Trpv1
entrez
193034
canonical
uniprot
Q704Y3
canonical
ensembl
ENSMUSG00000005952
resolver
ensp
ENSMUSP00000099585
resolver
genesymbol
Trpv1
resolver
uniprot
Q3V318
resolver
uniprot
Q5SSE1
resolver
uniprot
Q5SSE2
resolver
uniprot
Q5SSE4
resolver
uniprot
Q5WPV5
resolver
uniprot
Q68SW0
resolver
uniprot_entry
Q3V318_MOUSE
resolver
uniprot_entry
TRPV1_MOUSE
resolver
uniprot_sec
Q5SSE1
resolver
uniprot_sec
Q5SSE2
resolver
uniprot_sec
Q5SSE4
resolver
uniprot_sec
Q5WPV5
resolver
uniprot_sec
Q68SW0
resolver
activity_regulation
ACTIVITY REGULATION: 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. 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) (PubMed:26420335). 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). {ECO:0000250|UniProtKB:O35433, ECO:0000269|PubMed:26420335}.
uniprot
proteins
amino_acid_sequence
MEKWASLDSDESEPPAQENSCPDPPDRDPNSKPPPAKPHIFATRSRTRLFGKGDSEEASPMDCPYEEGGLASCPIITVSSVVTLQRSVDGPTCLRQTSQDSVSTGVETPPRLYDRRSIFDAVAQSNCQELESLLSFLQKSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDIARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTADNTKFVTNMYNEILILGAKLHPTLKLEELTNKKGLTPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTTAAYYRPVEGLPPYKLNNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSHRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSLPVESPPHKCRGSACRPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDFRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRDRHSTQPEEVQLKHYTGSLKPEDAEVFKDSMAPGEK
uniprot
proteins
function
FUNCTION: Non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli (PubMed:15194687, PubMed:15489017). Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia (PubMed:10764638). 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 (By similarity). {ECO:0000250|UniProtKB:O35433, ECO:0000269|PubMed:10764638, ECO:0000269|PubMed:15194687, ECO:0000269|PubMed:15489017}.
uniprot
proteins
mass_dalton
94976
uniprot
proteins
mutagenesis
MUTAGEN 461; /note="L->G: 17-fold less potently activated by the Scolopendra mutilans RhTx toxin."; /evidence="ECO:0000269|PubMed:26420335"; MUTAGEN 602; /note="D->A: 13-fold less potently activated by the Scolopendra mutilans RhTx toxin."; /evidence="ECO:0000269|PubMed:26420335"; MUTAGEN 632; /note="Y->A: 10-fold less potently activated by the Scolopendra mutilans RhTx toxin."; /evidence="ECO:0000269|PubMed:26420335"; MUTAGEN 634; /note="T->A: 8-fold less potently activated by the Scolopendra mutilans RhTx toxin."; /evidence="ECO:0000269|PubMed:26420335
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
10764638
uniprot
proteins
pubmed
15194687
uniprot
proteins
pubmed
15489017
uniprot
proteins
pubmed
18455988
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
25640077
uniprot
proteins
pubmed
26420335
uniprot
proteins
sequence_length
839
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. Cell membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O35433}. 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:0000250|UniProtKB:Q8NER1"; TRANSMEM 473..497; /note="Helical; Name=S2"; /evidence="ECO:0000250|UniProtKB:Q8NER1"; TRANSMEM 511..532; /note="Helical; Name=S3"; /evidence="ECO:0000250|UniProtKB:Q8NER1"; TRANSMEM 536..556; /note="Helical; Name=S4"; /evidence="ECO:0000250|UniProtKB:Q8NER1"; TRANSMEM 560..598; /note="Helical; Name=S5"; /evidence="ECO:0000250|UniProtKB:Q8NER1"; TRANSMEM 657..683; /note="Helical; Name=S6"; /evidence="ECO:0000250|UniProtKB:Q8NER1
uniprot
proteins