TRPV1_MOUSE
ID TRPV1_MOUSE Reviewed; 839 AA.
AC Q704Y3; Q5SSE1; Q5SSE2; Q5SSE4; Q5WPV5; Q68SW0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 1;
DE Short=TrpV1;
DE AltName: Full=Osm-9-like TRP channel 1;
DE Short=OTRPC1;
DE AltName: Full=Vanilloid receptor 1;
GN Name=Trpv1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=15194687; DOI=10.1074/jbc.m404164200;
RA Hu H.Z., Gu Q., Wang C., Colton C.K., Tang J., Kinoshita-Kawada M.,
RA Lee L.Y., Wood J.D., Zhu M.X.;
RT "2-aminoethoxydiphenyl borate is a common activator of TRPV1, TRPV2, and
RT TRPV3.";
RL J. Biol. Chem. 279:35741-35748(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RA McIntyre P.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=DBA;
RA Ogawa S., Sugiura A., Pang C., Shinjo K.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Swiss Webster;
RX PubMed=15489017; DOI=10.1016/j.neulet.2004.07.058;
RA Correll C.C., Phelps P.T., Greenfeder S.;
RT "Cloning and pharmacological characterization of mouse TRPV1.";
RL Neurosci. Lett. 370:55-60(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10764638; DOI=10.1126/science.288.5464.306;
RA Caterina M.J., Leffler A., Malmberg A.B., Martin W.J., Trafton J.,
RA Petersen-Zeitz K.R., Koltzenburg M., Basbaum A.I., Julius D.;
RT "Impaired nociception and pain sensation in mice lacking the capsaicin
RT receptor.";
RL Science 288:306-313(2000).
RN [7]
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIRT.
RX PubMed=18455988; DOI=10.1016/j.cell.2008.02.053;
RA Kim A.Y., Tang Z., Liu Q., Patel K.N., Maag D., Geng Y., Dong X.;
RT "Pirt, a phosphoinositide-binding protein, functions as a regulatory
RT subunit of TRPV1.";
RL Cell 133:475-485(2008).
RN [8]
RP INTERACTION WITH THE SCOLOPENDRA MUTILANS RHTX TOXIN, SUBUNIT, AND
RP MUTAGENESIS OF LEU-461; ASP-602; TYR-632 AND THR-634.
RX PubMed=26420335; DOI=10.1038/ncomms9297;
RA Yang S., Yang F., Wei N., Hong J., Li B., Luo L., Rong M.,
RA Yarov-Yarovoy V., Zheng J., Wang K., Lai R.;
RT "A pain-inducing centipede toxin targets the heat activation machinery of
RT nociceptor TRPV1.";
RL Nat. Commun. 6:8297-8297(2015).
RN [9]
RP INTERACTION WITH TMEM100.
RX PubMed=25640077; DOI=10.1016/j.neuron.2014.12.065;
RA Weng H.J., Patel K.N., Jeske N.A., Bierbower S.M., Zou W., Tiwari V.,
RA Zheng Q., Tang Z., Mo G.C., Wang Y., Geng Y., Zhang J., Guan Y.,
RA Akopian A.N., Dong X.;
RT "Tmem100 Is a regulator of TRPA1-TRPV1 complex and contributes to
RT persistent pain.";
RL Neuron 85:833-846(2015).
CC -!- FUNCTION: Ligand-activated non-selective calcium permeant cation
CC channel involved in detection of noxious chemical and thermal stimuli
CC (PubMed:15194687, PubMed:15489017). Seems to mediate proton influx and
CC may be involved in intracellular acidosis in nociceptive neurons.
CC Involved in mediation of inflammatory pain and hyperalgesia
CC (PubMed:10764638). 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 (By similarity). {ECO:0000250|UniProtKB:O35433,
CC ECO:0000269|PubMed:10764638, ECO:0000269|PubMed:15194687,
CC ECO:0000269|PubMed:15489017}.
