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Q8NER1

- TRPV1_HUMAN

UniProt

Q8NER1 - TRPV1_HUMAN

Protein

Transient receptor potential cation channel subfamily V member 1

Gene

TRPV1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Ligand-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. 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. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis By similarity. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca2+-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel.By similarity4 Publications

    Enzyme regulationi

    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. The channel is sensitized by ATP binding. Repeated stimulation with capsaicin gives rise to progressively smaller responses, due to desensitization. This desensitization is triggered by the influx of calcium ions and is inhibited by elevated ATP levels. Ca2+ and CALM displace ATP from its binding site and trigger a conformation change that leads to a closed, desensitized channel. Intracellular PIP2 inhibits desensitization. The double-knot toxin (DkTx) from the Chinese earth tiger tarantula activates the channel and traps it in an open conformation By similarity.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. calcium channel activity Source: ProtInc
    3. calcium-release channel activity Source: UniProtKB
    4. excitatory extracellular ligand-gated ion channel activity Source: UniProtKB
    5. phosphoprotein binding Source: UniProt
    6. transmembrane signaling receptor activity Source: UniProtKB

    GO - Biological processi

    1. calcium ion transmembrane transport Source: UniProtKB
    2. cell surface receptor signaling pathway Source: ProtInc
    3. cellular response to alkaloid Source: UniProtKB
    4. cellular response to ATP Source: UniProtKB
    5. chemosensory behavior Source: ProtInc
    6. ion transmembrane transport Source: Reactome
    7. thermoception Source: MGI
    8. transmembrane transport Source: Reactome
    9. transport Source: ProtInc

    Keywords - Molecular functioni

    Calcium channel, Ion channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_169333. TRP channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transient receptor potential cation channel subfamily V member 1
    Short name:
    TrpV1
    Alternative name(s):
    Capsaicin receptor
    Osm-9-like TRP channel 1
    Short name:
    OTRPC1
    Vanilloid receptor 1
    Gene namesi
    Name:TRPV1
    Synonyms:VR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:12716. TRPV1.

    Subcellular locationi

    Cell junctionsynapsepostsynaptic cell membrane By similarity; Multi-pass membrane protein By similarity. Cell projectiondendritic spine membrane By similarity; Multi-pass membrane protein By similarity. Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Mostly, but not exclusively expressed in postsynaptic dendritic spines.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. dendritic spine membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: MGI
    4. integral component of plasma membrane Source: ProtInc
    5. intrinsic component of plasma membrane Source: UniProtKB
    6. plasma membrane Source: Reactome
    7. postsynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi511 – 5111Y → A: Loss of sensitivity to capsaicin. 1 Publication
    Mutagenesisi550 – 5501T → I: Reduces sensitivity to capsaicin 40-fold. 1 Publication

    Organism-specific databases

    PharmGKBiPA37329.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 839839Transient receptor potential cation channel subfamily V member 1PRO_0000215338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei117 – 1171PhosphoserineBy similarity
    Modified residuei145 – 1451PhosphothreonineBy similarity
    Modified residuei371 – 3711PhosphothreonineBy similarity
    Modified residuei502 – 5021Phosphoserine; by PKC/PRKCEBy similarity
    Glycosylationi604 – 6041N-linked (GlcNAc...)By similarity
    Modified residuei705 – 7051PhosphothreonineBy similarity
    Modified residuei775 – 7751PhosphoserineBy similarity
    Modified residuei801 – 8011Phosphoserine; by PKC/PRKCEBy similarity
    Modified residuei821 – 8211PhosphoserineBy similarity

    Post-translational modificationi

    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 PRKCE, PRKCM and probably PRKCZ. Dephosphorylation by calcineurin seems to lead to receptor desensitization and phosphorylation by CAMKII recovers activity By similarity.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ8NER1.
    PRIDEiQ8NER1.

    PTM databases

    PhosphoSiteiQ8NER1.

