ID   PE2R2_RAT               Reviewed;         357 AA.
AC   Q62928; Q547S0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Prostaglandin E2 receptor EP2 subtype;
DE            Short=PGE receptor EP2 subtype;
DE            Short=PGE2 receptor EP2 subtype;
DE   AltName: Full=Prostanoid EP2 receptor;
GN   Name=Ptger2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=9440134; DOI=10.1016/s0090-6980(97)00145-7;
RA   Nemoto K., Pilbeam C.C., Bilak S.R., Raisz L.G.;
RT   "Molecular cloning and expression of a rat prostaglandin E2 receptor of the
RT   EP2 subtype.";
RL   Prostaglandins 54:713-725(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Spleen;
RX   PubMed=9537820; DOI=10.1016/s0014-2999(97)01383-6;
RA   Boie Y., Stocco R., Sawyer N., Slipetz D.M., Ungrin M.D.,
RA   Neuschafer-Rube F., Puschel G.P., Metters K.M., Abramovitz M.;
RT   "Molecular cloning and characterization of the four rat prostaglandin E2
RT   prostanoid receptor subtypes.";
RL   Eur. J. Pharmacol. 340:227-241(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
RA   Chien E.K., Mendoza J.;
RT   "Constitutive expression of Ptger-ep2 in the pregnant rat uterus.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this
CC       receptor is mediated by G(s) proteins that stimulate adenylate cyclase.
CC       The subsequent raise in intracellular cAMP is responsible for the
CC       relaxing effect of this receptor on smooth muscle (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U48858; AAA97889.1; -; mRNA.
DR   EMBL; U94708; AAB53325.1; -; mRNA.
DR   EMBL; AF454964; AAM73855.1; -; Genomic_DNA.
DR   RefSeq; NP_112350.1; NM_031088.1.
DR   AlphaFoldDB; Q62928; -.
DR   SMR; Q62928; -.
DR   STRING; 10116.ENSRNOP00000064907; -.
DR   BindingDB; Q62928; -.
DR   ChEMBL; CHEMBL4909; -.
DR   DrugCentral; Q62928; -.
DR   GuidetoPHARMACOLOGY; 341; -.
DR   GlyCosmos; Q62928; 1 site, No reported glycans.
DR   GlyGen; Q62928; 1 site.
DR   PhosphoSitePlus; Q62928; -.
DR   PaxDb; 10116-ENSRNOP00000064907; -.
DR   Ensembl; ENSRNOT00000075209.3; ENSRNOP00000064907.1; ENSRNOG00000050968.3.
DR   Ensembl; ENSRNOT00055046233; ENSRNOP00055037957; ENSRNOG00055026775.
DR   Ensembl; ENSRNOT00060049603; ENSRNOP00060041364; ENSRNOG00060028536.
DR   Ensembl; ENSRNOT00065013735; ENSRNOP00065010184; ENSRNOG00065008656.
DR   GeneID; 81752; -.
DR   KEGG; rno:81752; -.
DR   AGR; RGD:620020; -.
DR   CTD; 5732; -.
DR   RGD; 620020; Ptger2.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244902; -.
DR   HOGENOM; CLU_045991_0_2_1; -.
DR   InParanoid; Q62928; -.
DR   OMA; YSRHVTK; -.
DR   OrthoDB; 5355693at2759; -.
DR   PhylomeDB; Q62928; -.
DR   TreeFam; TF324982; -.
DR   Reactome; R-RNO-391908; Prostanoid ligand receptors.
DR   PRO; PR:Q62928; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000050968; Expressed in spleen and 11 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004957; F:prostaglandin E receptor activity; IDA:RGD.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:1904346; P:positive regulation of gastric mucosal blood circulation; IDA:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR   GO; GO:0009624; P:response to nematode; ISO:RGD.
DR   GO; GO:0032570; P:response to progesterone; ISO:RGD.
DR   GO; GO:0001501; P:skeletal system development; NAS:RGD.
DR   CDD; cd15139; 7tmA_PGE2_EP2; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR008365; Prostanoid_rcpt.
DR   InterPro; IPR001923; Prostglndn_EP2_rcpt.
DR   PANTHER; PTHR11866; G-PROTEIN COUPLED RECEPTOR FAMILY 1 MEMBER; 1.
DR   PANTHER; PTHR11866:SF8; PROSTAGLANDIN E2 RECEPTOR EP2 SUBTYPE; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01788; PROSTANOIDR.
DR   PRINTS; PR00581; PRSTNOIDEP2R.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q62928; RN.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..357
FT                   /note="Prostaglandin E2 receptor EP2 subtype"
FT                   /id="PRO_0000070056"
FT   TOPO_DOM        1..24
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..48
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..92
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..112
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..177
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..199
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..224
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..262
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..286
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..299
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..323
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..357
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          235..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        110..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   357 AA;  39772 MW;  AAB22A8280AFEFB0 CRC64;
     MDNSFNDSRR VENCESRQYL LSDESPAISS VMFTAGVLGN LIALALLARR WRGDTGCSAG
     SRTSISLFHV LVTELVLTDL LGTCLISPVV LASYSRNQTL VALAPESRAC TYFAFTMTFF
     SLATMLMLFA MALERYLAIG HPYFYRRRVS RRGGLAVLPA IYGVSLLFCS LPLLNYGEYV
     QYCPGTWCFI QHGRTAYLQL YATVLLLLIV AVLGCNISVI LNLIRMQLRS KRSRCGLSGS
     SLRGPGSRRR GERTSMAEET DHLILLAIMT ITFAVCSLPF TIFAYMDETS SRKEKWDLRA
     LRFLSVNSII DPWVFVILRP PVLRLMRSVL CCRTSLRAPE APGASCSTQQ TDLCGQL
//