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Transient receptor potential cation channel subfamily V member 1 (TrpV1) (Capsaicin receptor) (Osm-9-like TRP channel 1) (OTRPC1) (Vanilloid receptor 1) (Vanilloid receptor type 1-like)

 TRPV1_RAT               Reviewed;         838 AA.
O35433; Q920B3; Q920B4; Q9JLM0; Q9JM56; Q9JM57;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 155.
RecName: Full=Transient receptor potential cation channel subfamily V member 1;
Short=TrpV1;
AltName: Full=Capsaicin receptor;
AltName: Full=Osm-9-like TRP channel 1;
Short=OTRPC1;
AltName: Full=Vanilloid receptor 1;
AltName: Full=Vanilloid receptor type 1-like;
Name=Trpv1; Synonyms=Vr1, Vr1l;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Spinal ganglion;
PubMed=9349813; DOI=10.1038/39807;
Caterina M.J., Schumacher M.A., Tominaga M., Rosen T.A., Levine J.D.,
Julius D.;
"The capsaicin receptor: a heat-activated ion channel in the pain
pathway.";
Nature 389:816-824(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
FUNCTION (ISOFORM 3).
STRAIN=Sprague-Dawley;
TISSUE=Spinal ganglion, and Trigeminal ganglion;
PubMed=10644739; DOI=10.1074/jbc.275.4.2756;
Schumacher M.A., Moff I., Sudanagunta S.P., Levine J.D.;
"Molecular cloning of an N-terminal splice variant of the capsaicin
receptor. Loss of N-terminal domain suggests functional divergence
among capsaicin receptor subtypes.";
J. Biol. Chem. 275:2756-2762(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=11578842; DOI=10.1016/S0304-3940(01)02185-1;
Tsutsumi S., Tomioka A., Sudo M., Nakamura A., Shirakura K.,
Takagishi K., Kohama K.;
"Propofol activates vanilloid receptor channels expressed in human
embryonic kidney 293 cells.";
Neurosci. Lett. 312:45-49(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-468, AND ALTERNATIVE SPLICING.
STRAIN=Sprague-Dawley;
PubMed=11549313; DOI=10.1006/geno.2001.6582;
Xue Q., Yu Y., Trilk S.L., Jong B.E., Schumacher M.A.;
"The genomic organization of the gene encoding the vanilloid receptor:
evidence for multiple splice variants.";
Genomics 76:14-20(2001).
[5]
CHARACTERIZATION OF CHANNEL PORE, AND MUTAGENESIS OF GLU-636; LYS-639;
MET-644; ASP-646; GLU-648 AND GLU-651.
PubMed=10931826; DOI=10.1074/jbc.M002391200;
Garcia-Martinez C., Morenilla-Palao C., Planells-Cases R.,
Merino J.M., Ferrer-Montiel A.V.;
"Identification of an aspartic residue in the P-loop of the vanilloid
receptor that modulates pore properties.";
J. Biol. Chem. 275:32552-32558(2000).
[6]
FUNCTION.
PubMed=11140687; DOI=10.1038/35050121;
Premkumar L.S., Ahern G.P.;
"Induction of vanilloid receptor channel activity by protein kinase
C.";
Nature 408:985-990(2000).
[7]
SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-604.
PubMed=11683872; DOI=10.1046/j.1432-1033.2001.02500.x;
Jahnel R., Dreger M., Gillen C., Bender O., Kurreck J., Hucho F.;
"Biochemical characterization of the vanilloid receptor 1 expressed in
a dorsal root ganglia derived cell line.";
Eur. J. Biochem. 268:5489-5496(2001).
[8]
FUNCTION, AND INTERACTION WITH PRKCG AND NTRK1.
PubMed=11418861; DOI=10.1038/35082088;
Chuang H.H., Prescott E.D., Kong H., Shields S., Jordt S.E.,
Basbaum A.I., Chao M.V., Julius D.;
"Bradykinin and nerve growth factor release the capsaicin receptor
from PtdIns(4,5)P2-mediated inhibition.";
Nature 411:957-962(2001).
[9]
PHOSPHORYLATION AT SER-502 AND SER-800, AND MUTAGENESIS OF SER-502 AND
SER-800.
PubMed=11884385; DOI=10.1074/jbc.C200104200;
Numazaki M., Tominaga T., Toyooka H., Tominaga M.;
"Direct phosphorylation of capsaicin receptor VR1 by protein kinase
Cepsilon and identification of two target serine residues.";
J. Biol. Chem. 277:13375-13378(2002).
[10]
FUNCTION.
PubMed=12095983; DOI=10.1074/jbc.M201551200;
Olah Z., Karai L., Iadarola M.J.;
"Protein kinase C(alpha) is required for vanilloid receptor 1
activation. Evidence for multiple signaling pathways.";
J. Biol. Chem. 277:35752-35759(2002).
[11]
FUNCTION, AND PHOSPHORYLATION AT SER-116; THR-144; THR-370; SER-502;
SER-774 AND SER-820.
