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Database: UniProt
Entry: TRPV1_MOUSE
LinkDB: TRPV1_MOUSE
Original site: 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   05-JUL-2017, entry version 126.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP   SUBCELLULAR 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,
RT   and 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
RP   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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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   ENZYME 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 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
CC       stimuli (PubMed:15194687, PubMed:15489017). Seems to mediate
CC       proton influx and may be involved in intracellular acidosis in
CC       nociceptive neurons. Involved in mediation of inflammatory pain
CC       and hyperalgesia (PubMed:10764638). Sensitized by a
CC       phosphatidylinositol second messenger system activated by receptor
CC       tyrosine kinases, which involves PKC isozymes and PCL. Activation
CC       by vanilloids, like capsaicin, and temperatures higher than 42
CC       degrees Celsius, exhibits a time- and Ca(2+)-dependent outward
CC       rectification, followed by a long-lasting refractory state. Mild
CC       extracellular acidic pH (6.5) potentiates channel activation by
CC       noxious heat and vanilloids, whereas acidic conditions (pH <6)
CC       directly activate the channel. Can be activated by endogenous
CC       compounds, including 12-hydroperoxytetraenoic acid and bradykinin.
CC       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   -!- ENZYME REGULATION: The channel is sensitized by ATP binding.
CC       Repeated stimulation with capsaicin gives rise to progressively
CC       smaller responses, due to desensitization. This desensitization is
CC       triggered by the influx of calcium ions and is inhibited by
CC       elevated ATP levels. Ca(2+) and CALM displace ATP from its binding
CC       site and trigger a conformation change that leads to a closed,
CC       desensitized channel. The double-knot toxin (DkTx) from the
CC       Chinese earth tiger tarantula activates the channel and traps it
CC       in an open conformation (By similarity). Channel activity is
CC       activated via the interaction with PIRT and phosphatidylinositol
CC       4,5-bisphosphate (PIP2). Both PIRT and PIP2 are required to
CC       activate channel activity. Intracellular PIP2 inhibits
CC       desensitization (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. May also form a heteromeric channel with
CC       TRPV3 (By similarity). Interacts with CALM, PRKCM and CSK (By
CC       similarity). Interacts with PRKCG and NTRK1, probably by forming a
CC       trimeric complex (By similarity). Interacts with PIRT
CC       (PubMed:18455988). Interacts with TMEM100 (PubMed:25640077).
CC       {ECO:0000250|UniProtKB:O35433, ECO:0000250|UniProtKB:Q8NER1,
CC       ECO:0000269|PubMed:18455988, ECO:0000269|PubMed:25640077}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:O35433}. Cell projection, dendritic
CC       spine membrane {ECO:0000250|UniProtKB:O35433}; Multi-pass membrane
CC       protein {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
CC       protein level). Detected in dorsal root ganglia.
CC       {ECO:0000269|PubMed:10764638}.
CC   -!- DOMAIN: The association domain (AD) is necessary for self-
CC       association. {ECO:0000250}.
CC   -!- PTM: Phosphorylation by PKA reverses capsaicin-induced
CC       dephosphorylation at multiple sites probably including Ser-117 as
CC       a major phosphorylation site. Phosphorylation by CAMKII seems to
CC       regulate binding to vanilloids. Phosphorylated and modulated by
CC       PRKCE, PRKCM and probably PRKCZ. Dephosphorylation by calcineurin
CC       seems to lead to receptor desensitization and phosphorylation by
CC       CAMKII recovers activity. {ECO:0000250|UniProtKB:O35433}.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but lack
CC       behavorial and physiological responses to capsaicin and show
CC       impaired responses to noxious heat stimuli. Their dorsal root
CC       ganglion neurons do not display calcium channel activation in
CC       response to capsaicin or resiniferatoxin. Likewise, their dorsal
CC       root ganglion neurons do not display calcium channel activitation
CC       in response to low extracellular pH.
CC       {ECO:0000269|PubMed:10764638}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       TrpV 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};
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   UniGene; Mm.447485; -.
DR   ProteinModelPortal; Q704Y3; -.
DR   SMR; Q704Y3; -.
DR   BioGrid; 228724; 4.
DR   DIP; DIP-59791N; -.
DR   STRING; 10090.ENSMUSP00000099585; -.
DR   BindingDB; Q704Y3; -.
DR   ChEMBL; CHEMBL1781864; -.
DR   GuidetoPHARMACOLOGY; 507; -.
DR   iPTMnet; Q704Y3; -.
DR   PhosphoSitePlus; Q704Y3; -.
DR   PaxDb; Q704Y3; -.
DR   PRIDE; Q704Y3; -.
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   eggNOG; KOG3676; Eukaryota.
DR   eggNOG; ENOG4110DG4; LUCA.
DR   GeneTree; ENSGT00550000074425; -.
DR   HOGENOM; HOG000234630; -.
DR   HOVERGEN; HBG054085; -.
DR   InParanoid; Q704Y3; -.
