TRPV1
entrez
7442
canonical
uniprot
Q8NER1
canonical
ensembl
ENSG00000196689
resolver
ensp
ENSP00000382659
resolver
ensp
ENSP00000382661
resolver
ensp
ENSP00000459962
resolver
ensp
ENSP00000461007
resolver
genesymbol
TRPV1
resolver
genesymbol_syn
VR1
resolver
hgnc
HGNC:12716
resolver
uniprot
A2RUA9
resolver
uniprot
Q3LU47
resolver
uniprot
Q9H0G9
resolver
uniprot
Q9H303
resolver
uniprot
Q9H304
resolver
uniprot
Q9NQ74
resolver
uniprot
Q9NY22
resolver
uniprot_entry
TRPV1_HUMAN
resolver
uniprot_sec
A2RUA9
resolver
uniprot_sec
Q3LU47
resolver
uniprot_sec
Q9H0G9
resolver
uniprot_sec
Q9H303
resolver
uniprot_sec
Q9H304
resolver
uniprot_sec
Q9NQ74
resolver
uniprot_sec
Q9NY22
resolver
activity_regulation
ACTIVITY 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). 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. Ca(2+) 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). The Scolopendra mutilans RhTx toxin potentiates the heat activation pathway mediated by this channel by binding to the charge-rich outer pore region (in an activated state) (By similarity). {ECO:0000250|UniProtKB:O35433, ECO:0000250|UniProtKB:Q704Y3}.
uniprot
proteins
amino_acid_sequence
MKKWSSTDLGAAADPLQKDTCPDPLDGDPNSRPPPAKPQLSTAKSRTRLFGKGDSEEAFPVDCPHEEGELDSCPTITVSPVITIQRPGDGPTGARLLSQDSVAASTEKTLRLYDRRSIFEAVAQNNCQDLESLLLFLQKSKKHLTDNEFKDPETGKTCLLKAMLNLHDGQNTTIPLLLEIARQTDSLKELVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAAHGDFFKKTKGRPGFYFGELPLSLAACTNQLGIVKFLLQNSWQTADISARDSVGNTVLHALVEVADNTADNTKFVTSMYNEILMLGAKLHPTLKLEELTNKKGMTPLALAAGTGKIGVLAYILQREIQEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFLVYCLYMIIFTMAAYYRPVDGLPPFKMEKTGDYFRVTGEILSVLGGVYFFFRGIQYFLQRRPSMKTLFVDSYSEMLFFLQSLFMLATVVLYFSHLKEYVASMVFSLALGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYIVFLFGFSTAVVTLIEDGKNDSLPSESTSHRWRGPACRPPDSSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGYTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSSRVSGRHWKNFALVPLLREASARDRQSAQPEEVYLRQFSGSLKPEDAEVFKSPAASGEK
uniprot
proteins
function
FUNCTION: Non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli (PubMed:11050376, PubMed:11243859, PubMed:11226139, PubMed:12077606). 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. Activated by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius (PubMed:37117175). Upon activation, exhibits a time- and Ca(2+)-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. 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. {ECO:0000250|UniProtKB:O35433, ECO:0000269|PubMed:11050376, ECO:0000269|PubMed:11226139, ECO:0000269|PubMed:11243859, ECO:0000269|PubMed:12077606, ECO:0000269|PubMed:37117175}.
uniprot
proteins
mass_dalton
94956
uniprot
proteins
mutagenesis
MUTAGEN 511; /note="Y->A: Loss of sensitivity to capsaicin. Impairs response to inhibitor SB-366791."; /evidence="ECO:0000269|PubMed:14996838, ECO:0000269|PubMed:37117175"; MUTAGEN 515; /note="L->A: Abolishes response to inhibitor SB-366791."; /evidence="ECO:0000269|PubMed:37117175"; MUTAGEN 547; /note="L->R: Abolishes response to inhibitor SB-366791."; /evidence="ECO:0000269|PubMed:37117175"; MUTAGEN 550; /note="T->A: Abolishes response to inhibitor SB-366791."; /evidence="ECO:0000269|PubMed:37117175"; MUTAGEN 550; /note="T->I: Reduces sensitivity to capsaicin 40-fold."; /evidence="ECO:0000269|PubMed:14996838"; MUTAGEN 693; /note="E->A: Abolishes response to inhibitor SB-366791."; /evidence="ECO:0000269|PubMed:37117175
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-117 as a major phosphorylation site. Phosphorylation 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. {ECO:0000250|UniProtKB:O35433}.
uniprot
proteins
protein_family
TRPV1 sub-subfamily
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
protein_family
TrpV subfamily
uniprot
proteins
pubmed
11050376
uniprot
proteins
pubmed
11226139
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11243859
uniprot
proteins
pubmed
12077606
uniprot
proteins
pubmed
14987252
uniprot
proteins
pubmed
14996838
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
29656858
uniprot
proteins
pubmed
37117175
uniprot
proteins
sequence_length
839
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000269|PubMed:37117175}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000269|PubMed:37117175}. Cell membrane {ECO:0000269|PubMed:11050376, ECO:0000269|PubMed:11243859, ECO:0000269|PubMed:12077606, ECO:0000269|PubMed:37117175}; Multi-pass membrane protein {ECO:0000269|PubMed:37117175}. Note=Mostly, but not exclusively expressed in postsynaptic dendritic spines. {ECO:0000250|UniProtKB:O35433}.
uniprot
proteins
transmembrane_region
TRANSMEM 434..455; /note="Helical; Name=S1"; /evidence="ECO:0000269|PubMed:37117175, ECO:0007744|PDB:8GF8, ECO:0007744|PDB:8GF9, ECO:0007744|PDB:8GFA"; TRANSMEM 473..497; /note="Helical; Name=S2"; /evidence="ECO:0000269|PubMed:37117175, ECO:0007744|PDB:8GF8, ECO:0007744|PDB:8GF9, ECO:0007744|PDB:8GFA"; TRANSMEM 511..532; /note="Helical; Name=S3"; /evidence="ECO:0000269|PubMed:37117175, ECO:0007744|PDB:8GF8, ECO:0007744|PDB:8GF9, ECO:0007744|PDB:8GFA"; TRANSMEM 536..556; /note="Helical; Name=S4"; /evidence="ECO:0000269|PubMed:37117175, ECO:0007744|PDB:8GF8, ECO:0007744|PDB:8GF9, ECO:0007744|PDB:8GFA"; TRANSMEM 560..598; /note="Helical; Name=S5"; /evidence="ECO:0000269|PubMed:37117175, ECO:0007744|PDB:8GF8, ECO:0007744|PDB:8GF9, ECO:0007744|PDB:8GFA"; TRANSMEM 657..683; /note="Helical; Name=S6"; /evidence="ECO:0000269|PubMed:37117175, ECO:0007744|PDB:8GF8, ECO:0007744|PDB:8GF9, ECO:0007744|PDB:8GFA
uniprot
proteins