TRPV1_RAT
ID TRPV1_RAT Reviewed; 838 AA.
AC O35433; Q920B3; Q920B4; Q9JLM0; Q9JM56; Q9JM57;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 1;
DE Short=TrpV1;
DE AltName: Full=Capsaicin receptor;
DE AltName: Full=Osm-9-like TRP channel 1;
DE Short=OTRPC1;
DE AltName: Full=Vanilloid receptor 1;
DE AltName: Full=Vanilloid receptor type 1-like;
GN Name=Trpv1; Synonyms=Vr1, Vr1l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Spinal ganglion;
RX PubMed=9349813; DOI=10.1038/39807;
RA Caterina M.J., Schumacher M.A., Tominaga M., Rosen T.A., Levine J.D.,
RA Julius D.;
RT "The capsaicin receptor: a heat-activated ion channel in the pain
RT pathway.";
RL Nature 389:816-824(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND FUNCTION
RP (ISOFORM 3).
RC STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion, and Trigeminal ganglion;
RX PubMed=10644739; DOI=10.1074/jbc.275.4.2756;
RA Schumacher M.A., Moff I., Sudanagunta S.P., Levine J.D.;
RT "Molecular cloning of an N-terminal splice variant of the capsaicin
RT receptor. Loss of N-terminal domain suggests functional divergence among
RT capsaicin receptor subtypes.";
RL J. Biol. Chem. 275:2756-2762(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11578842; DOI=10.1016/s0304-3940(01)02185-1;
RA Tsutsumi S., Tomioka A., Sudo M., Nakamura A., Shirakura K., Takagishi K.,
RA Kohama K.;
RT "Propofol activates vanilloid receptor channels expressed in human
RT embryonic kidney 293 cells.";
RL Neurosci. Lett. 312:45-49(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-468, AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley;
RX PubMed=11549313; DOI=10.1006/geno.2001.6582;
RA Xue Q., Yu Y., Trilk S.L., Jong B.E., Schumacher M.A.;
RT "The genomic organization of the gene encoding the vanilloid receptor:
RT evidence for multiple splice variants.";
RL Genomics 76:14-20(2001).
RN [5]
RP CHARACTERIZATION OF CHANNEL PORE, AND MUTAGENESIS OF GLU-636; LYS-639;
RP MET-644; ASP-646; GLU-648 AND GLU-651.
RX PubMed=10931826; DOI=10.1074/jbc.m002391200;
RA Garcia-Martinez C., Morenilla-Palao C., Planells-Cases R., Merino J.M.,
RA Ferrer-Montiel A.V.;
RT "Identification of an aspartic residue in the P-loop of the vanilloid
RT receptor that modulates pore properties.";
RL J. Biol. Chem. 275:32552-32558(2000).
RN [6]
RP FUNCTION.
RX PubMed=11140687; DOI=10.1038/35050121;
RA Premkumar L.S., Ahern G.P.;
RT "Induction of vanilloid receptor channel activity by protein kinase C.";
RL Nature 408:985-990(2000).
RN [7]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-604.
RX PubMed=11683872; DOI=10.1046/j.1432-1033.2001.02500.x;
RA Jahnel R., Dreger M., Gillen C., Bender O., Kurreck J., Hucho F.;
RT "Biochemical characterization of the vanilloid receptor 1 expressed in a
RT dorsal root ganglia derived cell line.";
RL Eur. J. Biochem. 268:5489-5496(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH PRKCG AND NTRK1.
RX PubMed=11418861; DOI=10.1038/35082088;
RA Chuang H.H., Prescott E.D., Kong H., Shields S., Jordt S.E., Basbaum A.I.,
RA Chao M.V., Julius D.;
RT "Bradykinin and nerve growth factor release the capsaicin receptor from
RT PtdIns(4,5)P2-mediated inhibition.";
RL Nature 411:957-962(2001).
RN [9]
RP PHOSPHORYLATION AT SER-502 AND SER-800, AND MUTAGENESIS OF SER-502 AND
RP SER-800.
RX PubMed=11884385; DOI=10.1074/jbc.c200104200;
RA Numazaki M., Tominaga T., Toyooka H., Tominaga M.;
RT "Direct phosphorylation of capsaicin receptor VR1 by protein kinase
RT Cepsilon and identification of two target serine residues.";
RL J. Biol. Chem. 277:13375-13378(2002).
RN [10]
RP FUNCTION.
RX PubMed=12095983; DOI=10.1074/jbc.m201551200;
RA Olah Z., Karai L., Iadarola M.J.;
RT "Protein kinase C(alpha) is required for vanilloid receptor 1 activation.
RT Evidence for multiple signaling pathways.";
RL J. Biol. Chem. 277:35752-35759(2002).
RN [11]
RP FUNCTION, AND PHOSPHORYLATION AT SER-116; THR-144; THR-370; SER-502;
RP SER-774 AND SER-820.
RX PubMed=12194871; DOI=10.1016/s0896-6273(02)00802-4;
RA Bhave G., Zhu W., Wang H., Brasier D.J., Oxford G.S., Gereau R.W. IV;
RT "cAMP-dependent protein kinase regulates desensitization of the capsaicin
RT receptor (VR1) by direct phosphorylation.";
RL Neuron 35:721-731(2002).