PubMed=12194871; DOI=10.1016/S0896-6273(02)00802-4;
Bhave G., Zhu W., Wang H., Brasier D.J., Oxford G.S., Gereau R.W. IV;
"cAMP-dependent protein kinase regulates desensitization of the
capsaicin receptor (VR1) by direct phosphorylation.";
Neuron 35:721-731(2002).
[12]
FUNCTION, AND INTERACTION WITH CALMODULIN.
PubMed=12808128; DOI=10.1073/pnas.1337252100;
Numazaki M., Tominaga T., Takeuchi K., Murayama N., Toyooka H.,
Tominaga M.;
"Structural determinant of TRPV1 desensitization interacts with
calmodulin.";
Proc. Natl. Acad. Sci. U.S.A. 100:8002-8006(2003).
[13]
FUNCTION, AND MUTAGENESIS OF SER-502; THR-704 AND SER-800.
PubMed=14523239; DOI=10.1073/pnas.2032100100;
Bhave G., Hu H.J., Glauner K.S., Zhu W., Wang H., Brasier D.J.,
Oxford G.S., Gereau R.W. IV;
"Protein kinase C phosphorylation sensitizes but does not activate the
capsaicin receptor transient receptor potential vanilloid 1 (TRPV1).";
Proc. Natl. Acad. Sci. U.S.A. 100:12480-12485(2003).
[14]
FUNCTION, AND MUTAGENESIS OF ARG-785; LYS-788; ARG-797 AND SER-800.
PubMed=12764195; DOI=10.1126/science.1083646;
Prescott E.D., Julius D.;
"A modular PIP2 binding site as a determinant of capsaicin receptor
sensitivity.";
Science 300:1284-1288(2003).
[15]
INTERACTION WITH CSK.
PubMed=15084474; DOI=10.1152/ajpcell.00113.2004;
Jin X., Morsy N., Winston J., Pasricha P.J., Garrett K.,
Akbarali H.I.;
"Modulation of TRPV1 by nonreceptor tyrosine kinase, c-Src kinase.";
Am. J. Physiol. 287:C558-C563(2004).
[16]
MUTAGENESIS OF ARG-114; ARG-115 AND GLU-761.
PubMed=12228246; DOI=10.1074/jbc.M207103200;
Jung J., Lee S.Y., Hwang S.W., Cho H., Shin J., Kang Y.S., Kim S.,
Oh U.;
"Agonist recognition sites in the cytosolic tails of vanilloid
receptor 1.";
J. Biol. Chem. 277:44448-44454(2002).
[17]
FUNCTION, PHOSPHORYLATION AT SER-502 AND THR-704, AND MUTAGENESIS OF
SER-502 AND THR-704.
PubMed=14630912; DOI=10.1074/jbc.M311448200;
Jung J., Shin J.S., Lee S.-Y., Hwang S.W., Koo J., Cho H., Oh U.;
"Phosphorylation of vanilloid receptor 1 by Ca2+/calmodulin-dependent
kinase II regulates its vanilloid binding.";
J. Biol. Chem. 279:7048-7054(2004).
[18]
MUTAGENESIS OF TYR-511; MET-547 AND THR-550.
PubMed=14996838; DOI=10.1074/jbc.M312577200;
Gavva N.R., Klionsky L., Qu Y., Shi L., Tamir R., Edenson S.,
Zhang T.J., Viswanadhan V.N., Toth A., Pearce L.V., Vanderah T.W.,
Porreca F., Blumberg P.M., Lile J., Sun Y., Wild K., Louis J.C.,
Treanor J.J.;
"Molecular determinants of vanilloid sensitivity in TRPV1.";
J. Biol. Chem. 279:20283-20295(2004).
[19]
FUNCTION.
PubMed=15173182; DOI=10.1074/jbc.M402966200;
Hellwig N., Plant T.D., Janson W., Schafer M., Schultz G.,
Schaefer M.;
"TRPV1 acts as proton channel to induce acidification in nociceptive
neurons.";
J. Biol. Chem. 279:34553-34561(2004).
[20]
INTERACTION WITH PRKCM, PHOSPHORYLATION AT SER-116, AND MUTAGENESIS OF
SER-116.
PubMed=15471852; DOI=10.1074/jbc.M410331200;
Wang Y., Kedei N., Wang M., Wang Q.J., Huppler A.R., Toth A., Tran R.,
Blumberg P.M.;
"Interaction between protein kinase Cmu and the vanilloid receptor
type 1.";
J. Biol. Chem. 279:53674-53682(2004).
[21]
SUBUNIT.
