ID   PE2R2_MOUSE             Reviewed;         362 AA.
AC   Q62053;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 180.
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; Synonyms=Ptgerep2;
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].
RC   STRAIN=ddY; TISSUE=Lung;
RX   PubMed=7556658; DOI=10.1016/0014-5793(95)00966-d;
RA   Katsuyama M., Nishigaki N., Sugimoto Y., Morimoto K., Negishi M.,
RA   Narumiya S., Ichikawa A.;
RT   "The mouse prostaglandin E receptor EP2 subtype: cloning, expression, and
RT   northern blot analysis.";
RL   FEBS Lett. 372:151-156(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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.
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; D50589; BAA09137.1; -; mRNA.
DR   EMBL; BC005440; AAH05440.1; -; mRNA.
DR   CCDS; CCDS26972.1; -.
DR   PIR; S66674; S66674.
DR   RefSeq; NP_032990.1; NM_008964.4.
DR   AlphaFoldDB; Q62053; -.
DR   SMR; Q62053; -.
DR   STRING; 10090.ENSMUSP00000038483; -.
DR   BindingDB; Q62053; -.
DR   ChEMBL; CHEMBL2488; -.
DR   DrugCentral; Q62053; -.
DR   GuidetoPHARMACOLOGY; 341; -.
DR   GlyCosmos; Q62053; 1 site, No reported glycans.
DR   GlyGen; Q62053; 1 site.
DR   PhosphoSitePlus; Q62053; -.
DR   MaxQB; Q62053; -.
DR   PaxDb; 10090-ENSMUSP00000038483; -.
DR   ProteomicsDB; 301784; -.
DR   Antibodypedia; 10768; 649 antibodies from 33 providers.
DR   DNASU; 19217; -.
DR   Ensembl; ENSMUST00000046891.6; ENSMUSP00000038483.6; ENSMUSG00000037759.7.
DR   GeneID; 19217; -.
DR   KEGG; mmu:19217; -.
DR   UCSC; uc007tgd.2; mouse.
DR   AGR; MGI:97794; -.
DR   CTD; 5732; -.
DR   MGI; MGI:97794; Ptger2.
DR   VEuPathDB; HostDB:ENSMUSG00000037759; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244902; -.
DR   HOGENOM; CLU_045991_0_2_1; -.
DR   InParanoid; Q62053; -.
DR   OMA; CSVSPFV; -.
DR   OrthoDB; 5355693at2759; -.
DR   PhylomeDB; Q62053; -.
DR   TreeFam; TF324982; -.
DR   Reactome; R-MMU-391908; Prostanoid ligand receptors.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   BioGRID-ORCS; 19217; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Ptger2; mouse.
DR   PRO; PR:Q62053; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q62053; Protein.
DR   Bgee; ENSMUSG00000037759; Expressed in granulocyte and 89 other cell types or tissues.
DR   ExpressionAtlas; Q62053; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004957; F:prostaglandin E receptor activity; ISO:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:BHF-UCL.
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; ISO:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0009624; P:response to nematode; IMP:MGI.
DR   GO; GO:0032570; P:response to progesterone; IDA:CACAO.
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; Q62053; MM.
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..362
FT                   /note="Prostaglandin E2 receptor EP2 subtype"
FT                   /id="PRO_0000070055"
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..362
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          234..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   362 AA;  40479 MW;  A79FCEE8B6771F44 CRC64;
     MDNFLNDSKL MEDCKSRQWL LSGESPAISS VMFSAGVLGN LIALALLARR WRGDTGCSAG
     SRTSISLFHV LVTELVLTDL LGTCLISPVV LASYSRNQTL VALAPESHAC TYFAFTMTFF
     SLATMLMLFA MALERYLSIG YPYFYRRHLS RRGGLAVLPV IYGASLLFCS LPLLNYGEYV
     QYCPGTWCFI RHGRTAYLQL YATMLLLLIV AVLACNISVI LNLIRMHRRS RRSRCGLSGS
     SLRGPGSRRR GERTSMAEET DHLILLAIMT ITFAICSLPF TIFAYMDETS SLKEKWDLRA
     LRFLSVNSII DPWVFAILRP PVLRLMRSVL CCRTSLRTQE AQQTSCSTQS SASKQTDLCG
     QL
//