RN [12]
RP FUNCTION, AND INTERACTION WITH CALMODULIN.
RX PubMed=12808128; DOI=10.1073/pnas.1337252100;
RA Numazaki M., Tominaga T., Takeuchi K., Murayama N., Toyooka H.,
RA Tominaga M.;
RT "Structural determinant of TRPV1 desensitization interacts with
RT calmodulin.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8002-8006(2003).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF SER-502; THR-704 AND SER-800.
RX PubMed=14523239; DOI=10.1073/pnas.2032100100;
RA Bhave G., Hu H.J., Glauner K.S., Zhu W., Wang H., Brasier D.J.,
RA Oxford G.S., Gereau R.W. IV;
RT "Protein kinase C phosphorylation sensitizes but does not activate the
RT capsaicin receptor transient receptor potential vanilloid 1 (TRPV1).";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12480-12485(2003).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ARG-785; LYS-788; ARG-797 AND SER-800.
RX PubMed=12764195; DOI=10.1126/science.1083646;
RA Prescott E.D., Julius D.;
RT "A modular PIP2 binding site as a determinant of capsaicin receptor
RT sensitivity.";
RL Science 300:1284-1288(2003).
RN [15]
RP INTERACTION WITH CSK.
RX PubMed=15084474; DOI=10.1152/ajpcell.00113.2004;
RA Jin X., Morsy N., Winston J., Pasricha P.J., Garrett K., Akbarali H.I.;
RT "Modulation of TRPV1 by nonreceptor tyrosine kinase, c-Src kinase.";
RL Am. J. Physiol. 287:C558-C563(2004).
RN [16]
RP MUTAGENESIS OF ARG-114; ARG-115 AND GLU-761.
RX PubMed=12228246; DOI=10.1074/jbc.m207103200;
RA Jung J., Lee S.Y., Hwang S.W., Cho H., Shin J., Kang Y.S., Kim S., Oh U.;
RT "Agonist recognition sites in the cytosolic tails of vanilloid receptor
RT 1.";
RL J. Biol. Chem. 277:44448-44454(2002).
RN [17]
RP FUNCTION, PHOSPHORYLATION AT SER-502 AND THR-704, AND MUTAGENESIS OF
RP SER-502 AND THR-704.
RX PubMed=14630912; DOI=10.1074/jbc.m311448200;
RA Jung J., Shin J.S., Lee S.-Y., Hwang S.W., Koo J., Cho H., Oh U.;
RT "Phosphorylation of vanilloid receptor 1 by Ca2+/calmodulin-dependent
RT kinase II regulates its vanilloid binding.";
RL J. Biol. Chem. 279:7048-7054(2004).
RN [18]
RP MUTAGENESIS OF TYR-511; MET-547 AND THR-550.
RX PubMed=14996838; DOI=10.1074/jbc.m312577200;
RA Gavva N.R., Klionsky L., Qu Y., Shi L., Tamir R., Edenson S., Zhang T.J.,
RA Viswanadhan V.N., Toth A., Pearce L.V., Vanderah T.W., Porreca F.,
RA Blumberg P.M., Lile J., Sun Y., Wild K., Louis J.C., Treanor J.J.;
RT "Molecular determinants of vanilloid sensitivity in TRPV1.";
RL J. Biol. Chem. 279:20283-20295(2004).
RN [19]
RP FUNCTION.
RX PubMed=15173182; DOI=10.1074/jbc.m402966200;
RA Hellwig N., Plant T.D., Janson W., Schafer M., Schultz G., Schaefer M.;
RT "TRPV1 acts as proton channel to induce acidification in nociceptive
RT neurons.";
RL J. Biol. Chem. 279:34553-34561(2004).
RN [20]
RP INTERACTION WITH PRKCM, PHOSPHORYLATION AT SER-116, AND MUTAGENESIS OF
RP SER-116.
RX PubMed=15471852; DOI=10.1074/jbc.m410331200;
RA Wang Y., Kedei N., Wang M., Wang Q.J., Huppler A.R., Toth A., Tran R.,
RA Blumberg P.M.;
RT "Interaction between protein kinase Cmu and the vanilloid receptor type
RT 1.";
RL J. Biol. Chem. 279:53674-53682(2004).
RN [21]
RP SUBUNIT.
RX PubMed=15190102; DOI=10.1523/jneurosci.0202-04.2004;
RA Garcia-Sanz N., Fernandez-Carvajal A., Morenilla-Palao C.,
RA Planells-Cases R., Fajardo-Sanchez E., Fernandez-Ballester G.,
RA Ferrer-Montiel A.;
RT "Identification of a tetramerization domain in the C-terminus of the
RT vanilloid receptor.";
RL J. Neurosci. 24:5307-5314(2004).