PubMed=15190102; DOI=10.1523/JNEUROSCI.0202-04.2004;
Garcia-Sanz N., Fernandez-Carvajal A., Morenilla-Palao C.,
Planells-Cases R., Fajardo-Sanchez E., Fernandez-Ballester G.,
Ferrer-Montiel A.;
"Identification of a tetramerization domain in the C-terminus of the
vanilloid receptor.";
J. Neurosci. 24:5307-5314(2004).
[22]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15857679; DOI=10.1016/j.molbrainres.2004.12.003;
Toth A., Boczan J., Kedei N., Lizanecz E., Bagi Z., Papp Z., Edes I.,
Csiba L., Blumberg P.M.;
"Expression and distribution of vanilloid receptor 1 (TRPV1) in the
adult rat brain.";
Brain Res. Mol. Brain Res. 135:162-168(2005).
[23]
FUNCTION, AND ENZYME REGULATION.
PubMed=20510930; DOI=10.1016/j.cell.2010.03.052;
Bohlen C.J., Priel A., Zhou S., King D., Siemens J., Julius D.;
"A bivalent tarantula toxin activates the capsaicin receptor, TRPV1,
by targeting the outer pore domain.";
Cell 141:834-845(2010).
[24]
FUNCTION.
PubMed=21076423; DOI=10.1038/nn.2684;
Chavez A.E., Chiu C.Q., Castillo P.E.;
"TRPV1 activation by endogenous anandamide triggers postsynaptic long-
term depression in dentate gyrus.";
Nat. Neurosci. 13:1511-1518(2010).
[25]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 101-364 IN COMPLEX WITH ATP,
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, ATP-BINDING,
CALMODULIN-BINDING, MUTAGENESIS OF LYS-155; LYS-160; TYR-199 AND
GLN-202, AND ANKYRIN REPEATS.
PubMed=17582331; DOI=10.1016/j.neuron.2007.05.027;
Lishko P.V., Procko E., Jin X., Phelps C.B., Gaudet R.;
"The ankyrin repeats of TRPV1 bind multiple ligands and modulate
channel sensitivity.";
Neuron 54:905-918(2007).
[26]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 767-801 IN COMPLEX WITH
CALM, FUNCTION, MUTAGENESIS OF LYS-155; ARG-785; TRP-787 AND LYS-788,
CALMODULIN-BINDING, INTERACTION WITH CALM, AND ENZYME REGULATION.
PubMed=23109716; DOI=10.1085/jgp.201210810;
Lau S.Y., Procko E., Gaudet R.;
"Distinct properties of Ca2+-calmodulin binding to N- and C-terminal
regulatory regions of the TRPV1 channel.";
J. Gen. Physiol. 140:541-555(2012).
[27]
STRUCTURE BY ELECTRON MICROSCOPY (3.27 ANGSTROMS), FUNCTION,
SUBCELLULAR LOCATION, TOPOLOGY, ANK REPEATS, AND SUBUNIT.
PubMed=24305160; DOI=10.1038/nature12822;
Liao M., Cao E., Julius D., Cheng Y.;
"Structure of the TRPV1 ion channel determined by electron cryo-
microscopy.";
Nature 504:107-112(2013).
[28]
STRUCTURE BY ELECTROM MICROSCOPY (3.8 ANGSTROMS) IN COMPLEXES WITH
CAPSAICIN AND TARANTULA DOUBLE-KNOT TOXIN, AND SUBUNIT.
PubMed=24305161; DOI=10.1038/nature12823;
Cao E., Liao M., Cheng Y., Julius D.;
"TRPV1 structures in distinct conformations reveal activation
mechanisms.";
Nature 504:113-118(2013).
[29]
STRUCTURE BY ELECTRON MICROSCOPY (2.95 ANGSTROMS) OF 110-764 OF
APOPROTEIN AND IN COMPLEX WITH AGONIST, SUBUNIT, TOPOLOGY, AND
LIPID-BINDING.
PubMed=27281200; DOI=10.1038/nature17964;
Gao Y., Cao E., Julius D., Cheng Y.;
"TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid
action.";
Nature 534:347-351(2016).
-!- FUNCTION: 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. Activation
by vanilloids, like capsaicin, and temperatures higher than 42
degrees Celsius, 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: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}.
-!- ENZYME 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. {ECO:0000250, ECO:0000269|PubMed:17582331,
ECO:0000269|PubMed:20510930, ECO:0000269|PubMed:23109716}.
-!- SUBUNIT: Interacts with PIRT (By similarity). Homotetramer
(PubMed:15190102, PubMed:24305160, PubMed:24305161,
PubMed:27281200). May also form a heteromeric channel with TRPV3
(By similarity). Interacts with CALM, PRKCM and CSK
(PubMed:12808128, PubMed:15084474, PubMed:15471852,
PubMed:17582331). Interacts with PRKCG and NTRK1, probably by
forming a trimeric complex (PubMed:11418861). Interacts with
TMEM100 (By similarity). {ECO:0000250|UniProtKB:Q704Y3,
ECO:0000250|UniProtKB:Q8NER1, ECO:0000269|PubMed:11418861,
ECO:0000269|PubMed:12808128, ECO:0000269|PubMed:15084474,
ECO:0000269|PubMed:15190102, ECO:0000269|PubMed:15471852,
ECO:0000269|PubMed:23109716, ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:24305161, ECO:0000269|PubMed:27281200}.
-!- INTERACTION:
Self; NbExp=11; IntAct=EBI-2794004, EBI-2794004;
P0CH43:- (xeno); NbExp=2; IntAct=EBI-2794004, EBI-2793994;
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane {ECO:0000269|PubMed:15857679}; Multi-pass membrane
protein {ECO:0000305}. Cell projection, dendritic spine membrane
{ECO:0000269|PubMed:15857679}; Multi-pass membrane protein
{ECO:0000305}. 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=VR1L1;
IsoId=O35433-1; Sequence=Displayed;
Name=2; Synonyms=VR1L2;
IsoId=O35433-2; Sequence=VSP_013432;
Name=3; Synonyms=VR.5'sv;
IsoId=O35433-3; Sequence=VSP_013431, VSP_013432;
Note=Inactive.;
-!- TISSUE SPECIFICITY: Predominantly expressed in trigeminal and
dorsal root sensory ganglia. Expressed also in hippocampus,
cortex, cerebellum, olfactory bulb, mesencephalon and hindbrain.
High expression in the cell bodies and dendrites of neurons in the
hippocampus and in the cortex. In the brain detected also in
astrocytes and pericytes (at protein level) (PubMed:15857679).
Isoform 1 and isoform 3 are expressed in brain and peripheral
blood mononuclear cells. {ECO:0000269|PubMed:10644739,
ECO:0000269|PubMed:15857679, ECO:0000269|PubMed:9349813}.
-!- DOMAIN: The association domain (AD) is necessary for self-
association.
-!- 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}.
-!- MISCELLANEOUS: Responses evoked by capsaicin, but not by low pH
and heat, can be antagonized by capsazepine.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
TrpV subfamily. TRPV1 sub-subfamily. {ECO:0000305}.
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EMBL; AF029310; AAC53398.1; -; mRNA.
EMBL; AF158248; AAF28389.1; -; mRNA.
EMBL; AB041029; BAA94306.1; -; mRNA.
EMBL; AB040873; BAA94307.1; -; mRNA.
EMBL; AF327067; AAK83151.1; -; Genomic_DNA.
EMBL; AF327067; AAK83152.1; -; Genomic_DNA.
PIR; T09054; T09054.
RefSeq; NP_114188.1; NM_031982.1. [O35433-1]
UniGene; Rn.3073; -.
PDB; 2NYJ; X-ray; 3.20 A; A=101-364.
PDB; 2PNN; X-ray; 2.70 A; A=101-364.
PDB; 3J5P; EM; 3.28 A; A/B/C/D=111-719.
PDB; 3J5Q; EM; 3.80 A; B/D/E/G=111-719.
PDB; 3J5R; EM; 4.20 A; A/B/C/D=111-719.
PDB; 3J9J; EM; -; A/B/C/D=111-719.
PDB; 3SUI; X-ray; 1.95 A; B=767-801.
PDB; 5IRX; EM; 2.95 A; A/B/C/D=110-764.
PDB; 5IRZ; EM; 3.28 A; B/C/D/E=110-764.
PDB; 5IS0; EM; 3.43 A; B/C/D/E=110-764.
PDBsum; 2NYJ; -.
PDBsum; 2PNN; -.
PDBsum; 3J5P; -.
PDBsum; 3J5Q; -.
PDBsum; 3J5R; -.
PDBsum; 3J9J; -.
PDBsum; 3SUI; -.
PDBsum; 5IRX; -.
PDBsum; 5IRZ; -.
PDBsum; 5IS0; -.
ProteinModelPortal; O35433; -.
SMR; O35433; -.
BioGrid; 249845; 2.
DIP; DIP-56949N; -.
IntAct; O35433; 1.
MINT; MINT-5117510; -.
STRING; 10116.ENSRNOP00000026493; -.
BindingDB; O35433; -.
ChEMBL; CHEMBL5102; -.
GuidetoPHARMACOLOGY; 507; -.
TCDB; 1.A.4.2.1; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; O35433; -.
PhosphoSitePlus; O35433; -.
PaxDb; O35433; -.
PRIDE; O35433; -.
Ensembl; ENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486. [O35433-1]
GeneID; 83810; -.
KEGG; rno:83810; -.
CTD; 7442; -.
RGD; 628841; Trpv1.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
GeneTree; ENSGT00550000074425; -.
HOGENOM; HOG000234630; -.
HOVERGEN; HBG054085; -.
InParanoid; O35433; -.
KO; K05222; -.
OMA; VEEVNWN; -.
OrthoDB; EOG091G01LY; -.
PhylomeDB; O35433; -.
TreeFam; TF314711; -.
Reactome; R-RNO-3295583; TRP channels.
EvolutionaryTrace; O35433; -.
PRO; PR:O35433; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000019486; -.
Genevisible; O35433; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; IMP:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043005; C:neuron projection; ISO:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0005262; F:calcium channel activity; ISO:RGD.
GO; GO:0015278; F:calcium-release channel activity; IMP:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0005261; F:cation channel activity; IDA:RGD.
GO; GO:0008324; F:cation transmembrane transporter activity; IDA:MGI.
GO; GO:0017081; F:chloride channel regulator activity; IDA:RGD.
GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IDA:UniProtKB.
GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005216; F:ion channel activity; ISO:RGD.
GO; GO:0015276; F:ligand-gated ion channel activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
GO; GO:0097603; F:temperature-gated ion channel activity; ISO:RGD.
GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
GO; GO:0071312; P:cellular response to alkaloid; IMP:UniProtKB.
GO; GO:0071318; P:cellular response to ATP; IDA:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
GO; GO:0071502; P:cellular response to temperature stimulus; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; ISO:RGD.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISO:RGD.
GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; ISO:RGD.
GO; GO:0002024; P:diet induced thermogenesis; ISO:RGD.
GO; GO:0001660; P:fever generation; ISO:RGD.
GO; GO:0014047; P:glutamate secretion; IDA:RGD.
GO; GO:0006954; P:inflammatory response; IEP:RGD.
GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
GO; GO:0001774; P:microglial cell activation; IMP:RGD.
GO; GO:0090212; P:negative regulation of establishment of blood-brain barrier; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0002790; P:peptide secretion; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
GO; GO:0060454; P:positive regulation of gastric acid secretion; IMP:RGD.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:1901594; P:response to capsazepine; IMP:UniProtKB.
GO; GO:0009408; P:response to heat; IDA:MGI.
GO; GO:0010243; P:response to organonitrogen compound; ISO:RGD.
GO; GO:0048265; P:response to pain; ISO:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0009268; P:response to pH; IDA:MGI.
GO; GO:0050954; P:sensory perception of mechanical stimulus; ISO:RGD.
GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
GO; GO:0060083; P:smooth muscle contraction involved in micturition; ISO:RGD.
GO; GO:0001659; P:temperature homeostasis; ISO:RGD.
GO; GO:0050955; P:thermoception; ISO:RGD.
GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISO:RGD.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR004729; TRP_channel.
InterPro; IPR024862; TRPV.
InterPro; IPR024863; TRPV1.
InterPro; IPR008347; TRPV1-4_channel.
PANTHER; PTHR10582; PTHR10582; 1.
PANTHER; PTHR10582:SF17; PTHR10582:SF17; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR01768; TRPVRECEPTOR.
SMART; SM00248; ANK; 4.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; ATP-binding; Calcium;
Calcium channel; Calcium transport; Calmodulin-binding; Cell junction;
Cell membrane; Cell projection; Complete proteome; Glycoprotein;
Ion channel; Ion transport; Lipid-binding; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; Synapse; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 838 Transient receptor potential cation
channel subfamily V member 1.
/FTId=PRO_0000215341.
TOPO_DOM 1 432 Cytoplasmic.
{ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TRANSMEM 433 453 Helical. {ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TOPO_DOM 454 471 Extracellular.
{ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TRANSMEM 472 497 Helical. {ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TOPO_DOM 498 510 Cytoplasmic.
{ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TRANSMEM 511 531 Helical. {ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TOPO_DOM 532 535 Extracellular.
{ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TRANSMEM 536 556 Helical. {ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TOPO_DOM 557 571 Cytoplasmic.
{ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TRANSMEM 572 599 Helical. {ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TOPO_DOM 600 626 Extracellular.
{ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
INTRAMEM 627 649 Pore-forming.
{ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200,
ECO:0000305|PubMed:10931826}.
TRANSMEM 658 686 Helical. {ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
TOPO_DOM 687 838 Cytoplasmic.
{ECO:0000269|PubMed:24305160,
ECO:0000269|PubMed:27281200}.
REPEAT 110 152 ANK 1.
REPEAT 153 199 ANK 2.
REPEAT 200 246 ANK 3.
REPEAT 247 282 ANK 4.
REPEAT 283 331 ANK 5.
REPEAT 332 358 ANK 6.
NP_BIND 199 202 ATP. {ECO:0000244|PDB:2NYJ,
ECO:0000244|PDB:2PNN}.
NP_BIND 210 211 ATP. {ECO:0000244|PDB:2PNN}.
REGION 114 115 Important for channel activation by
agonists and heat.
{ECO:0000269|PubMed:12228246}.
REGION 684 712 AD.
REGION 767 801 Interaction with calmodulin.
{ECO:0000269|PubMed:23109716}.
REGION 777 792 Required for PIP2-mediated channel
inhibition.
MOTIF 643 646 Selectivity filter.
{ECO:0000305|PubMed:10931826}.
METAL 646 646 Calcium; shared with neighboring
subunits. {ECO:0000250|UniProtKB:Q9R186}.
BINDING 115 115 ATP. {ECO:0000244|PDB:2PNN}.
BINDING 155 155 ATP. {ECO:0000244|PDB:2PNN}.
BINDING 160 160 ATP. {ECO:0000244|PDB:2NYJ,
ECO:0000244|PDB:2PNN}.
BINDING 164 164 ATP. {ECO:0000244|PDB:2NYJ,
ECO:0000244|PDB:2PNN}.
BINDING 512 512 Agonist. {ECO:0000269|PubMed:27281200}.
BINDING 550 550 Agonist. {ECO:0000269|PubMed:27281200}.
SITE 557 557 Important for agonist binding.
{ECO:0000269|PubMed:27281200}.
MOD_RES 116 116 Phosphoserine; by PKA and PKD.
{ECO:0000269|PubMed:12194871,
ECO:0000269|PubMed:15471852}.
MOD_RES 144 144 Phosphothreonine; by PKA; in vitro.
{ECO:0000269|PubMed:12194871}.
MOD_RES 370 370 Phosphothreonine; by PKA; in vitro.
{ECO:0000269|PubMed:12194871}.
MOD_RES 502 502 Phosphoserine; by PKC/PRKCE.
{ECO:0000269|PubMed:11884385,
ECO:0000269|PubMed:12194871,
ECO:0000269|PubMed:14630912}.
MOD_RES 704 704 Phosphothreonine.
{ECO:0000269|PubMed:14630912}.
MOD_RES 774 774 Phosphoserine; by PKA; in vitro.
{ECO:0000269|PubMed:12194871}.
MOD_RES 800 800 Phosphoserine; by PKC/PRKCE and
PKC/PRKCZ. {ECO:0000269|PubMed:11884385}.
MOD_RES 820 820 Phosphoserine; by PKA; in vitro.
{ECO:0000269|PubMed:12194871}.
CARBOHYD 604 604 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11683872}.
VAR_SEQ 1 307 Missing (in isoform 3).
{ECO:0000303|PubMed:10644739}.
/FTId=VSP_013431.
VAR_SEQ 348 407 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10644739,
ECO:0000303|PubMed:11578842}.
/FTId=VSP_013432.
MUTAGEN 114 114 R->E: Abolishes capsaicin-evoked current
and binding to resiniferatoxin.
{ECO:0000269|PubMed:12228246}.
MUTAGEN 114 114 Missing: Abolishes sensitivity to acid.
{ECO:0000269|PubMed:12228246}.
MUTAGEN 115 115 R->D: Abolishes capsaicin-evoked current
and binding to resiniferatoxin.
{ECO:0000269|PubMed:12228246}.
MUTAGEN 116 116 S->A: Abolishes phosphorylation by PKCM
and enhances channel response to
capsaicin by PKCM.
{ECO:0000269|PubMed:15471852}.
MUTAGEN 155 155 K->A: Abolishes ATP binding. Abolishes
CALM binding. Impairs normal
desensitization by repeated exposure to
capsaicin. {ECO:0000269|PubMed:17582331,
ECO:0000269|PubMed:23109716}.
MUTAGEN 160 160 K->A: Abolishes ATP binding. Abolishes
CALM binding.
{ECO:0000269|PubMed:17582331}.
MUTAGEN 199 199 Y->A: Strongly reduces affinity for ATP;
when associated with A-202.
{ECO:0000269|PubMed:17582331}.
MUTAGEN 202 202 Q->A: Strongly reduces affinity for ATP;
when associated with A-199.
{ECO:0000269|PubMed:17582331}.
MUTAGEN 502 502 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. {ECO:0000269|PubMed:11884385,
ECO:0000269|PubMed:14523239,
ECO:0000269|PubMed:14630912}.
MUTAGEN 511 511 Y->A: Loss of sensitivity to capsaicin.
{ECO:0000269|PubMed:14996838}.
MUTAGEN 547 547 M->L: Reduces binding to resiniferatoxin.
{ECO:0000269|PubMed:14996838}.
MUTAGEN 550 550 T->I: Reduces sensitivity to capsaicin
10-fold; no effect on sensitivity to
resiniferatoxin. Reduces binding to
resiniferatoxin.
{ECO:0000269|PubMed:14996838}.
MUTAGEN 636 636 E->K: Abolishes channel activity.
Restored channel activity; when
associated with E-639.
{ECO:0000269|PubMed:10931826}.
MUTAGEN 636 636 E->Q: Slight modification of pore
attributes.
{ECO:0000269|PubMed:10931826}.
MUTAGEN 639 639 K->E: Restored channel activity; when
associated with K-636.
{ECO:0000269|PubMed:10931826}.
MUTAGEN 644 644 M->Y: Slightly modifies channel
permeability.