CC -!- ACTIVITY REGULATION: The channel is sensitized by ATP binding. Repeated
CC stimulation with capsaicin gives rise to progressively smaller
CC responses, due to desensitization. This desensitization is triggered by
CC the influx of calcium ions and is inhibited by elevated ATP levels.
CC Ca(2+) and CALM displace ATP from its binding site and trigger a
CC conformation change that leads to a closed, desensitized channel. The
CC double-knot toxin (DkTx) from the Chinese earth tiger tarantula
CC activates the channel and traps it in an open conformation (By
CC similarity). 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) (PubMed:26420335).
CC Channel activity is activated via the interaction with PIRT and
CC phosphatidylinositol 4,5-bisphosphate (PIP2). Both PIRT and PIP2 are
CC required to activate channel activity. Intracellular PIP2 inhibits
CC desensitization (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:26420335}.
CC -!- SUBUNIT: Homotetramer. May also form a heteromeric channel with TRPV3
CC (By similarity). Interacts with CALM, PRKCM and CSK (By similarity).
CC Interacts with PRKCG and NTRK1, probably by forming a trimeric complex
CC (By similarity). Interacts with PIRT (PubMed:18455988). Interacts with
CC the Scolopendra mutilans RhTx toxin (PubMed:26420335). Interacts with
CC TMEM100 (PubMed:25640077). Interacts with PACS2 (By similarity).
CC {ECO:0000250|UniProtKB:O35433, ECO:0000250|UniProtKB:Q8NER1,
CC ECO:0000269|PubMed:18455988, ECO:0000269|PubMed:25640077,
CC ECO:0000269|PubMed:26420335}.
CC -!- INTERACTION:
CC Q704Y3-1; Q704Y3-1: Trpv1; NbExp=5; IntAct=EBI-15845376, EBI-15845376;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O35433}. Cell projection, dendritic spine
CC membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O35433}. Cell membrane
CC {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O35433}. Note=Mostly, but not exclusively
CC expressed in postsynaptic dendritic spines.
CC {ECO:0000250|UniProtKB:O35433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q704Y3-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q704Y3-2; Sequence=VSP_013430;
CC -!- TISSUE SPECIFICITY: Detected in neurons in the root ganglia (at protein
CC level). Detected in dorsal root ganglia. {ECO:0000269|PubMed:10764638}.
CC -!- DOMAIN: The association domain (AD) is necessary for self-association.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation by PKA reverses capsaicin-induced
CC dephosphorylation at multiple sites probably including Ser-117 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:0000250|UniProtKB:O35433}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but lack behavorial
CC and physiological responses to capsaicin and show impaired responses to
CC noxious heat stimuli. Their dorsal root ganglion neurons do not display
CC calcium channel activation in response to capsaicin or resiniferatoxin.
CC Likewise, their dorsal root ganglion neurons do not display calcium
CC channel activitation in response to low extracellular pH.
CC {ECO:0000269|PubMed:10764638}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI24577.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI24579.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI24580.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY452083; AAS15574.1; -; mRNA.
DR EMBL; AY452084; AAS15575.1; -; mRNA.
DR EMBL; AJ620495; CAF05661.1; -; mRNA.
DR EMBL; AB180097; BAD20301.1; -; mRNA.
DR EMBL; AY445519; AAS01605.1; -; mRNA.
DR EMBL; AL663116; CAI24577.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL663116; CAI24578.1; -; Genomic_DNA.
DR EMBL; AL663116; CAI24579.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL663116; CAI24580.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS25003.1; -. [Q704Y3-1]
DR RefSeq; NP_001001445.1; NM_001001445.2. [Q704Y3-1]
DR AlphaFoldDB; Q704Y3; -.
DR SMR; Q704Y3; -.
DR BioGRID; 228724; 125.
DR DIP; DIP-59791N; -.
DR STRING; 10090.ENSMUSP00000099585; -.
DR BindingDB; Q704Y3; -.
DR ChEMBL; CHEMBL1781864; -.
DR DrugCentral; Q704Y3; -.
