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PE2R3_MOUSE
ID   PE2R3_MOUSE             Reviewed;         365 AA.
AC   P30557;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 154.
DE   RecName: Full=Prostaglandin E2 receptor EP3 subtype;
DE            Short=PGE receptor EP3 subtype;
DE            Short=PGE2 receptor EP3 subtype;
DE   AltName: Full=Prostanoid EP3 receptor;
GN   Name=Ptger3; Synonyms=Ptgerep3;
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] (ISOFORM ALPHA), FUNCTION, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=BDF1;
RX   PubMed=1372606; DOI=10.1016/s0021-9258(19)50448-3;
RA   Sugimoto Y., Namba T., Honda A., Hayashi Y., Negishi M., Ichikawa A.,
RA   Narumiya S.;
RT   "Cloning and expression of a cDNA for mouse prostaglandin E receptor EP3
RT   subtype.";
RL   J. Biol. Chem. 267:6463-6466(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=8381413; DOI=10.1016/s0021-9258(18)53832-1;
RA   Sugimoto Y., Negishi M., Hayashi Y., Namba T., Honda A., Watabe A.,
RA   Hirata M., Narumiya S., Ichikawa A.;
RT   "Two isoforms of the EP3 receptor with different carboxyl-terminal domains.
RT   Identical ligand binding properties and different coupling properties with
RT   Gi proteins.";
RL   J. Biol. Chem. 268:2712-2718(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=8223569; DOI=10.1111/j.1432-1033.1993.tb18248.x;
RA   Irie A., Sugimoto Y., Namba T., Harazono A., Honda A., Watabe A.,
RA   Negishi M., Narumiya S., Ichikawa A.;
RT   "Third isoform of the prostaglandin-E-receptor EP3 subtype with different
RT   C-terminal tail coupling to both stimulation and inhibition of adenylate
RT   cyclase.";
RL   Eur. J. Biochem. 217:313-318(1993).
RN   [4]
RP   CHARACTERIZATION (ISOFORMS ALPHA AND BETA), AND FUNCTION.
RX   PubMed=8567630; DOI=10.1074/jbc.271.4.1857;
RA   Hasegawa H., Negishi M., Ichikawa A.;
RT   "Two isoforms of the prostaglandin E receptor EP3 subtype different in
RT   agonist-independent constitutive activity.";
RL   J. Biol. Chem. 271:1857-1860(1996).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=9843913; DOI=10.1152/ajprenal.1998.275.6.f955;
RA   Fleming E.F., Athirakul K., Oliverio M.I., Key M., Goulet J., Koller B.H.,
RA   Coffman T.M.;
RT   "Urinary concentrating function in mice lacking EP3 receptors for
RT   prostaglandin E2.";
RL   Am. J. Physiol. 275:F955-F961(1998).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=9751056; DOI=10.1038/26233;
RA   Ushikubi F., Segi E., Sugimoto Y., Murata T., Matsuoka T., Kobayashi T.,
RA   Hizaki H., Tuboi K., Katsuyama M., Ichikawa A., Tanaka T., Yoshida N.,
RA   Narumiya S.;
RT   "Impaired febrile response in mice lacking the prostaglandin E receptor
RT   subtype EP3.";
RL   Nature 395:281-284(1998).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=10535876; DOI=10.1016/s0016-5085(99)70398-7;
RA   Takeuchi K., Ukawa H., Kato S., Furukawa O., Araki H., Sugimoto Y.,
RA   Ichikawa A., Ushikubi F., Narumiya S.;
RT   "Impaired duodenal bicarbonate secretion and mucosal integrity in mice
RT   lacking prostaglandin E-receptor subtype EP(3).";
RL   Gastroenterology 117:1128-1135(1999).
RN   [8]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11535576; DOI=10.1161/hc3601.094003;
RA   Ma H., Hara A., Xiao C.Y., Okada Y., Takahata O., Nakaya K., Sugimoto Y.,
RA   Ichikawa A., Narumiya S., Ushikubi F.;
RT   "Increased bleeding tendency and decreased susceptibility to
RT   thromboembolism in mice lacking the prostaglandin E receptor subtype
RT   EP(3).";
RL   Circulation 104:1176-1180(2001).
CC   -!- FUNCTION: Receptor for prostaglandin E2 (PGE2) (PubMed:1372606,
CC       PubMed:8381413, PubMed:8223569). Required for normal development of
CC       fever in response to pyrinogens, including IL1B, prostaglandin E2 and
CC       bacterial lipopolysaccharide (LPS) (PubMed:9751056). Required for
CC       normal potentiation of platelet aggregation by prostaglandin E2, and
CC       thus plays a role in the regulation of blood coagulation
CC       (PubMed:11535576). Required for increased HCO3(-) secretion in the
CC       duodenum in response to mucosal acidification, and thereby contributes
CC       to the protection of the mucosa against acid-induced ulceration
CC       (PubMed:10535876). Not required for normal kidney function, normal
CC       urine volume and osmolality (PubMed:9843913).
