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Protein

Transient receptor potential cation channel subfamily V member 1

Gene

Trpv1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 similarity2 Publications

Enzyme regulationi

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. The double-knot toxin (DkTx) from the Chinese earth tiger tarantula activates the channel and traps it in an open conformation (By similarity). 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. Intracellular PIP2 inhibits desensitization (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • behavioral response to pain Source: MGI
  • calcium ion transport Source: MGI
  • cation transport Source: MGI
  • cellular response to alkaloid Source: UniProtKB
  • cellular response to ATP Source: UniProtKB
  • cellular response to nerve growth factor stimulus Source: Ensembl
  • cellular response to temperature stimulus Source: Ensembl
  • cellular response to tumor necrosis factor Source: Ensembl
  • detection of chemical stimulus involved in sensory perception of pain Source: MGI
  • detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
  • detection of temperature stimulus involved in thermoception Source: MGI
  • diet induced thermogenesis Source: MGI
  • fever generation Source: MGI
  • glutamate secretion Source: Ensembl
  • ion transmembrane transport Source: UniProtKB
  • lipid metabolic process Source: MGI
  • microglial cell activation Source: Ensembl
  • negative regulation of establishment of blood-brain barrier Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • peptide secretion Source: MGI
  • positive regulation of apoptotic process Source: Ensembl
  • positive regulation of gastric acid secretion Source: Ensembl
  • positive regulation of nitric oxide biosynthetic process Source: Ensembl
  • release of sequestered calcium ion into cytosol Source: GOC
  • response to heat Source: MGI
  • response to organonitrogen compound Source: MGI
  • response to pain Source: MGI
  • response to peptide hormone Source: Ensembl
  • response to pH Source: MGI
  • sensory perception of mechanical stimulus Source: MGI
  • sensory perception of pain Source: MGI
  • smooth muscle contraction involved in micturition Source: MGI
  • temperature homeostasis Source: MGI
  • urinary bladder smooth muscle contraction Source: MGI
Complete GO annotation...

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

ReactomeiR-MMU-3295583. TRP channels.

Names & Taxonomyi

Protein namesi
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
Gene namesi
Name:Trpv1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1341787. Trpv1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 433433CytoplasmicBy similarityAdd
BLAST
Transmembranei434 – 45421HelicalBy similarityAdd
BLAST
Topological domaini455 – 47218ExtracellularBy similarityAdd
BLAST
Transmembranei473 – 49826HelicalBy similarityAdd
BLAST
Topological domaini499 – 51113CytoplasmicBy similarityAdd
BLAST
Transmembranei512 – 53221HelicalBy similarityAdd
BLAST
Topological domaini533 – 5364ExtracellularBy similarity
Transmembranei537 – 55721HelicalBy similarityAdd
BLAST
Topological domaini558 – 57215CytoplasmicBy similarityAdd
BLAST
Transmembranei573 – 60028HelicalBy similarityAdd
BLAST
Topological domaini601 – 62727ExtracellularBy similarityAdd
BLAST
Intramembranei628 – 65023Pore-formingBy similarityAdd
BLAST
Transmembranei659 – 68729HelicalBy similarityAdd
BLAST
Topological domaini688 – 839152CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1781864.
GuidetoPHARMACOLOGYi507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 839839Transient receptor potential cation channel subfamily V member 1PRO_0000215339Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei145 – 1451PhosphothreonineBy similarity
Modified residuei371 – 3711PhosphothreonineBy similarity
Modified residuei503 – 5031Phosphoserine; by PKC/PRKCEBy similarity
Glycosylationi605 – 6051N-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

PaxDbiQ704Y3.
PRIDEiQ704Y3.

PTM databases

iPTMnetiQ704Y3.
PhosphoSiteiQ704Y3.

Expressioni

Gene expression databases

BgeeiQ704Y3.
ExpressionAtlasiQ704Y3. baseline and differential.
GenevisibleiQ704Y3. MM.

Interactioni

Subunit structurei

Homotetramer. May also form a heteromeric channel with TRPV3 (By similarity). Interacts with CALM, PRKCM and CSK (By similarity). Interacts with PRKCG and NTRK1, probably by forming a trimeric complex (By similarity). Interacts with PIRT (PubMed:18455988). Interacts with TMEM100 (PubMed:25640077).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi228724. 4 interactions.
DIPiDIP-59791N.
STRINGi10090.ENSMUSP00000099585.