DR GuidetoPHARMACOLOGY; 507; -.
DR GlyGen; Q704Y3; 1 site.
DR iPTMnet; Q704Y3; -.
DR PhosphoSitePlus; Q704Y3; -.
DR PaxDb; Q704Y3; -.
DR PRIDE; Q704Y3; -.
DR ProteomicsDB; 298316; -. [Q704Y3-1]
DR ProteomicsDB; 298317; -. [Q704Y3-2]
DR ABCD; Q704Y3; 2 sequenced antibodies.
DR Antibodypedia; 5472; 553 antibodies from 39 providers.
DR DNASU; 193034; -.
DR Ensembl; ENSMUST00000102526; ENSMUSP00000099585; ENSMUSG00000005952. [Q704Y3-1]
DR GeneID; 193034; -.
DR KEGG; mmu:193034; -.
DR UCSC; uc007kah.2; mouse. [Q704Y3-1]
DR UCSC; uc011xyq.2; mouse. [Q704Y3-2]
DR CTD; 7442; -.
DR MGI; MGI:1341787; Trpv1.
DR VEuPathDB; HostDB:ENSMUSG00000005952; -.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000160870; -.
DR HOGENOM; CLU_012795_1_0_1; -.
DR InParanoid; Q704Y3; -.
DR OMA; YQYLHQN; -.
DR PhylomeDB; Q704Y3; -.
DR TreeFam; TF314711; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 193034; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q704Y3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q704Y3; protein.
DR Bgee; ENSMUSG00000005952; Expressed in lumbar dorsal root ganglion and 53 other tissues.
DR ExpressionAtlas; Q704Y3; baseline and differential.
DR Genevisible; Q704Y3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IMP:MGI.
DR GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; ISA:MGI.
DR GO; GO:0008324; F:cation transmembrane transporter activity; ISO:MGI.
DR GO; GO:0017081; F:chloride channel regulator activity; ISO:MGI.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0005230; F:extracellular ligand-gated ion channel activity; ISS: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; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0097603; F:temperature-gated ion channel activity; IDA:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0048266; P:behavioral response to pain; IDA:MGI.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0006812; P:cation transport; ISA:MGI.
DR GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
DR GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; IDA:MGI.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; IDA:MGI.
DR GO; GO:0002024; P:diet induced thermogenesis; IMP:MGI.
DR GO; GO:0001660; P:fever generation; IMP:MGI.
DR GO; GO:0014047; P:glutamate secretion; ISO:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0001774; P:microglial cell activation; ISO:MGI.
DR GO; GO:0090212; P:negative regulation of establishment of blood-brain barrier; ISO:MGI.
DR GO; GO:0010459; P:negative regulation of heart rate; ISO:MGI.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0002790; P:peptide secretion; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0060454; P:positive regulation of gastric acid secretion; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:1901594; P:response to capsazepine; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; IMP:MGI.
DR GO; GO:0048265; P:response to pain; IDA:MGI.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0009268; P:response to pH; IMP:MGI.
DR GO; GO:0050954; P:sensory perception of mechanical stimulus; IMP:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR GO; GO:0060083; P:smooth muscle contraction involved in micturition; IMP:MGI.
DR GO; GO:0001659; P:temperature homeostasis; IMP:MGI.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IMP:MGI.
