TRPV1_CANLF
ID TRPV1_CANLF Reviewed; 840 AA.
AC Q697L1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Phelps P.T., Anthes J.C., Correll C.C.;
RT "Cloning and functional characterization of dog TRPV1.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:O35433}.
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. The channel is
CC sensitized by ATP binding. Repeated stimulation with capsaicin gives
CC rise to progressively smaller responses, due to desensitization. This
CC desensitization is triggered by the influx of calcium ions and is
CC inhibited by elevated ATP levels. Ca(2+) and CALM displace ATP from its
CC binding site and trigger a conformation change that leads to a closed,
CC desensitized channel. Intracellular PIP2 inhibits desensitization. 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) (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q704Y3}.
CC -!- SUBUNIT: Interacts with PIRT (By similarity). Homotetramer. May also
CC form a heteromeric channel with TRPV3. Interacts with CALM, PRKCM and
CC CSK. Interacts with PRKCG and NTRK1, probably by forming a trimeric
CC complex (By similarity). Interacts with the Scolopendra mutilans RhTx
CC toxin (By similarity). Interacts with TMEM100 (By similarity).
CC Interacts with PACS2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O35433, ECO:0000250|UniProtKB:Q704Y3,
CC ECO:0000250|UniProtKB:Q8NER1}.
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 -!- 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. Phosphorylation by CAMKII seems to
CC regulate binding to vanilloids. Phosphorylated and modulated by PRKCE,
CC PRKCM and probably PRKCZ. Dephosphorylation by calcineurin seems to
CC lead to receptor desensitization and phosphorylation by CAMKII recovers
CC activity. {ECO:0000250|UniProtKB:O35433}.
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; AY568758; AAT71314.1; -; mRNA.
DR RefSeq; NP_001003970.1; NM_001003970.1.
DR AlphaFoldDB; Q697L1; -.
DR SMR; Q697L1; -.
DR STRING; 9612.ENSCAFP00000028568; -.
DR ChEMBL; CHEMBL5254; -.
DR PaxDb; Q697L1; -.
DR Ensembl; ENSCAFT00030019193; ENSCAFP00030016743; ENSCAFG00030010048.
DR Ensembl; ENSCAFT00040007666; ENSCAFP00040006693; ENSCAFG00040003970.
DR GeneID; 445457; -.
DR KEGG; cfa:445457; -.
DR CTD; 7442; -.
DR eggNOG; KOG3676; Eukaryota.
DR InParanoid; Q697L1; -.
DR OrthoDB; 693004at2759; -.
DR PRO; PR:Q697L1; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
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:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0097603; F:temperature-gated ion channel activity; IEA:Ensembl.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl.
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: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:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0050968; P:detection of chemical stimulus involved in sensory perception of pain; IEA:Ensembl.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; IEA:Ensembl.
DR GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
DR GO; GO:0001660; P:fever generation; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0002790; P:peptide secretion; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:1901594; P:response to capsazepine; ISS:UniProtKB.
DR GO; GO:0050954; P:sensory perception of mechanical stimulus; IEA:Ensembl.
DR GO; GO:0060083; P:smooth muscle contraction involved in micturition; IEA:Ensembl.
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 2: Evidence at transcript level;
KW ANK repeat; ATP-binding; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Cell membrane; Cell projection; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..840
FT /note="Transient receptor potential cation channel
FT subfamily V member 1"
FT /id="PRO_0000215336"
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..659
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 660..688
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 689..840
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..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..714
FT /note="AD"
FT /evidence="ECO:0000250"
FT REGION 769..803
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT REGION 779..794
FT /note="Required for PIP2-mediated channel inhibition"
FT /evidence="ECO:0000250"
FT MOTIF 645..648
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:O35433"
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 648
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 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 706
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 802
FT /note="Phosphoserine; by PKC/PRKCE and PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 840 AA; 95237 MW; 5F5D5A366DC46459 CRC64;
MKNWGSSDSG GSEDPPQEDS CLDPLDGDPN SRPVPAKPHI FPTAKSRSRL FGKCDSEEAS
MDCSYEEGQL ASCPAITVSP VVMIPKHEDG PTCARQPSQD SVTAGSEKSL KLYDRRKIFE
AVAQNNCEEL QSLLLFLQKS KKHLMDSEFK DPETGKTCLL KAMLNLHDGQ NDTIPLLLEI
ARQTDSLKEL VNASYTDSYY KGQTALHIAI ERRNMALVTL LVENGADVQA AANGDFFKKT
KGRPGFYFGE LPLSLAACTN QLGIVKFLLQ NSWQPADISA RDSVGNTVLH ALVEVADNTA
DNTKFVTSMY NEILILGAKL HPTLKLEGLT NKKGLTPLAL AARSGKIGVL AYILQREIQE
PECRHLSRKF TEWAYGPVHS SLYDLSCIDT CEKNSVLEVI AYSSSETPNR HDMLLVEPLN
RLLQDKWDRF VKRIFYFNFF IYCLYMIIFT TAAYYRPVDG LPPYKLKHTV GDYFRVTGEI
LSVLGGVYFF FRGIQYFLQR RPSLKTLFVD SYSEMLFFVQ SLFMLGTVVL YFCHHKEYVA
SMVFSLAMGW TNMLYYTRGF QQMGIYAVMI EKMILRDLCR FMFVYLVFLF GFSTAVVTLI
EDGKNNSVPT ESTLHRWRGP GCRPPDSSYN SLYSTCLELF KFTIGMGDLE FTENYDFKAV
FIILLLAYVI LTYILLLNML IALMGETVNK IAQESKNIWK LQRAITILDT EKSFLKCMRK
AFRSGKLLQV GYTPDGKDDY RWCFRVDEVN WTTWNTNVGI INEDPGNCEG IKRTLSFSLR
SGRVSGRNWK NFSLVPLLRD ASTRERHPAQ PEEVHLRHFA GSLKPEDAEI FKDPVGLGEK