RN [22]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15857679; DOI=10.1016/j.molbrainres.2004.12.003;
RA Toth A., Boczan J., Kedei N., Lizanecz E., Bagi Z., Papp Z., Edes I.,
RA Csiba L., Blumberg P.M.;
RT "Expression and distribution of vanilloid receptor 1 (TRPV1) in the adult
RT rat brain.";
RL Brain Res. Mol. Brain Res. 135:162-168(2005).
RN [23]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=20510930; DOI=10.1016/j.cell.2010.03.052;
RA Bohlen C.J., Priel A., Zhou S., King D., Siemens J., Julius D.;
RT "A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by
RT targeting the outer pore domain.";
RL Cell 141:834-845(2010).
RN [24]
RP FUNCTION.
RX PubMed=21076423; DOI=10.1038/nn.2684;
RA Chavez A.E., Chiu C.Q., Castillo P.E.;
RT "TRPV1 activation by endogenous anandamide triggers postsynaptic long-term
RT depression in dentate gyrus.";
RL Nat. Neurosci. 13:1511-1518(2010).
RN [25] {ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 101-364 IN COMPLEX WITH ATP,
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, ATP-BINDING,
RP CALMODULIN-BINDING, MUTAGENESIS OF LYS-155; LYS-160; TYR-199 AND GLN-202,
RP AND ANKYRIN REPEATS.
RX PubMed=17582331; DOI=10.1016/j.neuron.2007.05.027;
RA Lishko P.V., Procko E., Jin X., Phelps C.B., Gaudet R.;
RT "The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel
RT sensitivity.";
RL Neuron 54:905-918(2007).
RN [26] {ECO:0007744|PDB:3SUI}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 767-801 IN COMPLEX WITH CALM,
RP FUNCTION, MUTAGENESIS OF LYS-155; ARG-785; TRP-787 AND LYS-788,
RP CALMODULIN-BINDING, INTERACTION WITH CALM, AND ACTIVITY REGULATION.
RX PubMed=23109716; DOI=10.1085/jgp.201210810;
RA Lau S.Y., Procko E., Gaudet R.;
RT "Distinct properties of Ca2+-calmodulin binding to N- and C-terminal
RT regulatory regions of the TRPV1 channel.";
RL J. Gen. Physiol. 140:541-555(2012).
RN [27] {ECO:0007744|PDB:3J5P}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.27 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, TOPOLOGY, ANK REPEATS, AND SUBUNIT.
RX PubMed=24305160; DOI=10.1038/nature12822;
RA Liao M., Cao E., Julius D., Cheng Y.;
RT "Structure of the TRPV1 ion channel determined by electron cryo-
RT microscopy.";
RL Nature 504:107-112(2013).
RN [28] {ECO:0007744|PDB:3J5Q, ECO:0007744|PDB:3J5R}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS) IN COMPLEXES WITH
RP CAPSAICIN AND TARANTULA DOUBLE-KNOT TOXIN, AND SUBUNIT.
RX PubMed=24305161; DOI=10.1038/nature12823;
RA Cao E., Liao M., Cheng Y., Julius D.;
RT "TRPV1 structures in distinct conformations reveal activation mechanisms.";
RL Nature 504:113-118(2013).
RN [29] {ECO:0007744|PDB:5IRX, ECO:0007744|PDB:5IRZ, ECO:0007744|PDB:5IS0}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.95 ANGSTROMS) OF 110-764 OF APOPROTEIN
RP AND IN COMPLEX WITH AGONIST, SUBUNIT, TOPOLOGY, AND LIPID-BINDING.
RX PubMed=27281200; DOI=10.1038/nature17964;
RA Gao Y., Cao E., Julius D., Cheng Y.;
RT "TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid
RT action.";
RL Nature 534:347-351(2016).
CC -!- FUNCTION: Ligand-activated non-selective calcium permeant cation
CC channel involved in detection of noxious chemical and thermal stimuli.
CC Seems to mediate proton influx and may be involved in intracellular
CC acidosis in nociceptive neurons. Involved in mediation of inflammatory
CC pain and hyperalgesia. Sensitized by a phosphatidylinositol second
CC messenger system activated by receptor tyrosine kinases, which involves
CC PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and
CC temperatures higher than 42 degrees Celsius, exhibits a time- and
CC Ca(2+)-dependent outward rectification, followed by a long-lasting
CC refractory state. Mild extracellular acidic pH (6.5) potentiates
CC channel activation by noxious heat and vanilloids, whereas acidic
CC conditions (pH <6) directly activate the channel. Can be activated by
CC endogenous compounds, including 12-hydroperoxytetraenoic acid and
CC bradykinin. Acts as ionotropic endocannabinoid receptor with central
CC neuromodulatory effects. Triggers a form of long-term depression
CC (TRPV1-LTD) mediated by the endocannabinoid anandamine in the
CC hippocampus and nucleus accumbens by affecting AMPA receptors
CC endocytosis. {ECO:0000269|PubMed:11140687, ECO:0000269|PubMed:11418861,
CC ECO:0000269|PubMed:11578842, ECO:0000269|PubMed:12095983,
CC ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:12764195,
CC ECO:0000269|PubMed:12808128, ECO:0000269|PubMed:14523239,
CC ECO:0000269|PubMed:14630912, ECO:0000269|PubMed:15173182,
CC ECO:0000269|PubMed:17582331, ECO:0000269|PubMed:20510930,
CC ECO:0000269|PubMed:21076423, ECO:0000269|PubMed:23109716,
CC ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:9349813}.
