HS_TRPV1.
GermOnline	ENSG00000196689. Homo sapiens.
Family and domain databases
InterPro	IPR002110. ANK. IPR005821. Ion_trans. IPR004729. TRP_channel. IPR008347. Vanilpoid_rcpt. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit.
Pfam	PF00023. Ank. 3 hits. PF00520. Ion_trans. 1 hit. [Graphical view]
PRINTS	PR01768. TRPVRECEPTOR.
SMART	SM00248. ANK. 4 hits. [Graphical view]
TIGRFAMs	TIGR00870. trp. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
BindingDB	Q8NER1.
DrugBank	DB00132. Alpha-Linolenic Acid. DB00168. Aspartame. DB00159. Icosapent.
NextBio	29140.
SOURCE	Search...

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Entry information

Entry name

TRPV1_HUMAN

Accession

Primary (citable) accession number: Q8NER1
Secondary accession number(s): Q9H0G9

Q9NY22

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	October 1, 2002
Last modified:	July 7, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents