Trpv1
entrez
83810
canonical
uniprot
O35433
canonical
ensembl
ENSRNOG00000019486
resolver
ensp
ENSRNOP00000026493
resolver
genesymbol
Trpv1
resolver
genesymbol_syn
Vr1
resolver
genesymbol_syn
Vr1l
resolver
uniprot
Q920B3
resolver
uniprot
Q920B4
resolver
uniprot
Q9JLM0
resolver
uniprot
Q9JM56
resolver
uniprot
Q9JM57
resolver
uniprot_entry
TRPV1_RAT
resolver
uniprot_sec
Q920B3
resolver
uniprot_sec
Q920B4
resolver
uniprot_sec
Q9JLM0
resolver
uniprot_sec
Q9JM56
resolver
uniprot_sec
Q9JM57
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. 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:Q704Y3, ECO:0000269|PubMed:17582331, ECO:0000269|PubMed:20510930, ECO:0000269|PubMed:23109716}.
uniprot
proteins
amino_acid_sequence
MEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSEEASPLDCPYEEGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSLPMESTPHKCRGSACKPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRDRHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPGEK
uniprot
proteins
function
FUNCTION: 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. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius (By similarity). 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:Q8NER1, ECO:0000269|PubMed:11140687, ECO:0000269|PubMed:11418861, ECO:0000269|PubMed:11578842, ECO:0000269|PubMed:12095983, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:12764195, ECO:0000269|PubMed:12808128, ECO:0000269|PubMed:14523239, ECO:0000269|PubMed:14630912, ECO:0000269|PubMed:15173182, ECO:0000269|PubMed:17582331, ECO:0000269|PubMed:20510930, ECO:0000269|PubMed:21076423, ECO:0000269|PubMed:23109716, ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:9349813}.; FUNCTION: [Isoform 3]: Does not display channel activity in response to noxious chemical compounds, such as capsaicin and the vanilloid resiniferatoxin. Channel activity is not elicited by mildly acidic extracellular pH, and only slight channel activity is observed in response to noxiuos heat stimuli. {ECO:0000269|PubMed:10644739}.
uniprot
proteins
mass_dalton
94948
uniprot
proteins
mutagenesis
MUTAGEN 114; /note="R->E: Abolishes capsaicin-evoked current and binding to resiniferatoxin."; /evidence="ECO:0000269|PubMed:12228246"; MUTAGEN 114; /note="Missing: Abolishes sensitivity to acid."; /evidence="ECO:0000269|PubMed:12228246"; MUTAGEN 115; /note="R->D: Abolishes capsaicin-evoked current and binding to resiniferatoxin."; /evidence="ECO:0000269|PubMed:12228246"; MUTAGEN 116; /note="S->A: Abolishes phosphorylation by PKCM and enhances channel response to capsaicin by PKCM."; /evidence="ECO:0000269|PubMed:15471852"; MUTAGEN 155; /note="K->A: Abolishes ATP binding. Abolishes CALM binding. Impairs normal desensitization by repeated exposure to capsaicin."; /evidence="ECO:0000269|PubMed:17582331, ECO:0000269|PubMed:23109716"; MUTAGEN 160; /note="K->A: Abolishes ATP binding. Abolishes CALM binding."; /evidence="ECO:0000269|PubMed:17582331"; MUTAGEN 199; /note="Y->A: Strongly reduces affinity for ATP; when associated with A-202."; /evidence="ECO:0000269|PubMed:17582331"; MUTAGEN 202; /note="Q->A: Strongly reduces affinity for ATP; when associated with A-199."; /evidence="ECO:0000269|PubMed:17582331"; MUTAGEN 502; /note="S->A: Largely reduces PMA enhancement of capsaicin-evoked currents, but no effect on direct activation by PMA. Loss of activation by capsaicin and loss of vanilloid binding; when associated with I-704."; /evidence="ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:14523239, ECO:0000269|PubMed:14630912"; MUTAGEN 511; /note="Y->A: Loss of sensitivity to capsaicin."; /evidence="ECO:0000269|PubMed:14996838"; MUTAGEN 547; /note="M->L: Reduces binding to resiniferatoxin."; /evidence="ECO:0000269|PubMed:14996838"; MUTAGEN 550; /note="T->I: Reduces sensitivity to capsaicin 10-fold; no effect on sensitivity to resiniferatoxin. Reduces binding to resiniferatoxin."; /evidence="ECO:0000269|PubMed:14996838"; MUTAGEN 636; /note="E->K: Abolishes channel activity. Restored channel activity; when associated with E-639."; /evidence="ECO:0000269|PubMed:10931826"; MUTAGEN 636; /note="E->Q: Slight modification of pore attributes."; /evidence="ECO:0000269|PubMed:10931826"; MUTAGEN 639; /note="K->E: Restored channel activity; when associated with K-636."; /evidence="ECO:0000269|PubMed:10931826"; MUTAGEN 644; /note="M->Y: Slightly modifies channel permeability."; /evidence="ECO:0000269|PubMed:10931826"; MUTAGEN 646; /note="D->N: Strongly reduces the affinity for pore blocker ruthenium red and lowered channel permeability for Mg(2+)."; /evidence="ECO:0000269|PubMed:10931826"; MUTAGEN 648; /note="E->Q: Minor modification of pore attributes."; /evidence="ECO:0000269|PubMed:10931826"; MUTAGEN 651; /note="E->Q: Minor modification of pore attributes."; /evidence="ECO:0000269|PubMed:10931826"; MUTAGEN 704; /note="T->A: No effect on PMA-induced enhancement of capsaicin-evoked currents but reduces direct activation by PMA."; /evidence="ECO:0000269|PubMed:14523239, ECO:0000269|PubMed:14630912"; MUTAGEN 704; /note="T->I: Loss of activation by capsaicin and loss of vanilloid binding; when associated with A-502."; /evidence="ECO:0000269|PubMed:14523239, ECO:0000269|PubMed:14630912"; MUTAGEN 761; /note="E->K,Q: Abolishes capsaicin-evoked current and binding to resiniferatoxin."; /evidence="ECO:0000269|PubMed:12228246"; MUTAGEN 761; /note="Missing: Abolishes sensitivity to acid."; /evidence="ECO:0000269|PubMed:12228246"; MUTAGEN 785; /note="R->Q: Strongly reduces CALM-binding and abolishes PLC-mediated channel activity; when associated with Q-788."; /evidence="ECO:0000269|PubMed:12764195, ECO:0000269|PubMed:23109716"; MUTAGEN 787; /note="W->R: Reduces CALM-binding. Reduces desensitization by repeated exposure to capsaicin."; /evidence="ECO:0000269|PubMed:23109716"; MUTAGEN 788; /note="K->Q: Strongly reduces CALM-binding and abolishes PLC-mediated channel activity; when associated with Q-785 or Q-797."; /evidence="ECO:0000269|PubMed:12764195, ECO:0000269|PubMed:23109716"; MUTAGEN 797; /note="R->Q: Abolishes PLC-mediated channel activity; when associated with Q-788."; /evidence="ECO:0000269|PubMed:12764195"; MUTAGEN 800; /note="S->A: Largely reduces direct activation of by PMA and PMA-induced currents; no effect on receptor kinase-induced currents."; /evidence="ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12764195, ECO:0000269|PubMed:14523239
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-116 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:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912, ECO:0000269|PubMed:15471852}.
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
10644739
uniprot
proteins
pubmed
10931826
uniprot
proteins
pubmed
11140687
uniprot
proteins
pubmed
11418861
uniprot
proteins
pubmed
11549313
uniprot
proteins
pubmed
11578842
uniprot
proteins
pubmed
11683872
uniprot
proteins
pubmed
11884385
uniprot
proteins
pubmed
12095983
uniprot
proteins
pubmed
12194871
uniprot
proteins
pubmed
12228246
uniprot
proteins
pubmed
12764195
uniprot
proteins
pubmed
12808128
uniprot
proteins
pubmed
14523239
uniprot
proteins
pubmed
14630912
uniprot
proteins
pubmed
14996838
uniprot
proteins
pubmed
15084474
uniprot
proteins
pubmed
15173182
uniprot
proteins
pubmed
15190102
uniprot
proteins
pubmed
15471852
uniprot
proteins
pubmed
15857679
uniprot
proteins
pubmed
17582331
uniprot
proteins
pubmed
20510930
uniprot
proteins
pubmed
21076423
uniprot
proteins
pubmed
23109716
uniprot
proteins
pubmed
24305160
uniprot
proteins
pubmed
24305161
uniprot
proteins
pubmed
27281200
uniprot
proteins
pubmed
9349813
uniprot
proteins
sequence_length
838
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:15857679}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NER1}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:15857679}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NER1}. Cell membrane {ECO:0000269|PubMed:11578842, ECO:0000269|PubMed:15857679, ECO:0000269|PubMed:9349813}; Multi-pass membrane protein {ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:24305161, ECO:0000269|PubMed:27281200}. Note=Mostly, but not exclusively expressed in postsynaptic dendritic spines. {ECO:0000269|PubMed:15857679}.
uniprot
proteins
transmembrane_region
TRANSMEM 433..453; /note="Helical; Name=S1"; /evidence="ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0"; TRANSMEM 472..497; /note="Helical; Name=S2"; /evidence="ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0"; TRANSMEM 511..531; /note="Helical; Name=S3"; /evidence="ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0"; TRANSMEM 536..556; /note="Helical; Name=S4"; /evidence="ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0"; TRANSMEM 572..599; /note="Helical; Name=S5"; /evidence="ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0"; TRANSMEM 658..686; /note="Helical; Name=S6"; /evidence="ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0007744|PDB:3J5P, ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0
uniprot
proteins