CC -!- FUNCTION: [Isoform 3]: Does not display channel activity in response to
CC noxious chemical compounds, such as capsaicin and the vanilloid
CC resiniferatoxin. Channel activity is not elicited by mildly acidic
CC extracellular pH, and only slight channel activity is observed in
CC response to noxiuos heat stimuli. {ECO:0000269|PubMed:10644739}.
CC -!- ACTIVITY REGULATION: Channel activity is activated via the interaction
CC with PIRT and phosphatidylinositol 4,5-bisphosphate (PIP2). Both PIRT
CC and PIP2 are required to activate channel activity (By similarity). The
CC channel is sensitized by ATP binding. Repeated stimulation with
CC capsaicin gives rise to progressively smaller responses, due to
CC desensitization. This desensitization is triggered by the influx of
CC calcium ions and is inhibited by elevated ATP levels. Ca(2+) and CALM
CC displace ATP from its binding site and trigger a conformation change
CC that leads to a closed, desensitized channel. Intracellular PIP2
CC inhibits desensitization. The double-knot toxin (DkTx) from the Chinese
CC earth tiger tarantula activates the channel and traps it in an open
CC conformation. The Scolopendra mutilans RhTx toxin potentiates the heat
CC activation pathway mediated by this channel by binding to the charge-
CC rich outer pore region (in an activated state) (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q704Y3,
CC ECO:0000269|PubMed:17582331, ECO:0000269|PubMed:20510930,
CC ECO:0000269|PubMed:23109716}.
CC -!- SUBUNIT: Interacts with PIRT (By similarity). Homotetramer
CC (PubMed:15190102, PubMed:24305160, PubMed:24305161, PubMed:27281200).
CC May also form a heteromeric channel with TRPV3 (By similarity).
CC Interacts with CALM, PRKCM and CSK (PubMed:12808128, PubMed:15084474,
CC PubMed:15471852, PubMed:17582331). Interacts with PRKCG and NTRK1,
CC probably by forming a trimeric complex (PubMed:11418861). Interacts
CC with the Scolopendra mutilans RhTx toxin (By similarity). Interacts
CC with the spider Tau-theraphotoxin-Hs1a (PubMed:27281200). Interacts
CC with TMEM100 (By similarity). Interacts with PACS2 (By similarity).
CC {ECO:0000250|UniProtKB:Q704Y3, ECO:0000250|UniProtKB:Q8NER1,
CC ECO:0000269|PubMed:11418861, ECO:0000269|PubMed:12808128,
CC ECO:0000269|PubMed:15084474, ECO:0000269|PubMed:15190102,
CC ECO:0000269|PubMed:15471852, ECO:0000269|PubMed:23109716,
CC ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:24305161,
CC ECO:0000269|PubMed:27281200}.
CC -!- INTERACTION:
CC O35433; O35433: Trpv1; NbExp=11; IntAct=EBI-2794004, EBI-2794004;
CC O35433; P0CH43; Xeno; NbExp=2; IntAct=EBI-2794004, EBI-2793994;
CC O35433-1; O35433-1: Trpv1; NbExp=2; IntAct=EBI-15703031, EBI-15703031;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:15857679}; Multi-pass membrane protein
CC {ECO:0000305}. Cell projection, dendritic spine membrane
CC {ECO:0000269|PubMed:15857679}; Multi-pass membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11578842,
CC ECO:0000269|PubMed:15857679, ECO:0000269|PubMed:9349813}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:24305160,
CC ECO:0000269|PubMed:24305161, ECO:0000269|PubMed:27281200}. Note=Mostly,
CC but not exclusively expressed in postsynaptic dendritic spines.
CC {ECO:0000269|PubMed:15857679}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=VR1L1;
CC IsoId=O35433-1; Sequence=Displayed;
CC Name=2; Synonyms=VR1L2;
CC IsoId=O35433-2; Sequence=VSP_013432;
CC Name=3; Synonyms=VR.5'sv;
CC IsoId=O35433-3; Sequence=VSP_013431, VSP_013432;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in trigeminal and dorsal
CC root sensory ganglia. Expressed also in hippocampus, cortex,
CC cerebellum, olfactory bulb, mesencephalon and hindbrain. High
CC expression in the cell bodies and dendrites of neurons in the
CC hippocampus and in the cortex. In the brain detected also in astrocytes
CC and pericytes (at protein level) (PubMed:15857679). Isoform 1 and
CC isoform 3 are expressed in brain and peripheral blood mononuclear
CC cells. {ECO:0000269|PubMed:10644739, ECO:0000269|PubMed:15857679,
CC ECO:0000269|PubMed:9349813}.
CC -!- DOMAIN: The association domain (AD) is necessary for self-association.
CC -!- PTM: Phosphorylation by PKA reverses capsaicin-induced
CC dephosphorylation at multiple sites, probably including Ser-116 as a
CC major phosphorylation site. Phosphorylation by CAMKII seems to regulate
CC binding to vanilloids. Phosphorylated and modulated by PRKCE, PRKCM and
CC probably PRKCZ. Dephosphorylation by calcineurin seems to lead to
CC receptor desensitization and phosphorylation by CAMKII recovers
CC activity. {ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871,
CC ECO:0000269|PubMed:14630912, ECO:0000269|PubMed:15471852}.
CC -!- MISCELLANEOUS: Responses evoked by capsaicin, but not by low pH and
CC heat, can be antagonized by capsazepine.
CC -!- MISCELLANEOUS: [Isoform 3]: Inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV1 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF029310; AAC53398.1; -; mRNA.
DR EMBL; AF158248; AAF28389.1; -; mRNA.
DR EMBL; AB041029; BAA94306.1; -; mRNA.
DR EMBL; AB040873; BAA94307.1; -; mRNA.
DR EMBL; AF327067; AAK83151.1; -; Genomic_DNA.
DR EMBL; AF327067; AAK83152.1; -; Genomic_DNA.
DR PIR; T09054; T09054.
DR RefSeq; NP_114188.1; NM_031982.1. [O35433-1]
DR PDB; 2NYJ; X-ray; 3.20 A; A=101-364.
DR PDB; 2PNN; X-ray; 2.70 A; A=101-364.
DR PDB; 3J5P; EM; 3.28 A; A/B/C/D=111-719.
DR PDB; 3J5Q; EM; 3.80 A; B/D/E/G=111-719.
DR PDB; 3J5R; EM; 4.20 A; A/B/C/D=111-719.
DR PDB; 3J9J; EM; -; A/B/C/D=111-719.
DR PDB; 3SUI; X-ray; 1.95 A; B=767-801.
DR PDB; 5IRX; EM; 2.95 A; A/B/C/D=110-764.
DR PDB; 5IRZ; EM; 3.28 A; B/C/D/E=110-764.
DR PDB; 5IS0; EM; 3.43 A; B/C/D/E=110-764.
DR PDB; 7L2H; EM; 2.63 A; A/B/C/D=2-838.
DR PDB; 7L2I; EM; 3.70 A; A/B/C/D=2-838.
DR PDB; 7L2J; EM; 3.66 A; A/B/C/D=2-838.
DR PDB; 7L2K; EM; 3.89 A; A/B/C/D=2-838.
DR PDB; 7L2L; EM; 3.42 A; A/B/C/D=2-838.
DR PDB; 7L2M; EM; 3.84 A; A/B/C/D=2-838.
DR PDB; 7L2N; EM; 3.09 A; A/B/C/D=2-838.
DR PDB; 7L2O; EM; 3.64 A; A/B/C/D=2-838.
DR PDB; 7L2P; EM; 2.60 A; A/B/C/D=110-764.
DR PDB; 7L2R; EM; 3.30 A; A/B/C/D=110-764.
DR PDB; 7L2S; EM; 2.71 A; A/B/C/D=110-764.
DR PDB; 7L2T; EM; 3.08 A; A/B/C/D=110-764.
DR PDB; 7L2U; EM; 3.47 A; A/B/C/D=110-764.
DR PDB; 7L2V; EM; 3.64 A; A/B/C/D=110-764.
DR PDB; 7L2W; EM; 3.16 A; A/B/C/D=110-764.
DR PDB; 7L2X; EM; 3.26 A; A/B/C/D=110-764.
DR PDB; 7LP9; EM; 2.63 A; A/B/C/D=1-838.
DR PDB; 7LPA; EM; 3.37 A; A/B/C/D=1-838.
DR PDB; 7LPB; EM; 3.54 A; A/B/C/D=1-838.
DR PDB; 7LPC; EM; 3.06 A; A/B/C/D=1-838.
DR PDB; 7LPD; EM; 3.55 A; A/B/C/D=1-838.
DR PDB; 7LPE; EM; 3.72 A; A/B/C/D=1-838.
DR PDB; 7MZ5; EM; 2.76 A; A/B/C/D=2-838.
DR PDB; 7MZ6; EM; 2.91 A; A/B/C/D=110-764.
DR PDB; 7MZ7; EM; 3.35 A; A/B/C/D=110-764.
DR PDB; 7MZ9; EM; 3.18 A; A/B/C/D=110-764.
DR PDB; 7MZA; EM; 3.46 A; A/B/C/D=110-764.
DR PDB; 7MZB; EM; 3.72 A; A/B/C/D=110-764.
DR PDB; 7MZC; EM; 3.03 A; A/B/C/D=110-764.
DR PDB; 7MZD; EM; 2.90 A; A/B/C/D=110-764.
DR PDB; 7MZE; EM; 3.42 A; A/B/C/D=110-764.
DR PDBsum; 2NYJ; -.
DR PDBsum; 2PNN; -.
DR PDBsum; 3J5P; -.
DR PDBsum; 3J5Q; -.
DR PDBsum; 3J5R; -.
DR PDBsum; 3J9J; -.
DR PDBsum; 3SUI; -.