Chemistry

BindingDBiQ704Y3.

Structurei

3D structure databases

ProteinModelPortaliQ704Y3.
SMRiQ704Y3. Positions 112-720.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ704Y3.
KOiK05222.
OMAiCHRKEYV.
OrthoDBiEOG7WHH8R.
PhylomeDBiQ704Y3.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024863. TRPV1_channel.
[Graphical view]
PANTHERiPTHR10582:SF17. PTHR10582:SF17. 2 hits.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q704Y3-1) [UniParc]FASTAAdd to basket

Also known as: Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEKWASLDSD ESEPPAQENS CPDPPDRDPN SKPPPAKPHI FATRSRTRLF
60 70 80 90 100
GKGDSEEASP MDCPYEEGGL ASCPIITVSS VVTLQRSVDG PTCLRQTSQD
110 120 130 140 150
SVSTGVETPP RLYDRRSIFD AVAQSNCQEL ESLLSFLQKS KKRLTDSEFK
160 170 180 190 200
DPETGKTCLL KAMLNLHNGQ NDTIALLLDI ARKTDSLKQF VNASYTDSYY
210 220 230 240 250
KGQTALHIAI ERRNMALVTL LVENGADVQA AANGDFFKKT KGRPGFYFGE
260 270 280 290 300
LPLSLAACTN QLAIVKFLLQ NSWQPADISA RDSVGNTVLH ALVEVADNTA
310 320 330 340 350
DNTKFVTNMY NEILILGAKL HPTLKLEELT NKKGLTPLAL AASSGKIGVL
360 370 380 390 400
AYILQREIHE PECRHLSRKF TEWAYGPVHS SLYDLSCIDT CEKNSVLEVI
410 420 430 440 450
AYSSSETPNR HDMLLVEPLN RLLQDKWDRF VKRIFYFNFF VYCLYMIIFT
460 470 480 490 500
TAAYYRPVEG LPPYKLNNTV GDYFRVTGEI LSVSGGVYFF FRGIQYFLQR
510 520 530 540 550
RPSLKSLFVD SYSEILFFVQ SLFMLVSVVL YFSHRKEYVA SMVFSLAMGW
560 570 580 590 600
TNMLYYTRGF QQMGIYAVMI EKMILRDLCR FMFVYLVFLF GFSTAVVTLI
610 620 630 640 650
EDGKNNSLPV ESPPHKCRGS ACRPGNSYNS LYSTCLELFK FTIGMGDLEF
660 670 680 690 700
TENYDFKAVF IILLLAYVIL TYILLLNMLI ALMGETVNKI AQESKNIWKL
710 720 730 740 750
QRAITILDTE KSFLKCMRKA FRSGKLLQVG FTPDGKDDFR WCFRVDEVNW
760 770 780 790 800
TTWNTNVGII NEDPGNCEGV KRTLSFSLRS GRVSGRNWKN FALVPLLRDA
810 820 830
STRDRHSTQP EEVQLKHYTG SLKPEDAEVF KDSMAPGEK
Length:839
Mass (Da):94,976
Last modified:July 5, 2004 - v1
Checksum:iEB50780E9281C2B7
GO
Isoform 2 (identifier: Q704Y3-2) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     399-408: Missing.

Show »
Length:829
Mass (Da):93,941
Checksum:i4925B877D299D29E
GO

Sequence cautioni

The sequence CAI24577.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI24579.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI24580.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti734 – 7341D → E in AAS01605 (PubMed:15489017).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei399 – 40810Missing in isoform 2. 1 PublicationVSP_013430

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY452083 mRNA. Translation: AAS15574.1.
AY452084 mRNA. Translation: AAS15575.1.
AJ620495 mRNA. Translation: CAF05661.1.
AB180097 mRNA. Translation: BAD20301.1.
AY445519 mRNA. Translation: AAS01605.1.
AL663116 Genomic DNA. Translation: CAI24577.1. Sequence problems.
AL663116 Genomic DNA. Translation: CAI24578.1.
AL663116 Genomic DNA. Translation: CAI24579.1. Sequence problems.
AL663116 Genomic DNA. Translation: CAI24580.1. Sequence problems.
CCDSiCCDS25003.1. [Q704Y3-1]
RefSeqiNP_001001445.1. NM_001001445.2. [Q704Y3-1]
UniGeneiMm.447485.

