ID   PE2R2_CANLF             Reviewed;         361 AA.
AC   Q9XT82;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=10410384; DOI=10.1016/s0090-6980(98)00081-1;
RA   Hibbs T.A., Lu B., Smock S.L., Vestergaard P., Pan L.C., Owen T.A.;
RT   "Molecular cloning and characterization of the canine prostaglandin E
RT   receptor EP2 subtype.";
RL   Prostaglandins Other Lipid Mediat. 57:133-147(1999).
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; AF075602; AAD43140.1; -; mRNA.
DR   RefSeq; NP_001003170.1; NM_001003170.1.
DR   AlphaFoldDB; Q9XT82; -.
DR   SMR; Q9XT82; -.
DR   STRING; 9615.ENSCAFP00000021671; -.
DR   BindingDB; Q9XT82; -.
DR   PaxDb; Q9XT82; -.
DR   Ensembl; ENSCAFT00000023338; ENSCAFP00000021671; ENSCAFG00000014701.
DR   Ensembl; ENSCAFT00030007739; ENSCAFP00030006785; ENSCAFG00030004194.
DR   Ensembl; ENSCAFT00040008881; ENSCAFP00040007709; ENSCAFG00040004719.
DR   Ensembl; ENSCAFT00845006662; ENSCAFP00845005301; ENSCAFG00845003728.
DR   GeneID; 403797; -.
DR   KEGG; cfa:403797; -.
DR   CTD; 5732; -.
DR   VEuPathDB; HostDB:ENSCAFG00845003728; -.
DR   VGNC; VGNC:45143; PTGER2.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244902; -.
DR   InParanoid; Q9XT82; -.
DR   OrthoDB; 972015at2759; -.
DR   Reactome; R-CFA-391908; Prostanoid ligand receptors.
DR   Reactome; R-CFA-418555; G alpha (s) signalling events.
DR   Proteomes; UP000002254; Chromosome 8.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004957; F:prostaglandin E receptor activity; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CAFA.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:CAFA.
DR   GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IMP:CAFA.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:CAFA.
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; PTHR11866; 1.
DR   PANTHER; PTHR11866:SF8; PTHR11866:SF8; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01788; PROSTANOIDR.
DR   PRINTS; PR00581; PRSTNOIDEP2R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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..361
FT                   /note="Prostaglandin E2 receptor EP2 subtype"
FT                   /id="PRO_0000070053"
FT   TOPO_DOM        1..23
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..47
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..91
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..111
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..198
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..223
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..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..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   361 AA;  40275 MW;  BC997FC8DD4FBDCB CRC64;
     MGSISNNSGS EDCESREWLP SGESPAISSA MFSAGVLGNL IALALLARRW RGDAGRRAGR
     GNSISLFHVL VTELVFTDLL GTCLISPVVL ASYARNQTLM ALEPERRACT YFAFAMTFFS
     LATMLMLFAM ALERYLSIGR PYFYQRHVTR RGGLAVLPTI YTVSLLFCSL PLLGYGQYVQ
     YCPGTWCFIR HGRTAYLQLY ATLLLLLIVA VLACNFSVIL NLIRMHRRSG RSRCGPSLGS
     CRDGSGTRRR GERVSVAEET DHLILLAIMT ITFAICSLPF TIFAYMNETS SRREKWDLQA
     LRFLSINSII DPWVFAIFRP PVLRLMRSVL CCRVSLRAQD ATQTSCSIQS NASRLTFVDT
     S