DR PDBsum; 5IRX; -.
DR PDBsum; 5IRZ; -.
DR PDBsum; 5IS0; -.
DR PDBsum; 7L2H; -.
DR PDBsum; 7L2I; -.
DR PDBsum; 7L2J; -.
DR PDBsum; 7L2K; -.
DR PDBsum; 7L2L; -.
DR PDBsum; 7L2M; -.
DR PDBsum; 7L2N; -.
DR PDBsum; 7L2O; -.
DR PDBsum; 7L2P; -.
DR PDBsum; 7L2R; -.
DR PDBsum; 7L2S; -.
DR PDBsum; 7L2T; -.
DR PDBsum; 7L2U; -.
DR PDBsum; 7L2V; -.
DR PDBsum; 7L2W; -.
DR PDBsum; 7L2X; -.
DR PDBsum; 7LP9; -.
DR PDBsum; 7LPA; -.
DR PDBsum; 7LPB; -.
DR PDBsum; 7LPC; -.
DR PDBsum; 7LPD; -.
DR PDBsum; 7LPE; -.
DR PDBsum; 7MZ5; -.
DR PDBsum; 7MZ6; -.
DR PDBsum; 7MZ7; -.
DR PDBsum; 7MZ9; -.
DR PDBsum; 7MZA; -.
DR PDBsum; 7MZB; -.
DR PDBsum; 7MZC; -.
DR PDBsum; 7MZD; -.
DR PDBsum; 7MZE; -.
DR AlphaFoldDB; O35433; -.
DR SMR; O35433; -.
DR BioGRID; 249845; 3.
DR DIP; DIP-56949N; -.
DR IntAct; O35433; 3.
DR MINT; O35433; -.
DR STRING; 10116.ENSRNOP00000026493; -.
DR BindingDB; O35433; -.
DR ChEMBL; CHEMBL5102; -.
DR DrugCentral; O35433; -.
DR GuidetoPHARMACOLOGY; 507; -.
DR TCDB; 1.A.4.2.1; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; O35433; 1 site.
DR iPTMnet; O35433; -.
DR PhosphoSitePlus; O35433; -.
DR PaxDb; O35433; -.
DR ABCD; O35433; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486. [O35433-1]
DR Ensembl; ENSRNOT00000093394; ENSRNOP00000086172; ENSRNOG00000019486. [O35433-2]
DR GeneID; 83810; -.
DR KEGG; rno:83810; -.
DR CTD; 7442; -.
DR RGD; 628841; Trpv1.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000160870; -.
DR HOGENOM; CLU_012795_1_0_1; -.
DR InParanoid; O35433; -.
DR OMA; YQYLHQN; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; O35433; -.
DR TreeFam; TF314711; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR EvolutionaryTrace; O35433; -.
DR PRO; PR:O35433; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000019486; Expressed in adult mammalian kidney and 16 other tissues.
DR Genevisible; O35433; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR GO; GO:0015278; F:calcium-release channel activity; IMP:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IDA:RGD.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IDA:MGI.
DR GO; GO:0017081; F:chloride channel regulator activity; IDA:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IDA:UniProtKB.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0097603; F:temperature-gated ion channel activity; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0071312; P:cellular response to alkaloid; IMP:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; IDA:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; ISO:RGD.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISO:RGD.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; ISO:RGD.
DR GO; GO:0002024; P:diet induced thermogenesis; ISO:RGD.
DR GO; GO:0001660; P:fever generation; ISO:RGD.
DR GO; GO:0014047; P:glutamate secretion; IDA:RGD.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0001774; P:microglial cell activation; IMP:RGD.
DR GO; GO:0090212; P:negative regulation of establishment of blood-brain barrier; IMP:RGD.
DR GO; GO:0010459; P:negative regulation of heart rate; IMP:RGD.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IMP:RGD.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0002790; P:peptide secretion; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0060454; P:positive regulation of gastric acid secretion; IMP:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:1901594; P:response to capsazepine; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IDA:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:RGD.
DR GO; GO:0048265; P:response to pain; ISO:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009268; P:response to pH; IDA:MGI.
DR GO; GO:0050954; P:sensory perception of mechanical stimulus; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR GO; GO:0060083; P:smooth muscle contraction involved in micturition; ISO:RGD.
DR GO; GO:0001659; P:temperature homeostasis; ISO:RGD.
DR GO; GO:0050955; P:thermoception; ISO:RGD.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISO:RGD.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR024862; TRPV.
DR InterPro; IPR024863; TRPV1.