Genome annotation databases

EnsembliENSMUST00000102526; ENSMUSP00000099585; ENSMUSG00000005952. [Q704Y3-1]
GeneIDi193034.
KEGGimmu:193034.
UCSCiuc007kah.2. mouse. [Q704Y3-1]
uc011xyq.2. mouse. [Q704Y3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY452083 mRNA. Translation: AAS15574.1.
AY452084 mRNA. Translation: AAS15575.1.
AJ620495 mRNA. Translation: CAF05661.1.
AB180097 mRNA. Translation: BAD20301.1.
AY445519 mRNA. Translation: AAS01605.1.
AL663116 Genomic DNA. Translation: CAI24577.1. Sequence problems.
AL663116 Genomic DNA. Translation: CAI24578.1.
AL663116 Genomic DNA. Translation: CAI24579.1. Sequence problems.
AL663116 Genomic DNA. Translation: CAI24580.1. Sequence problems.
CCDSiCCDS25003.1. [Q704Y3-1]
RefSeqiNP_001001445.1. NM_001001445.2. [Q704Y3-1]
UniGeneiMm.447485.

3D structure databases

ProteinModelPortaliQ704Y3.
SMRiQ704Y3. Positions 112-720.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228724. 4 interactions.
DIPiDIP-59791N.
STRINGi10090.ENSMUSP00000099585.

Chemistry

BindingDBiQ704Y3.
ChEMBLiCHEMBL1781864.
GuidetoPHARMACOLOGYi507.

PTM databases

iPTMnetiQ704Y3.
PhosphoSiteiQ704Y3.

Proteomic databases

PaxDbiQ704Y3.
PRIDEiQ704Y3.

Protocols and materials databases

DNASUi193034.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102526; ENSMUSP00000099585; ENSMUSG00000005952. [Q704Y3-1]
GeneIDi193034.
KEGGimmu:193034.
UCSCiuc007kah.2. mouse. [Q704Y3-1]
uc011xyq.2. mouse. [Q704Y3-2]

Organism-specific databases

CTDi7442.
MGIiMGI:1341787. Trpv1.

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ704Y3.
KOiK05222.
OMAiCHRKEYV.
OrthoDBiEOG7WHH8R.
PhylomeDBiQ704Y3.
TreeFamiTF314711.

Enzyme and pathway databases

ReactomeiR-MMU-3295583. TRP channels.

Miscellaneous databases

NextBioi371416.
PROiQ704Y3.
SOURCEiSearch...

Gene expression databases

BgeeiQ704Y3.
ExpressionAtlasiQ704Y3. baseline and differential.
GenevisibleiQ704Y3. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024863. TRPV1_channel.
[Graphical view]
PANTHERiPTHR10582:SF17. PTHR10582:SF17. 2 hits.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "2-aminoethoxydiphenyl borate is a common activator of TRPV1, TRPV2, and TRPV3."
    Hu H.Z., Gu Q., Wang C., Colton C.K., Tang J., Kinoshita-Kawada M., Lee L.Y., Wood J.D., Zhu M.X.
    J. Biol. Chem. 279:35741-35748(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
    Strain: C57BL/6J.
  2. McIntyre P.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Spinal ganglion.
  3. Ogawa S., Sugiura A., Pang C., Shinjo K.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: DBA.
  4. "Cloning and pharmacological characterization of mouse TRPV1."
    Correll C.C., Phelps P.T., Greenfeder S.
    Neurosci. Lett. 370:55-60(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    Strain: Swiss Webster.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1."
    Kim A.Y., Tang Z., Liu Q., Patel K.N., Maag D., Geng Y., Dong X.
    Cell 133:475-485(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH PIRT.
  7. "Tmem100 Is a regulator of TRPA1-TRPV1 complex and contributes to persistent pain."
    Weng H.J., Patel K.N., Jeske N.A., Bierbower S.M., Zou W., Tiwari V., Zheng Q., Tang Z., Mo G.C., Wang Y., Geng Y., Zhang J., Guan Y., Akopian A.N., Dong X.
    Neuron 85:833-846(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM100.

Entry informationi

Entry nameiTRPV1_MOUSE
AccessioniPrimary (citable) accession number: Q704Y3
Secondary accession number(s): Q5SSE1
, Q5SSE2, Q5SSE4, Q5WPV5, Q68SW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.