PE2R2_HUMAN
ID PE2R2_HUMAN Reviewed; 358 AA.
AC P43116; D3DSC0; Q52LG8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 177.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8078484;
RA Regan J.W., Bailey T.J., Pepperl D.J., Pierce K.L., Bogardus A.M.,
RA Donello J.E., Fairbairn C.E., Kedzie K.M., Woodward D.F., Gil D.W.;
RT "Cloning of a novel human prostaglandin receptor with characteristics of
RT the pharmacologically defined EP2 subtype.";
RL Mol. Pharmacol. 46:213-220(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Oakley C.J.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10521663; DOI=10.1016/s0378-1119(99)00323-6;
RA Smock S.L., Pan L.C., Castleberry T.A., Lu B., Mather R.J., Owen T.A.;
RT "Cloning, structural characterization, and chromosomal localization of the
RT gene encoding the human prostaglandin E2 receptor EP2 subtype.";
RL Gene 237:393-402(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 -!- TISSUE SPECIFICITY: Placenta and lung.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ptger2/";
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DR EMBL; U19487; AAA61681.1; -; mRNA.
DR EMBL; X83868; CAA58749.1; -; mRNA.
DR EMBL; AF134202; AAD44177.1; -; Genomic_DNA.
DR EMBL; AF134201; AAD44177.1; JOINED; Genomic_DNA.
DR EMBL; AY275471; AAP32303.1; -; mRNA.
DR EMBL; DQ398948; ABD48958.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65652.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65654.1; -; Genomic_DNA.
DR EMBL; BC093927; AAH93927.1; -; mRNA.
DR EMBL; BC093929; AAH93929.1; -; mRNA.
DR CCDS; CCDS9708.1; -.
DR PIR; I38920; I38920.
DR PIR; S51312; S51312.
DR RefSeq; NP_000947.2; NM_000956.3.
DR PDB; 7CX2; EM; 2.80 A; R=1-358.
DR PDB; 7CX3; EM; 2.80 A; R=1-358.
DR PDB; 7CX4; EM; 2.90 A; R=1-358.
DR PDBsum; 7CX2; -.
DR PDBsum; 7CX3; -.
DR PDBsum; 7CX4; -.
DR AlphaFoldDB; P43116; -.
DR SMR; P43116; -.
DR BioGRID; 111704; 2.
DR IntAct; P43116; 4.
DR STRING; 9606.ENSP00000245457; -.
DR BindingDB; P43116; -.
DR ChEMBL; CHEMBL1881; -.
DR DrugBank; DB00770; Alprostadil.
DR DrugBank; DB00917; Dinoprostone.
DR DrugBank; DB08964; Gemeprost.
DR DrugBank; DB09211; Limaprost.
DR DrugBank; DB00929; Misoprostol.
DR DrugCentral; P43116; -.
DR GuidetoPHARMACOLOGY; 341; -.
DR GlyGen; P43116; 4 sites.
DR iPTMnet; P43116; -.
DR PhosphoSitePlus; P43116; -.
DR BioMuta; PTGER2; -.
DR DMDM; 38258920; -.
DR MassIVE; P43116; -.
DR PaxDb; P43116; -.
DR PeptideAtlas; P43116; -.
DR PRIDE; P43116; -.
DR ProteomicsDB; 55587; -.
DR Antibodypedia; 10768; 590 antibodies from 33 providers.
DR DNASU; 5732; -.
DR Ensembl; ENST00000245457.6; ENSP00000245457.5; ENSG00000125384.7.
DR GeneID; 5732; -.
DR KEGG; hsa:5732; -.
DR MANE-Select; ENST00000245457.6; ENSP00000245457.5; NM_000956.4; NP_000947.2.
DR UCSC; uc001wzr.4; human.
DR CTD; 5732; -.
DR DisGeNET; 5732; -.
DR GeneCards; PTGER2; -.
DR HGNC; HGNC:9594; PTGER2.
DR HPA; ENSG00000125384; Tissue enhanced (bone).
DR MalaCards; PTGER2; -.
DR MIM; 176804; gene.
DR neXtProt; NX_P43116; -.
DR OpenTargets; ENSG00000125384; -.
DR PharmGKB; PA287; -.
DR VEuPathDB; HostDB:ENSG00000125384; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244902; -.
DR HOGENOM; CLU_045991_0_1_1; -.
DR InParanoid; P43116; -.
DR OMA; FYQRWVT; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; P43116; -.
DR TreeFam; TF324982; -.
DR PathwayCommons; P43116; -.
DR Reactome; R-HSA-391908; Prostanoid ligand receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SABIO-RK; P43116; -.
DR SignaLink; P43116; -.
DR SIGNOR; P43116; -.
DR BioGRID-ORCS; 5732; 12 hits in 1070 CRISPR screens.
DR GeneWiki; Prostaglandin_E2_receptor; -.
DR GenomeRNAi; 5732; -.
DR Pharos; P43116; Tclin.
DR PRO; PR:P43116; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P43116; protein.
DR Bgee; ENSG00000125384; Expressed in granulocyte and 106 other tissues.
DR ExpressionAtlas; P43116; baseline and differential.
DR Genevisible; P43116; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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; ISS:BHF-UCL.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
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:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009624; P:response to nematode; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..358
FT /note="Prostaglandin E2 receptor EP2 subtype"
FT /id="PRO_0000070054"
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..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 231..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
FT CONFLICT 150
FT /note="R -> A (in Ref. 1; AAA61681 and 3; AAD44177)"
FT /evidence="ECO:0000305"
FT HELIX 27..45
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:7CX2"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:7CX2"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:7CX2"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 110..139
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:7CX2"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:7CX2"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:7CX2"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 196..227
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 259..276
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:7CX2"
FT TURN 288..295
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 297..316
FT /evidence="ECO:0007829|PDB:7CX2"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:7CX2"
SQ SEQUENCE 358 AA; 39761 MW; B3B0E2AA3CF2E363 CRC64;
MGNASNDSQS EDCETRQWLP PGESPAISSV MFSAGVLGNL IALALLARRW RGDVGCSAGR
RSSLSLFHVL VTELVFTDLL GTCLISPVVL ASYARNQTLV ALAPESRACT YFAFAMTFFS
LATMLMLFAM ALERYLSIGH PYFYQRRVSR SGGLAVLPVI YAVSLLFCSL PLLDYGQYVQ
YCPGTWCFIR HGRTAYLQLY ATLLLLLIVS VLACNFSVIL NLIRMHRRSR RSRCGPSLGS
GRGGPGARRR GERVSMAEET DHLILLAIMT ITFAVCSLPF TIFAYMNETS SRKEKWDLQA
LRFLSINSII DPWVFAILRP PVLRLMRSVL CCRISLRTQD ATQTSCSTQS DASKQADL