DR InterPro; IPR008347; TrpV1-4.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR PANTHER; PTHR10582:SF17; PTHR10582:SF17; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01768; TRPVRECEPTOR.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; ATP-binding; Calcium;
KW Calcium channel; Calcium transport; Calmodulin-binding; Cell membrane;
KW Cell projection; Glycoprotein; Ion channel; Ion transport; Lipid-binding;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..838
FT /note="Transient receptor potential cation channel
FT subfamily V member 1"
FT /id="PRO_0000215341"
FT TOPO_DOM 1..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TOPO_DOM 454..471
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TRANSMEM 472..497
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TOPO_DOM 498..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TOPO_DOM 532..535
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TOPO_DOM 557..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TRANSMEM 572..599
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TOPO_DOM 600..626
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT INTRAMEM 627..649
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826"
FT TRANSMEM 658..686
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT TOPO_DOM 687..838
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24305160,
FT ECO:0000269|PubMed:27281200"
FT REPEAT 110..152
FT /note="ANK 1"
FT REPEAT 153..199
FT /note="ANK 2"
FT REPEAT 200..246
FT /note="ANK 3"
FT REPEAT 247..282
FT /note="ANK 4"
FT REPEAT 283..331
FT /note="ANK 5"
FT REPEAT 332..358
FT /note="ANK 6"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..712
FT /note="AD"
FT REGION 767..801
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000269|PubMed:23109716"
FT REGION 777..792
FT /note="Required for PIP2-mediated channel inhibition"
FT MOTIF 643..646
FT /note="Selectivity filter"
FT /evidence="ECO:0000305|PubMed:10931826"
FT COMPBIAS 86..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2PNN"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2PNN"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN"
FT BINDING 199..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2NYJ, ECO:0007744|PDB:2PNN"
FT BINDING 210..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:2PNN"
FT BINDING 511..512
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:27281200,
FT ECO:0007744|PDB:5IRX"
FT BINDING 550
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:27281200,
FT ECO:0007744|PDB:5IRX"
FT BINDING 557
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:27281200,
FT ECO:0007744|PDB:5IRX"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT MOD_RES 116
FT /note="Phosphoserine; by PKA and PKD"
FT /evidence="ECO:0000269|PubMed:12194871,
FT ECO:0000269|PubMed:15471852"
FT MOD_RES 144
FT /note="Phosphothreonine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:12194871"
FT MOD_RES 370
FT /note="Phosphothreonine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:12194871"
FT MOD_RES 502
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000269|PubMed:11884385,
FT ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912"
FT MOD_RES 704
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14630912"
FT MOD_RES 774
FT /note="Phosphoserine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:12194871"
FT MOD_RES 800
FT /note="Phosphoserine; by PKC/PRKCE and PKC/PRKCZ"
FT /evidence="ECO:0000269|PubMed:11884385"
FT MOD_RES 820
FT /note="Phosphoserine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:12194871"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11683872"
FT VAR_SEQ 1..307
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10644739"
FT /id="VSP_013431"
FT VAR_SEQ 348..407
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10644739,
FT ECO:0000303|PubMed:11578842"
FT /id="VSP_013432"
FT MUTAGEN 114
FT /note="R->E: Abolishes capsaicin-evoked current and binding
FT to resiniferatoxin."
FT /evidence="ECO:0000269|PubMed:12228246"
FT MUTAGEN 114
FT /note="Missing: Abolishes sensitivity to acid."
FT /evidence="ECO:0000269|PubMed:12228246"
FT MUTAGEN 115
FT /note="R->D: Abolishes capsaicin-evoked current and binding
FT to resiniferatoxin."
FT /evidence="ECO:0000269|PubMed:12228246"
FT MUTAGEN 116
FT /note="S->A: Abolishes phosphorylation by PKCM and enhances
FT channel response to capsaicin by PKCM."
FT /evidence="ECO:0000269|PubMed:15471852"
FT MUTAGEN 155
FT /note="K->A: Abolishes ATP binding. Abolishes CALM binding.
FT Impairs normal desensitization by repeated exposure to
FT capsaicin."
FT /evidence="ECO:0000269|PubMed:17582331,
FT ECO:0000269|PubMed:23109716"
FT MUTAGEN 160
FT /note="K->A: Abolishes ATP binding. Abolishes CALM
FT binding."
FT /evidence="ECO:0000269|PubMed:17582331"
FT MUTAGEN 199
FT /note="Y->A: Strongly reduces affinity for ATP; when
FT associated with A-202."
FT /evidence="ECO:0000269|PubMed:17582331"
FT MUTAGEN 202
FT /note="Q->A: Strongly reduces affinity for ATP; when
FT associated with A-199."
FT /evidence="ECO:0000269|PubMed:17582331"
FT MUTAGEN 502
FT /note="S->A: Largely reduces PMA enhancement of capsaicin-
FT evoked currents, but no effect on direct activation by PMA.
FT Loss of activation by capsaicin and loss of vanilloid
FT binding; when associated with I-704."
FT /evidence="ECO:0000269|PubMed:11884385,
FT ECO:0000269|PubMed:14523239, ECO:0000269|PubMed:14630912"
FT MUTAGEN 511
FT /note="Y->A: Loss of sensitivity to capsaicin."
FT /evidence="ECO:0000269|PubMed:14996838"
FT MUTAGEN 547
FT /note="M->L: Reduces binding to resiniferatoxin."
FT /evidence="ECO:0000269|PubMed:14996838"
FT MUTAGEN 550
FT /note="T->I: Reduces sensitivity to capsaicin 10-fold; no
FT effect on sensitivity to resiniferatoxin. Reduces binding
FT to resiniferatoxin."