    Expressioni

    Tissue specificityi

    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).3 Publications

    Gene expression databases

    BgeeiQ8NER1.
    CleanExiHS_TRPV1.
    GenevestigatoriQ8NER1.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with CALM, PRKCM and CSK. Interacts with PRKCG and NTRK1, probably by forming a trimeric complex. Interacts with PIRT By similarity. Interacts with TRPV3 and may also form a heteromeric channel with TRPV3.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi113281. 7 interactions.
    MINTiMINT-4721979.
    STRINGi9606.ENSP00000174621.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NER1.
    SMRiQ8NER1. Positions 112-720.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 433433CytoplasmicBy similarityAdd
    BLAST
    Topological domaini455 – 47117ExtracellularBy similarityAdd
    BLAST
    Topological domaini498 – 51013CytoplasmicBy similarityAdd
    BLAST
    Topological domaini532 – 5354ExtracellularBy similarity
    Topological domaini557 – 57115CytoplasmicBy similarityAdd
    BLAST
    Topological domaini600 – 62728ExtracellularBy similarityAdd
    BLAST
    Topological domaini688 – 839152CytoplasmicBy similarityAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei628 – 65023Pore-formingBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei434 – 45421HelicalBy similarityAdd
    BLAST
    Transmembranei472 – 49726HelicalBy similarityAdd
    BLAST
    Transmembranei511 – 53121HelicalBy similarityAdd
    BLAST
    Transmembranei536 – 55621HelicalBy similarityAdd
    BLAST
    Transmembranei572 – 59928HelicalBy similarityAdd
    BLAST
    Transmembranei659 – 68729HelicalBy similarityAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati111 – 15343ANK 1Add
    BLAST
    Repeati154 – 20047ANK 2Add
    BLAST
    Repeati201 – 24747ANK 3Add
    BLAST
    Repeati248 – 28336ANK 4Add
    BLAST
    Repeati284 – 33249ANK 5Add
    BLAST
    Repeati333 – 35927ANK 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni685 – 71329ADBy similarityAdd
    BLAST
    Regioni768 – 80235Interaction with calmodulinBy similarityAdd
    BLAST
    Regioni778 – 79316Required for PIP2-mediated channel inhibitionBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi644 – 6474Selectivity filterBy similarity

    Domaini

    The association domain (AD) is necessary for self-association.By similarity

    Sequence similaritiesi

    Contains 6 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG278734.
    HOVERGENiHBG054085.
    KOiK05222.
    OrthoDBiEOG7WHH8R.
    PhylomeDBiQ8NER1.
    TreeFamiTF314711.

    Family and domain databases

    Gene3Di1.25.40.20. 2 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR004729. TRP_channel.
    IPR008347. TRPV1-4_channel.
    IPR024863. TRPV1_channel.
    [Graphical view]
    PANTHERiPTHR10582:SF17. PTHR10582:SF17. 1 hit.
    PfamiPF12796. Ank_2. 1 hit.
    [Graphical view]
    PRINTSiPR01768. TRPVRECEPTOR.
    SMARTiSM00248. ANK. 4 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    TIGRFAMsiTIGR00870. trp. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8NER1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKWSSTDLG AAADPLQKDT CPDPLDGDPN SRPPPAKPQL STAKSRTRLF    50
    GKGDSEEAFP VDCPHEEGEL DSCPTITVSP VITIQRPGDG PTGARLLSQD 100
    SVAASTEKTL RLYDRRSIFE AVAQNNCQDL ESLLLFLQKS KKHLTDNEFK 150
    DPETGKTCLL KAMLNLHDGQ NTTIPLLLEI ARQTDSLKEL VNASYTDSYY 200
    KGQTALHIAI ERRNMALVTL LVENGADVQA AAHGDFFKKT KGRPGFYFGE 250
    LPLSLAACTN QLGIVKFLLQ NSWQTADISA RDSVGNTVLH ALVEVADNTA 300
    DNTKFVTSMY NEILMLGAKL HPTLKLEELT NKKGMTPLAL AAGTGKIGVL 350
    AYILQREIQE PECRHLSRKF TEWAYGPVHS SLYDLSCIDT CEKNSVLEVI 400
    AYSSSETPNR HDMLLVEPLN RLLQDKWDRF VKRIFYFNFL VYCLYMIIFT 450
    MAAYYRPVDG LPPFKMEKTG DYFRVTGEIL SVLGGVYFFF RGIQYFLQRR 500
    PSMKTLFVDS YSEMLFFLQS LFMLATVVLY FSHLKEYVAS MVFSLALGWT 550
    NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYIVFLFG FSTAVVTLIE 600
    DGKNDSLPSE STSHRWRGPA CRPPDSSYNS LYSTCLELFK FTIGMGDLEF 650
    TENYDFKAVF IILLLAYVIL TYILLLNMLI ALMGETVNKI AQESKNIWKL 700
    QRAITILDTE KSFLKCMRKA FRSGKLLQVG YTPDGKDDYR WCFRVDEVNW 750
    TTWNTNVGII NEDPGNCEGV KRTLSFSLRS SRVSGRHWKN FALVPLLREA 800
    SARDRQSAQP EEVYLRQFSG SLKPEDAEVF KSPAASGEK 839
    Length:839
    Mass (Da):94,956
    Last modified:May 18, 2010 - v2
    Checksum:i7142F59D428827FB
    GO