DR   KO; K05222; -.
DR   OMA; VEEVNWN; -.
DR   OrthoDB; EOG091G01LY; -.
DR   PhylomeDB; Q704Y3; -.
DR   TreeFam; TF314711; -.
DR   Reactome; R-MMU-3295583; TRP channels.
DR   PRO; PR:Q704Y3; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000005952; -.
DR   ExpressionAtlas; Q704Y3; baseline and differential.
DR   Genevisible; Q704Y3; MM.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
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:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0005216; F:ion channel activity; IDA: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: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; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0090212; P:negative regulation of establishment of blood-brain barrier; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR   GO; GO:0002790; P:peptide secretion; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0060454; P:positive regulation of gastric acid secretion; IEA:Ensembl.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
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   CDD; cd00204; ANK; 1.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR004729; TRP_channel.
DR   InterPro; IPR024862; TRPV.
DR   InterPro; IPR008347; TRPV1-4_channel.
DR   InterPro; IPR024863; TRPV1_channel.
DR   PANTHER; PTHR10582; PTHR10582; 1.
DR   PANTHER; PTHR10582:SF38; PTHR10582:SF38; 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   TIGRFAMs; TIGR00870; trp; 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;
KW   Calcium channel; Calcium transport; Calmodulin-binding; Cell junction;
KW   Cell membrane; Cell projection; Complete proteome; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Postsynaptic cell membrane;
KW   Reference proteome; Repeat; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    839       Transient receptor potential cation
FT                                channel subfamily V member 1.
FT                                /FTId=PRO_0000215339.
FT   TOPO_DOM      1    433       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   TRANSMEM    434    454       Helical. {ECO:0000250|UniProtKB:O35433}.
FT   TOPO_DOM    455    472       Extracellular.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   TRANSMEM    473    498       Helical. {ECO:0000250|UniProtKB:O35433}.
FT   TOPO_DOM    499    511       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   TRANSMEM    512    532       Helical. {ECO:0000250|UniProtKB:O35433}.
FT   TOPO_DOM    533    536       Extracellular.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   TRANSMEM    537    557       Helical. {ECO:0000250|UniProtKB:O35433}.
FT   TOPO_DOM    558    572       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   TRANSMEM    573    600       Helical. {ECO:0000250|UniProtKB:O35433}.
FT   TOPO_DOM    601    658       Extracellular.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   TRANSMEM    659    687       Helical. {ECO:0000250|UniProtKB:O35433}.
FT   TOPO_DOM    688    839       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   REPEAT      111    153       ANK 1.
FT   REPEAT      154    200       ANK 2.
FT   REPEAT      201    247       ANK 3.
FT   REPEAT      248    283       ANK 4.
FT   REPEAT      284    332       ANK 5.
FT   REPEAT      333    359       ANK 6.
FT   NP_BIND     200    203       ATP. {ECO:0000250|UniProtKB:O35433}.
FT   NP_BIND     211    212       ATP. {ECO:0000250|UniProtKB:O35433}.
FT   REGION      115    116       Important for channel activation by
FT                                agonists and heat.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   REGION      685    713       AD. {ECO:0000250}.
FT   REGION      768    802       Interaction with calmodulin.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   REGION      778    793       Required for PIP2-mediated channel
FT                                inhibition. {ECO:0000250}.
FT   MOTIF       644    647       Selectivity filter.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   METAL       647    647       Calcium; shared with neighboring
FT                                subunits. {ECO:0000250|UniProtKB:Q9R186}.
FT   BINDING     116    116       ATP. {ECO:0000250|UniProtKB:O35433}.
FT   BINDING     156    156       ATP. {ECO:0000250|UniProtKB:O35433}.
FT   BINDING     161    161       ATP. {ECO:0000250|UniProtKB:O35433}.
FT   BINDING     165    165       ATP. {ECO:0000250|UniProtKB:O35433}.
FT   BINDING     513    513       Agonist. {ECO:0000250|UniProtKB:O35433}.
FT   BINDING     551    551       Agonist. {ECO:0000250|UniProtKB:O35433}.
FT   SITE        558    558       Important for agonist binding.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   MOD_RES     117    117       Phosphoserine; by PKA and PKD.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   MOD_RES     145    145       Phosphothreonine; by PKA; in vitro.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   MOD_RES     371    371       Phosphothreonine; by PKA; in vitro.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   MOD_RES     503    503       Phosphoserine; by PKC/PRKCE.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   MOD_RES     705    705       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   MOD_RES     775    775       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   MOD_RES     801    801       Phosphoserine; by PKC/PRKCE and
FT                                PKC/PRKCZ.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   MOD_RES     821    821       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35433}.
FT   CARBOHYD    605    605       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000250}.
FT   VAR_SEQ     399    408       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15194687}.
FT                                /FTId=VSP_013430.
FT   CONFLICT    734    734       D -> E (in Ref. 4; AAS01605).
FT                                {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
//
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