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 27-MAR-2024, entry version 125.
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 GlyCosmos; Q9XT82; 3 sites, No reported glycans.
DR PaxDb; 9612-ENSCAFP00000021671; -.
DR Ensembl; ENSCAFT00000023338.5; ENSCAFP00000021671.5; ENSCAFG00000014701.5.
DR Ensembl; ENSCAFT00030007739.1; ENSCAFP00030006785.1; ENSCAFG00030004194.1.
DR Ensembl; ENSCAFT00040008881.1; ENSCAFP00040007709.1; ENSCAFG00040004719.1.
DR Ensembl; ENSCAFT00805002545; ENSCAFP00805001978; ENSCAFG00805001406.
DR Ensembl; ENSCAFT00845006662.1; ENSCAFP00845005301.1; ENSCAFG00845003728.1.
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; 5355693at2759; -.
DR Reactome; R-CFA-391908; Prostanoid ligand receptors.
DR Reactome; R-CFA-418555; G alpha (s) signalling events.
DR Proteomes; UP000002254; Chromosome 8.
DR Proteomes; UP000694429; Chromosome 8.
DR Proteomes; UP000694542; Chromosome 8.
DR Proteomes; UP000805418; Chromosome 8.
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 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.
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
//