FT /evidence="ECO:0000269|PubMed:14996838"
FT MUTAGEN 636
FT /note="E->K: Abolishes channel activity. Restored channel
FT activity; when associated with E-639."
FT /evidence="ECO:0000269|PubMed:10931826"
FT MUTAGEN 636
FT /note="E->Q: Slight modification of pore attributes."
FT /evidence="ECO:0000269|PubMed:10931826"
FT MUTAGEN 639
FT /note="K->E: Restored channel activity; when associated
FT with K-636."
FT /evidence="ECO:0000269|PubMed:10931826"
FT MUTAGEN 644
FT /note="M->Y: Slightly modifies channel permeability."
FT /evidence="ECO:0000269|PubMed:10931826"
FT MUTAGEN 646
FT /note="D->N: Strongly reduces the affinity for pore blocker
FT ruthenium red and lowered channel permeability for Mg(2+)."
FT /evidence="ECO:0000269|PubMed:10931826"
FT MUTAGEN 648
FT /note="E->Q: Minor modification of pore attributes."
FT /evidence="ECO:0000269|PubMed:10931826"
FT MUTAGEN 651
FT /note="E->Q: Minor modification of pore attributes."
FT /evidence="ECO:0000269|PubMed:10931826"
FT MUTAGEN 704
FT /note="T->A: No effect on PMA-induced enhancement of
FT capsaicin-evoked currents but reduces direct activation by
FT PMA."
FT /evidence="ECO:0000269|PubMed:14523239,
FT ECO:0000269|PubMed:14630912"
FT MUTAGEN 704
FT /note="T->I: Loss of activation by capsaicin and loss of
FT vanilloid binding; when associated with A-502."
FT /evidence="ECO:0000269|PubMed:14523239,
FT ECO:0000269|PubMed:14630912"
FT MUTAGEN 761
FT /note="E->K,Q: Abolishes capsaiin-evoked current and
FT binding to resiniferatoxin."
FT /evidence="ECO:0000269|PubMed:12228246"
FT MUTAGEN 761
FT /note="Missing: Abolishes sensitivity to acid."
FT /evidence="ECO:0000269|PubMed:12228246"
FT MUTAGEN 785
FT /note="R->Q: Strongly reduces CALM-binding and abolishes
FT PLC-mediated channel activity; when associated with Q-788."
FT /evidence="ECO:0000269|PubMed:12764195,
FT ECO:0000269|PubMed:23109716"
FT MUTAGEN 787
FT /note="W->R: Reduces CALM-binding. Reduces desensitization
FT by repeated exposure to capsaicin."
FT /evidence="ECO:0000269|PubMed:23109716"
FT MUTAGEN 788
FT /note="K->Q: Strongly reduces CALM-binding and abolishes
FT PLC-mediated channel activity; when associated with Q-785
FT or Q-797."
FT /evidence="ECO:0000269|PubMed:12764195,
FT ECO:0000269|PubMed:23109716"
FT MUTAGEN 797
FT /note="R->Q: Abolishes PLC-mediated channel activity; when
FT associated with Q-788."
FT /evidence="ECO:0000269|PubMed:12764195"
FT MUTAGEN 800
FT /note="S->A: Largely reduces direct activation of by PMA
FT and PMA-induced currents; no effect on receptor kinase-
FT induced currents."
FT /evidence="ECO:0000269|PubMed:11884385,
FT ECO:0000269|PubMed:12764195, ECO:0000269|PubMed:14523239"
FT CONFLICT 18
FT /note="E -> D (in Ref. 3; BAA94307)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="V -> A (in Ref. 4; AAK83151)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="R -> G (in Ref. 3; BAA94306)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="G -> W (in Ref. 3; BAA94306)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="P -> Q (in Ref. 3; BAA94307)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="V -> I (in Ref. 4; AAK83151)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="K -> Q (in Ref. 3; BAA94306)"
FT /evidence="ECO:0000305"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:7LP9"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7L2W"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 299..319
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:7LPC"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:2NYJ"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 367..373
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:5IS0"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:7LP9"
FT HELIX 395..400
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:7MZ5"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 416..453
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 469..499
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 501..504
FT /evidence="ECO:0007829|PDB:3J9J"
FT HELIX 505..508
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 511..531
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 537..551
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 552..556
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 560..598
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 627..629
FT /evidence="ECO:0007829|PDB:5IRX"
FT HELIX 630..638
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 639..643
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:5IS0"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:7L2L"
FT HELIX 656..669
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 673..688
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 690..711
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 713..715
FT /evidence="ECO:0007829|PDB:7L2H"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:7LP9"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:7MZ5"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:7L2H"
FT STRAND 732..734
FT /evidence="ECO:0007829|PDB:7L2P"
FT STRAND 736..738
FT /evidence="ECO:0007829|PDB:7L2H"
FT STRAND 742..747
FT /evidence="ECO:0007829|PDB:7L2P"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:7LPC"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:7L2P"
FT HELIX 788..792
FT /evidence="ECO:0007829|PDB:3SUI"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:3SUI"
SQ 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