CC       {ECO:0000269|PubMed:10535876, ECO:0000269|PubMed:11535576,
CC       ECO:0000269|PubMed:1372606, ECO:0000269|PubMed:8223569,
CC       ECO:0000269|PubMed:8381413, ECO:0000269|PubMed:9751056,
CC       ECO:0000269|PubMed:9843913}.
CC   -!- FUNCTION: [Isoform Alpha]: Receptor for prostaglandin E2 (PGE2); ligand
CC       binding activates a signaling cascade via G(i) proteins that leads to
CC       inhibition of adenylate cyclase (PubMed:1372606, PubMed:8381413). Shows
CC       high agonist-independent constitutive inhibition of adenylate cyclase
CC       (PubMed:8223569). {ECO:0000269|PubMed:1372606,
CC       ECO:0000269|PubMed:8223569, ECO:0000269|PubMed:8381413}.
CC   -!- FUNCTION: [Isoform Beta]: Receptor for prostaglandin E2 (PGE2); ligand
CC       binding activates a signaling cascade via G(i) proteins that leads to
CC       inhibition of adenylate cyclase. Requires much higher ligand
CC       concentrations than isoform Alpha for activation (PubMed:8381413). Does
CC       not display agonist-independent constitutive inhibition of adenylate
CC       cyclase (PubMed:8223569). {ECO:0000269|PubMed:8223569,
CC       ECO:0000269|PubMed:8381413}.
CC   -!- FUNCTION: [Isoform Gamma]: Receptor for prostaglandin E2 (PGE2); ligand
CC       binding can activate several distinct signaling cascades, resulting in
CC       activation or inhibition of adenylate cyclase.
CC       {ECO:0000269|PubMed:8223569}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with MKLN1.
CC       {ECO:0000250|UniProtKB:P34980}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1372606,
CC       ECO:0000269|PubMed:8223569, ECO:0000269|PubMed:8381413}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist (Probable). Isoforms have
CC         identical ligand binding properties but different coupling properties
CC         with G proteins: isoform Alpha and isoform Beta couple to G(i)
CC         proteins, whereas isoform Gamma couples to multiple G proteins, G(i)
CC         and G(s) (PubMed:1372606, PubMed:8381413, PubMed:8223569).
CC         {ECO:0000269|PubMed:1372606, ECO:0000269|PubMed:8223569,
CC         ECO:0000269|PubMed:8381413, ECO:0000305};
CC       Name=Alpha;
CC         IsoId=P30557-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=P30557-2; Sequence=VSP_001940;
CC       Name=Gamma;
CC         IsoId=P30557-3; Sequence=VSP_001941;
CC   -!- TISSUE SPECIFICITY: Detected in platelets (PubMed:11535576). Kidney,
CC       uterus, and mastocytoma cells, and in a lesser amount in brain, thymus,
CC       lung, heart, stomach and spleen (PubMed:1372606).
CC       {ECO:0000269|PubMed:11535576, ECO:0000269|PubMed:1372606}.
CC   -!- PTM: Ligand binding is affected by cAMP-dependent phosphorylation in
CC       brain membranes.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are born at the
CC       expected Mendelian rate. Females have normal fertility. Mutant mice
CC       have normal renal function, urine volume and urine osmolality
CC       (PubMed:9843913). Mutant mice fail to develop fever in response to
CC       pyrinogens, including IL1B, prostaglandin E2 and bacterial
CC       lipopolysaccharide (LPS) (PubMed:9751056). Mutant mice lack the normal
CC       potentiation of platelet aggregation by prostaglandin E2 and display
CC       prolonged bleeding times and decreased susceptibility to
CC       thromboembolism (PubMed:11535576). Mutant mice have normal basal levels
CC       of HCO3(-) secretion in the duodenum, but fail to respond to mucosal
CC       acidification by increased HCO3(-) secretion. Unlike wild-type, they
CC       have a high incidence of ulcers in response to mucosal acidification
CC       (PubMed:10535876). {ECO:0000269|PubMed:10535876,
CC       ECO:0000269|PubMed:11535576, ECO:0000269|PubMed:9751056,
CC       ECO:0000269|PubMed:9843913}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; D10204; BAA01051.1; -; mRNA.
DR   EMBL; D13321; BAA02578.1; -; mRNA.
DR   EMBL; D17406; BAA04229.1; -; mRNA.
DR   PIR; A42414; A42414.
DR   PIR; A45211; A45211.
DR   PIR; S65009; S65009.
DR   AlphaFoldDB; P30557; -.
DR   SMR; P30557; -.
DR   STRING; 10090.ENSMUSP00000043302; -.
DR   BindingDB; P30557; -.
DR   ChEMBL; CHEMBL4336; -.
DR   DrugCentral; P30557; -.
DR   GuidetoPHARMACOLOGY; 342; -.
DR   GlyGen; P30557; 2 sites.
DR   iPTMnet; P30557; -.
DR   PhosphoSitePlus; P30557; -.
DR   PaxDb; P30557; -.
DR   PRIDE; P30557; -.
DR   ProteomicsDB; 287908; -. [P30557-1]
DR   ProteomicsDB; 287909; -. [P30557-2]
DR   ProteomicsDB; 287910; -. [P30557-3]
DR   MGI; MGI:97795; Ptger3.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; P30557; -.