    Sequence cautioni

    The sequence AAG43467.1 differs from that shown. Reason: Frameshift at position 498.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti315 – 3151M → I in CAB95729. (PubMed:11050376)Curated
    Sequence conflicti315 – 3151M → I in AAG43467. (PubMed:11243859)Curated
    Sequence conflicti315 – 3151M → I in CAB89866. (PubMed:11226139)Curated
    Sequence conflicti315 – 3151M → I in AAM89472. 1 PublicationCurated
    Sequence conflicti315 – 3151M → I in CAB66735. (PubMed:11230166)Curated
    Sequence conflicti315 – 3151M → I in EAW90497. 1 PublicationCurated
    Sequence conflicti315 – 3151M → I in AAI32821. (PubMed:15489334)Curated
    Sequence conflicti315 – 3151M → I in AAI36634. (PubMed:15489334)Curated
    Sequence conflicti336 – 3361T → M in CAB89866. (PubMed:11226139)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911P → S.1 Publication
    Corresponds to variant rs222749 [ dbSNP | Ensembl ].
    VAR_057307
    Natural varianti469 – 4691T → I.2 Publications
    Corresponds to variant rs224534 [ dbSNP | Ensembl ].
    VAR_057308
    Natural varianti505 – 5051T → A.
    Corresponds to variant rs17633288 [ dbSNP | Ensembl ].
    VAR_057309
    Natural varianti585 – 5851I → V.1 Publication
    Corresponds to variant rs8065080 [ dbSNP | Ensembl ].
    VAR_022246

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    AC027796 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90497.1.
    BC132820 mRNA. Translation: AAI32821.1.
    BC136633 mRNA. Translation: AAI36634.1.
    CCDSiCCDS45576.1.
    PIRiJC7621.
    RefSeqiNP_061197.4. NM_018727.5.
    NP_542435.2. NM_080704.3.
    NP_542436.2. NM_080705.3.
    NP_542437.2. NM_080706.3.
    UniGeneiHs.579217.
    Hs.655380.

    Genome annotation databases

    EnsembliENST00000572705; ENSP00000459962; ENSG00000262304.
    GeneIDi7442.
    KEGGihsa:7442.
    UCSCiuc010vrr.2. human.

    Polymorphism databases

    DMDMi296452849.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    AC027796 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90497.1 .
    BC132820 mRNA. Translation: AAI32821.1 .
    BC136633 mRNA. Translation: AAI36634.1 .
    CCDSi CCDS45576.1.
    PIRi JC7621.
    RefSeqi NP_061197.4. NM_018727.5.
    NP_542435.2. NM_080704.3.
    NP_542436.2. NM_080705.3.
    NP_542437.2. NM_080706.3.
    UniGenei Hs.579217.
    Hs.655380.

    3D structure databases

    ProteinModelPortali Q8NER1.
    SMRi Q8NER1. Positions 112-720.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113281. 7 interactions.
    MINTi MINT-4721979.
    STRINGi 9606.ENSP00000174621.

    Chemistry

    BindingDBi Q8NER1.
    ChEMBLi CHEMBL4794.
    DrugBanki DB00132. Alpha-Linolenic Acid.
    DB00168. Aspartame.
    DB00159. Icosapent.
    GuidetoPHARMACOLOGYi 507.

    PTM databases

    PhosphoSitei Q8NER1.

    Polymorphism databases

    DMDMi 296452849.

    Proteomic databases

    PaxDbi Q8NER1.
    PRIDEi Q8NER1.

    Protocols and materials databases

    DNASUi 7442.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000572705 ; ENSP00000459962 ; ENSG00000262304 .
    GeneIDi 7442.
    KEGGi hsa:7442.
    UCSCi uc010vrr.2. human.

    Organism-specific databases

    CTDi 7442.
    GeneCardsi GC17M003469.
    H-InvDB HIX0013428.
    HIX0079948.
    HGNCi HGNC:12716. TRPV1.
    MIMi 602076. gene.
    neXtProti NX_Q8NER1.
    PharmGKBi PA37329.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278734.
    HOVERGENi HBG054085.
    KOi K05222.
    OrthoDBi EOG7WHH8R.
    PhylomeDBi Q8NER1.
    TreeFami TF314711.

    Enzyme and pathway databases

    Reactomei REACT_169333. TRP channels.

    Miscellaneous databases

    GeneWikii TRPV1.
    GenomeRNAii 7442.
    NextBioi 29140.
    PROi Q8NER1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8NER1.
    CleanExi HS_TRPV1.
    Genevestigatori Q8NER1.

    Family and domain databases

    Gene3Di 1.25.40.20. 2 hits.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR004729. TRP_channel.
    IPR008347. TRPV1-4_channel.
    IPR024863. TRPV1_channel.
    [Graphical view ]
    PANTHERi PTHR10582:SF17. PTHR10582:SF17. 1 hit.
    Pfami PF12796. Ank_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01768. TRPVRECEPTOR.
    SMARTi SM00248. ANK. 4 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    TIGRFAMsi TIGR00870. trp. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT VAL-585.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANTS SER-91 AND ILE-469.
      Tissue: Spinal ganglion.
    3. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-469.
      Tissue: Testis.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    9. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TRPV3.
    10. "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] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. Cited for: MUTAGENESIS OF TYR-511 AND THR-550.

    Entry informationi

    Entry nameiTRPV1_HUMAN
    AccessioniPrimary (citable) accession number: Q8NER1
    Secondary accession number(s): A2RUA9
    , Q9H0G9, Q9H303, Q9H304, Q9NQ74, Q9NY22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Responses evoked by low pH and heat, and capsaicin can be antagonized by capsazepine.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3