{ECO:0000269|PubMed:10931826}.
MUTAGEN 646 646 D->N: Strongly reduces the affinity for
pore blocker ruthenium red and lowered
channel permeability for Mg(2+).
{ECO:0000269|PubMed:10931826}.
MUTAGEN 648 648 E->Q: Minor modification of pore
attributes.
{ECO:0000269|PubMed:10931826}.
MUTAGEN 651 651 E->Q: Minor modification of pore
attributes.
{ECO:0000269|PubMed:10931826}.
MUTAGEN 704 704 T->A: No effect on PMA-induced
enhancement of capsaicin-evoked currents
but reduces direct activation by PMA.
{ECO:0000269|PubMed:14523239,
ECO:0000269|PubMed:14630912}.
MUTAGEN 704 704 T->I: Loss of activation by capsaicin and
loss of vanilloid binding; when
associated with A-502.
{ECO:0000269|PubMed:14523239,
ECO:0000269|PubMed:14630912}.
MUTAGEN 761 761 E->K,Q: Abolishes capsaiin-evoked current
and binding to resiniferatoxin.
{ECO:0000269|PubMed:12228246}.
MUTAGEN 761 761 Missing: Abolishes sensitivity to acid.
{ECO:0000269|PubMed:12228246}.
MUTAGEN 785 785 R->Q: Strongly reduces CALM-binding and
abolishes PLC-mediated channel activity;
when associated with Q-788.
{ECO:0000269|PubMed:12764195,
ECO:0000269|PubMed:23109716}.
MUTAGEN 787 787 W->R: Reduces CALM-binding. Reduces
desensitization by repeated exposure to
capsaicin. {ECO:0000269|PubMed:23109716}.
MUTAGEN 788 788 K->Q: Strongly reduces CALM-binding and
abolishes PLC-mediated channel activity;
when associated with Q-785 or Q-797.
{ECO:0000269|PubMed:12764195,
ECO:0000269|PubMed:23109716}.
MUTAGEN 797 797 R->Q: Abolishes PLC-mediated channel
activity; when associated with Q-788.
{ECO:0000269|PubMed:12764195}.
MUTAGEN 800 800 S->A: Largely reduces direct activation
of by PMA and PMA-induced currents; no
effect on receptor kinase-induced
currents. {ECO:0000269|PubMed:11884385,
ECO:0000269|PubMed:12764195,
ECO:0000269|PubMed:14523239}.
CONFLICT 18 18 E -> D (in Ref. 3; BAA94307).
{ECO:0000305}.
CONFLICT 36 36 V -> A (in Ref. 4; AAK83151).
{ECO:0000305}.
CONFLICT 48 48 R -> G (in Ref. 3; BAA94306).
{ECO:0000305}.
CONFLICT 51 51 G -> W (in Ref. 3; BAA94306).
{ECO:0000305}.
CONFLICT 96 96 P -> Q (in Ref. 3; BAA94307).
{ECO:0000305}.
CONFLICT 179 179 V -> I (in Ref. 4; AAK83151).
{ECO:0000305}.
CONFLICT 735 735 K -> Q (in Ref. 3; BAA94306).
{ECO:0000305}.
HELIX 114 122 {ECO:0000244|PDB:2PNN}.
TURN 128 131 {ECO:0000244|PDB:2PNN}.
HELIX 132 138 {ECO:0000244|PDB:2PNN}.
HELIX 146 148 {ECO:0000244|PDB:2PNN}.
TURN 151 153 {ECO:0000244|PDB:2PNN}.
HELIX 157 163 {ECO:0000244|PDB:2PNN}.
HELIX 171 182 {ECO:0000244|PDB:2PNN}.
HELIX 186 190 {ECO:0000244|PDB:2PNN}.
TURN 197 201 {ECO:0000244|PDB:2PNN}.
HELIX 204 210 {ECO:0000244|PDB:2PNN}.
HELIX 214 222 {ECO:0000244|PDB:2PNN}.
HELIX 234 236 {ECO:0000244|PDB:2PNN}.
STRAND 240 242 {ECO:0000244|PDB:2PNN}.
HELIX 251 257 {ECO:0000244|PDB:2PNN}.
HELIX 261 269 {ECO:0000244|PDB:2PNN}.
HELIX 287 294 {ECO:0000244|PDB:2PNN}.
HELIX 299 319 {ECO:0000244|PDB:2PNN}.
HELIX 325 327 {ECO:0000244|PDB:2PNN}.
HELIX 336 342 {ECO:0000244|PDB:2PNN}.
HELIX 346 356 {ECO:0000244|PDB:2PNN}.
TURN 360 362 {ECO:0000244|PDB:5IRX}.
TURN 363 365 {ECO:0000244|PDB:5IRZ}.
STRAND 369 374 {ECO:0000244|PDB:5IRX}.
STRAND 377 381 {ECO:0000244|PDB:5IRX}.
