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

 TRPV1_CANLF             Reviewed;         840 AA.
Q697L1;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 1.
23-MAY-2018, entry version 102.
RecName: Full=Transient receptor potential cation channel subfamily V member 1;
Short=TrpV1;
AltName: Full=Osm-9-like TRP channel 1;
Short=OTRPC1;
AltName: Full=Vanilloid receptor 1;
Name=TRPV1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Phelps P.T., Anthes J.C., Correll C.C.;
"Cloning and functional characterization of dog TRPV1.";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000250|UniProtKB:O35433}.
-!- 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. 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 (By similarity). The Scolopendra mutilans RhTx toxin
potentiates the heat activation pathway mediated by this channel
by binding to the charge-rich outer pore region (in an activated
state) (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q704Y3}.
-!- SUBUNIT: Interacts with PIRT (By similarity). Homotetramer. May
also form a heteromeric channel with TRPV3. Interacts with CALM,
PRKCM and CSK. Interacts with PRKCG and NTRK1, probably by forming
a trimeric complex (By similarity). Interacts with the Scolopendra
mutilans RhTx toxin (By similarity). Interacts with TMEM100 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:O35433,
ECO:0000250|UniProtKB:Q704Y3}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane
protein {ECO:0000250|UniProtKB:O35433}. Cell projection, dendritic
spine membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane
protein {ECO:0000250|UniProtKB:O35433}. Cell membrane
{ECO:0000250|UniProtKB:O35433}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:O35433}. Note=Mostly, but not exclusively
expressed in postsynaptic dendritic spines.
{ECO:0000250|UniProtKB:O35433}.
-!- DOMAIN: The association domain (AD) is necessary for self-
association. {ECO:0000250}.
-!- PTM: Phosphorylation by PKA reverses capsaicin-induced
dephosphorylation at multiple sites. Phosphorylation by CAMKII
seems to regulate binding to vanilloids. Phosphorylated and
modulated by PRKCE, PRKCM and probably PRKCZ. Dephosphorylation by
calcineurin seems to lead to receptor desensitization and
phosphorylation by CAMKII recovers activity.
{ECO:0000250|UniProtKB:O35433}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
TrpV subfamily. TRPV1 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY568758; AAT71314.1; -; mRNA.
RefSeq; NP_001003970.1; NM_001003970.1.
UniGene; Cfa.15820; -.
ProteinModelPortal; Q697L1; -.
SMR; Q697L1; -.
STRING; 9615.ENSCAFP00000028568; -.
ChEMBL; CHEMBL5254; -.
PaxDb; Q697L1; -.
PRIDE; Q697L1; -.
GeneID; 445457; -.
KEGG; cfa:445457; -.
CTD; 7442; -.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
HOGENOM; HOG000234630; -.
HOVERGEN; HBG054085; -.
InParanoid; Q697L1; -.
KO; K05222; -.
PRO; PR:Q697L1; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; ISS:UniProtKB.
GO; GO:0005230; F:extracellular ligand-gated ion channel activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
GO; GO:0071318; P:cellular response to ATP; ISS:UniProtKB.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO; GO:1901594; P:response to capsazepine; ISS:UniProtKB.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
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.
2: Evidence at transcript level;
ANK repeat; ATP-binding; Calcium; Calcium channel; Calcium transport;
Calmodulin-binding; Cell junction; Cell membrane; Cell projection;
Complete proteome; Glycoprotein; Ion channel; Ion transport; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein;
Postsynaptic cell membrane; Reference proteome; Repeat; Synapse;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 840 Transient receptor potential cation
channel subfamily V member 1.
/FTId=PRO_0000215336.
TOPO_DOM 1 433 Cytoplasmic.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 434 454 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 455 472 Extracellular.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 473 498 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 499 511 Cytoplasmic.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 512 532 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 533 536 Extracellular.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 537 557 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 558 572 Cytoplasmic.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 573 600 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 601 659 Extracellular.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 660 688 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 689 840 Cytoplasmic.
{ECO:0000250|UniProtKB:O35433}.
REPEAT 111 153 ANK 1.
REPEAT 154 200 ANK 2.
REPEAT 201 247 ANK 3.
REPEAT 248 283 ANK 4.
REPEAT 284 332 ANK 5.
REPEAT 333 359 ANK 6.
NP_BIND 200 203 ATP. {ECO:0000250|UniProtKB:O35433}.
NP_BIND 211 212 ATP. {ECO:0000250|UniProtKB:O35433}.
REGION 115 116 Important for channel activation by
agonists and heat.
{ECO:0000250|UniProtKB:O35433}.
REGION 686 714 AD. {ECO:0000250}.
REGION 769 803 Interaction with calmodulin.
{ECO:0000250|UniProtKB:O35433}.
REGION 779 794 Required for PIP2-mediated channel
inhibition. {ECO:0000250}.
MOTIF 645 648 Selectivity filter.
{ECO:0000250|UniProtKB:O35433}.
METAL 648 648 Calcium; shared with neighboring
subunits. {ECO:0000250|UniProtKB:Q9R186}.
BINDING 116 116 ATP. {ECO:0000250|UniProtKB:O35433}.
BINDING 156 156 ATP. {ECO:0000250|UniProtKB:O35433}.
BINDING 161 161 ATP. {ECO:0000250|UniProtKB:O35433}.
BINDING 165 165 ATP. {ECO:0000250|UniProtKB:O35433}.
BINDING 513 513 Agonist. {ECO:0000250|UniProtKB:O35433}.
BINDING 551 551 Agonist. {ECO:0000250|UniProtKB:O35433}.
SITE 558 558 Important for agonist binding.
{ECO:0000250|UniProtKB:O35433}.
MOD_RES 371 371 Phosphothreonine; by PKA; in vitro.
{ECO:0000250|UniProtKB:O35433}.
MOD_RES 503 503 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:O35433}.
MOD_RES 706 706 Phosphothreonine.
{ECO:0000250|UniProtKB:O35433}.
MOD_RES 776 776 Phosphoserine.
{ECO:0000250|UniProtKB:O35433}.
MOD_RES 802 802 Phosphoserine; by PKC/PRKCE and
PKC/PRKCZ.
{ECO:0000250|UniProtKB:O35433}.
MOD_RES 822 822 Phosphoserine.
{ECO:0000250|UniProtKB:O35433}.
CARBOHYD 605 605 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
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


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