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 Alternative splicing; ANK repeat; ATP-binding; Calcium; Calcium channel;
KW Calcium transport; Calmodulin-binding; Cell membrane; Cell projection;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..839
FT /note="Transient receptor potential cation channel
FT subfamily V member 1"
FT /id="PRO_0000215339"
FT TOPO_DOM 1..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 455..472
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 473..498
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 499..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 533..536
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 558..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 573..600
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 601..658
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 659..687
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 688..839
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT REPEAT 111..153
FT /note="ANK 1"
FT REPEAT 154..200
FT /note="ANK 2"
FT REPEAT 201..247
FT /note="ANK 3"
FT REPEAT 248..283
FT /note="ANK 4"
FT REPEAT 284..332
FT /note="ANK 5"
FT REPEAT 333..359
FT /note="ANK 6"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..713
FT /note="AD"
FT /evidence="ECO:0000250"
FT REGION 768..802
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT REGION 778..793
FT /note="Required for PIP2-mediated channel inhibition"
FT /evidence="ECO:0000250"
FT REGION 802..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 644..647
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT COMPBIAS 18..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 200..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 211..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 512..513
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 551
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 558
FT /ligand="resiniferatoxin"
FT /ligand_id="ChEBI:CHEBI:8809"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT BINDING 647
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 117
FT /note="Phosphoserine; by PKA and PKD"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 145
FT /note="Phosphothreonine; by PKA; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 371
FT /note="Phosphothreonine; by PKA; in vitro"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 503
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 705
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 801
FT /note="Phosphoserine; by PKC/PRKCE and PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 399..408
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15194687"
FT /id="VSP_013430"
FT MUTAGEN 461
FT /note="L->G: 17-fold less potently activated by the
FT Scolopendra mutilans RhTx toxin."
FT /evidence="ECO:0000269|PubMed:26420335"
FT MUTAGEN 602
FT /note="D->A: 13-fold less potently activated by the
FT Scolopendra mutilans RhTx toxin."
FT /evidence="ECO:0000269|PubMed:26420335"
FT MUTAGEN 632
FT /note="Y->A: 10-fold less potently activated by the
FT Scolopendra mutilans RhTx toxin."
FT /evidence="ECO:0000269|PubMed:26420335"
FT MUTAGEN 634
FT /note="T->A: 8-fold less potently activated by the
FT Scolopendra mutilans RhTx toxin."
FT /evidence="ECO:0000269|PubMed:26420335"
FT CONFLICT 734
FT /note="D -> E (in Ref. 4; AAS01605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 94976 MW; EB50780E9281C2B7 CRC64;
MEKWASLDSD ESEPPAQENS CPDPPDRDPN SKPPPAKPHI FATRSRTRLF GKGDSEEASP
MDCPYEEGGL ASCPIITVSS VVTLQRSVDG PTCLRQTSQD SVSTGVETPP RLYDRRSIFD
AVAQSNCQEL ESLLSFLQKS KKRLTDSEFK DPETGKTCLL KAMLNLHNGQ NDTIALLLDI
ARKTDSLKQF VNASYTDSYY KGQTALHIAI ERRNMALVTL LVENGADVQA AANGDFFKKT
KGRPGFYFGE LPLSLAACTN QLAIVKFLLQ NSWQPADISA RDSVGNTVLH ALVEVADNTA
DNTKFVTNMY NEILILGAKL HPTLKLEELT NKKGLTPLAL AASSGKIGVL AYILQREIHE
PECRHLSRKF TEWAYGPVHS SLYDLSCIDT CEKNSVLEVI AYSSSETPNR HDMLLVEPLN
RLLQDKWDRF VKRIFYFNFF VYCLYMIIFT TAAYYRPVEG LPPYKLNNTV GDYFRVTGEI
LSVSGGVYFF FRGIQYFLQR RPSLKSLFVD SYSEILFFVQ SLFMLVSVVL YFSHRKEYVA
SMVFSLAMGW TNMLYYTRGF QQMGIYAVMI EKMILRDLCR FMFVYLVFLF GFSTAVVTLI
EDGKNNSLPV ESPPHKCRGS ACRPGNSYNS LYSTCLELFK FTIGMGDLEF TENYDFKAVF
IILLLAYVIL TYILLLNMLI ALMGETVNKI AQESKNIWKL QRAITILDTE KSFLKCMRKA
FRSGKLLQVG FTPDGKDDFR WCFRVDEVNW TTWNTNVGII NEDPGNCEGV KRTLSFSLRS
GRVSGRNWKN FALVPLLRDA STRDRHSTQP EEVQLKHYTG SLKPEDAEVF KDSMAPGEK