DR   PhylomeDB; P30557; -.
DR   Reactome; R-MMU-391908; Prostanoid ligand receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   ChiTaRS; Ptger3; mouse.
DR   PRO; PR:P30557; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P30557; protein.
DR   GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:1990769; C:proximal neuron projection; ISO:MGI.
DR   GO; GO:0004957; F:prostaglandin E receptor activity; IDA:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0015701; P:bicarbonate transport; IMP:MGI.
DR   GO; GO:1904322; P:cellular response to forskolin; ISO:MGI.
DR   GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0001660; P:fever generation; IDA:MGI.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0014827; P:intestine smooth muscle contraction; ISO:MGI.
DR   GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:1903170; P:negative regulation of calcium ion transmembrane transport; ISO:MGI.
DR   GO; GO:1904326; P:negative regulation of circadian sleep/wake cycle, wakefulness; ISO:MGI.
DR   GO; GO:2000978; P:negative regulation of forebrain neuron differentiation; ISO:MGI.
DR   GO; GO:0060455; P:negative regulation of gastric acid secretion; ISO:MGI.
DR   GO; GO:1903640; P:negative regulation of gastrin-induced gastric acid secretion; ISO:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR   GO; GO:0010700; P:negative regulation of norepinephrine secretion; ISO:MGI.
DR   GO; GO:0090331; P:negative regulation of platelet aggregation; ISO:MGI.
DR   GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR   GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; ISO:MGI.
DR   GO; GO:1904343; P:positive regulation of colon smooth muscle contraction; ISO:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:MGI.
DR   GO; GO:0031622; P:positive regulation of fever generation; IMP:BHF-UCL.
DR   GO; GO:1904346; P:positive regulation of gastric mucosal blood circulation; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:1904325; P:positive regulation of inhibitory G protein-coupled receptor phosphorylation; ISO:MGI.
DR   GO; GO:1904330; P:positive regulation of myofibroblast contraction; ISO:MGI.
DR   GO; GO:2000391; P:positive regulation of neutrophil extravasation; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:1904320; P:positive regulation of smooth muscle contraction involved in micturition; ISO:MGI.
DR   GO; GO:0035810; P:positive regulation of urine volume; IMP:MGI.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR   GO; GO:1990767; P:prostaglandin receptor internalization; ISO:MGI.
DR   GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR   GO; GO:0010840; P:regulation of circadian sleep/wake cycle, wakefulness; ISO:MGI.
DR   GO; GO:0014061; P:regulation of norepinephrine secretion; ISO:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISO:MGI.
DR   InterPro; IPR000154; EP3_rcpt_3.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR008365; Prostanoid_rcpt.
DR   InterPro; IPR001244; Prostglndn_DP_rcpt.
DR   InterPro; IPR000265; Prostglndn_EP3_rcpt.
DR   PANTHER; PTHR11866; PTHR11866; 1.
DR   PANTHER; PTHR11866:SF10; PTHR11866:SF10; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00428; PROSTAGLNDNR.
DR   PRINTS; PR01788; PROSTANOIDR.
DR   PRINTS; PR00585; PRSTNOIDE33R.
DR   PRINTS; PR00582; PRSTNOIDEP3R.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..365
FT                   /note="Prostaglandin E2 receptor EP3 subtype"
FT                   /id="PRO_0000070059"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..55
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..68
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..130
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..173
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        174..203
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..229
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..283
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..303
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..325
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        16
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         336..365
FT                   /note="IRDHTNYASSSTSLPCPGSSALMWSDQLER -> MMNNLKWTFIAVPVSLGL
FT                   RISSPREG (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:8381413"
FT                   /id="VSP_001940"
FT   VAR_SEQ         336..365
FT                   /note="IRDHTNYASSSTSLPCPGSSALMWSDQLER -> VANAVSSCSSDGQKGQAI
FT                   SLSNEVVQPGP (in isoform Gamma)"
FT                   /evidence="ECO:0000303|PubMed:8223569"
FT                   /id="VSP_001941"
SQ   SEQUENCE   365 AA;  40077 MW;  1FEBEBB30C5EA67E CRC64;
     MASMWAPEHS AEAHSNLSST TDDCGSVSVA FPITMMVTGF VGNALAMLLV SRSYRRRESK
     RKKSFLLCIG WLALTDLVGQ LLTSPVVILV YLSQRRWEQL DPSGRLCTFF GLTMTVFGLS
     SLLVASAMAV ERALAIRAPH WYASHMKTRA TPVLLGVWLS VLAFALLPVL GVGRYSVQWP
     GTWCFISTGP AGNETDPARE PGSVAFASAF ACLGLLALVV TFACNLATIK ALVSRCRAKA
     AVSQSSAQWG RITTETAIQL MGIMCVLSVC WSPLLIMMLK MIFNQMSVEQ CKTQMGKEKE
     CNSFLIAVRL ASLNQILDPW VYLLLRKILL RKFCQIRDHT NYASSSTSLP CPGSSALMWS
     DQLER
 
 
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