STRAND 385 388 {ECO:0000244|PDB:5IRX}.
TURN 390 392 {ECO:0000244|PDB:3J9J}.
HELIX 395 400 {ECO:0000244|PDB:5IRX}.
TURN 407 411 {ECO:0000244|PDB:3J5P}.
HELIX 412 415 {ECO:0000244|PDB:5IRX}.
HELIX 419 428 {ECO:0000244|PDB:5IRX}.
HELIX 430 453 {ECO:0000244|PDB:5IRX}.
STRAND 458 461 {ECO:0000244|PDB:3J5P}.
HELIX 469 498 {ECO:0000244|PDB:5IRX}.
HELIX 501 504 {ECO:0000244|PDB:3J9J}.
TURN 506 508 {ECO:0000244|PDB:5IRX}.
HELIX 511 531 {ECO:0000244|PDB:5IRX}.
HELIX 537 550 {ECO:0000244|PDB:5IRX}.
HELIX 551 554 {ECO:0000244|PDB:5IRX}.
TURN 555 558 {ECO:0000244|PDB:5IRX}.
TURN 560 563 {ECO:0000244|PDB:5IRX}.
HELIX 564 574 {ECO:0000244|PDB:5IRX}.
HELIX 576 580 {ECO:0000244|PDB:5IRX}.
TURN 581 583 {ECO:0000244|PDB:5IRX}.
HELIX 584 598 {ECO:0000244|PDB:5IRX}.
STRAND 601 603 {ECO:0000244|PDB:3J5P}.
STRAND 627 629 {ECO:0000244|PDB:5IRX}.
HELIX 630 641 {ECO:0000244|PDB:5IRX}.
STRAND 647 649 {ECO:0000244|PDB:5IS0}.
HELIX 656 670 {ECO:0000244|PDB:5IRX}.
TURN 671 673 {ECO:0000244|PDB:5IRX}.
HELIX 674 691 {ECO:0000244|PDB:5IRX}.
HELIX 693 712 {ECO:0000244|PDB:5IRX}.
HELIX 716 719 {ECO:0000244|PDB:5IRX}.
STRAND 732 734 {ECO:0000244|PDB:5IS0}.
STRAND 743 746 {ECO:0000244|PDB:5IRX}.
HELIX 788 792 {ECO:0000244|PDB:3SUI}.
HELIX 793 795 {ECO:0000244|PDB:3SUI}.
SEQUENCE 838 AA; 94948 MW; DAFC80B12BDF71BF CRC64;
MEQRASLDSE ESESPPQENS CLDPPDRDPN CKPPPVKPHI FTTRSRTRLF GKGDSEEASP
LDCPYEEGGL ASCPIITVSS VLTIQRPGDG PASVRPSSQD SVSAGEKPPR LYDRRSIFDA
VAQSNCQELE SLLPFLQRSK KRLTDSEFKD PETGKTCLLK AMLNLHNGQN DTIALLLDVA
RKTDSLKQFV NASYTDSYYK GQTALHIAIE RRNMTLVTLL VENGADVQAA ANGDFFKKTK
GRPGFYFGEL PLSLAACTNQ LAIVKFLLQN SWQPADISAR DSVGNTVLHA LVEVADNTVD
NTKFVTSMYN EILILGAKLH PTLKLEEITN RKGLTPLALA ASSGKIGVLA YILQREIHEP
ECRHLSRKFT EWAYGPVHSS LYDLSCIDTC EKNSVLEVIA YSSSETPNRH DMLLVEPLNR
LLQDKWDRFV KRIFYFNFFV YCLYMIIFTA AAYYRPVEGL PPYKLKNTVG DYFRVTGEIL
SVSGGVYFFF RGIQYFLQRR PSLKSLFVDS YSEILFFVQS LFMLVSVVLY FSQRKEYVAS
MVFSLAMGWT NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYLVFLFG FSTAVVTLIE
DGKNNSLPME STPHKCRGSA CKPGNSYNSL YSTCLELFKF TIGMGDLEFT ENYDFKAVFI
ILLLAYVILT YILLLNMLIA LMGETVNKIA QESKNIWKLQ RAITILDTEK SFLKCMRKAF
RSGKLLQVGF TPDGKDDYRW CFRVDEVNWT TWNTNVGIIN EDPGNCEGVK RTLSFSLRSG
RVSGRNWKNF ALVPLLRDAS TRDRHATQQE EVQLKHYTGS LKPEDAEVFK DSMVPGEK


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DL-TRPV1-Mu Mouse Transient Receptor Potential Cation Channel Subfamily V, Member 1 (TRPV1) ELISA Kit 96T
UB-E10451 Rat Transient Receptor Potential Cation Channel Subfamily V, Member 1(TRPV1)ELISA Kit 96T
201-11-1194 Rat Transient Receptor Potential Cation Channel Subfamily V, Member 1 (TRPV1)ELISA Kit 96T


 

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