ID PE2R1_RAT Reviewed; 405 AA. AC P70597; P97537; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 24-JAN-2024, entry version 164. DE RecName: Full=Prostaglandin E2 receptor EP1 subtype; DE Short=PGE receptor EP1 subtype; DE Short=PGE2 receptor EP1 subtype; DE AltName: Full=Prostanoid EP1 receptor; GN Name=Ptger1; 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 STRAIN=Sprague-Dawley; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RC STRAIN=Wistar; TISSUE=Uterus; RX PubMed=8940129; DOI=10.1074/jbc.271.49.31255; RA Okuda-Ashitaka E., Sakamoto K., Ezashi T., Miwa K., Ito S., Hayaishi O.; RT "Suppression of prostaglandin E receptor signaling by the variant form of RT EP1 subtype."; RL J. Biol. Chem. 271:31255-31261(1996). CC -!- FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this CC receptor is mediated by G(q) proteins which activate a CC phosphatidylinositol-calcium second messenger system. May play a role CC as an important modulator of renal function (By similarity). Implicated CC the smooth muscle contractile response to PGE2 in various tissues. CC Isoform 1 and isoform 2 have identical ligand binding properties, but CC isoform 2 lacks coupling to calcium mobilization and may therefore CC attenuate the action of PGE2 on tissues. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P70597-1; Sequence=Displayed; CC Name=2; CC IsoId=P70597-2; Sequence=VSP_001927, VSP_001928; CC -!- TISSUE SPECIFICITY: Highly abundant in kidney and lung. Found in a CC lesser extent in spleen, colon, and thymus. Also expressed in uterine CC myometrium and endometrium. CC -!- PTM: Phosphorylated. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U68037; AAB07735.1; -; mRNA. DR EMBL; D88751; BAA13691.1; -; mRNA. DR EMBL; D88752; BAA13692.1; -; mRNA. DR RefSeq; NP_001265404.1; NM_001278475.1. [P70597-1] DR AlphaFoldDB; P70597; -. DR SMR; P70597; -. DR BioGRID; 247666; 1. DR STRING; 10116.ENSRNOP00000005470; -. DR BindingDB; P70597; -. DR ChEMBL; CHEMBL5068; -. DR DrugCentral; P70597; -. DR GuidetoPHARMACOLOGY; 340; -. DR GlyCosmos; P70597; 3 sites, No reported glycans. DR GlyGen; P70597; 3 sites. DR PhosphoSitePlus; P70597; -. DR PaxDb; 10116-ENSRNOP00000005470; -. DR Ensembl; ENSRNOT00000005470.5; ENSRNOP00000005470.1; ENSRNOG00000004094.5. [P70597-1] DR GeneID; 25637; -. DR KEGG; rno:25637; -. DR AGR; RGD:3434; -. DR CTD; 5731; -. DR RGD; 3434; Ptger1. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01030000234559; -. DR HOGENOM; CLU_045991_3_0_1; -. DR InParanoid; P70597; -. DR OrthoDB; 4642085at2759; -. DR PhylomeDB; P70597; -. DR TreeFam; TF324982; -. DR Reactome; R-RNO-391908; Prostanoid ligand receptors. DR Reactome; R-RNO-416476; G alpha (q) signalling events. DR PRO; PR:P70597; -. DR Proteomes; UP000002494; Chromosome 19. DR Bgee; ENSRNOG00000004094; Expressed in thymus and 18 other cell types or tissues. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:RGD. DR GO; GO:0004957; F:prostaglandin E receptor activity; IDA:RGD. DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISO:RGD. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. 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:0032496; P:response to lipopolysaccharide; ISO:RGD. 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; IPR001244; Prostglndn_DP_rcpt. DR InterPro; IPR000708; Prostglndn_EP1_rcpt. DR PANTHER; PTHR11866; G-PROTEIN COUPLED RECEPTOR FAMILY 1 MEMBER; 1. DR PANTHER; PTHR11866:SF3; PROSTAGLANDIN E2 RECEPTOR EP1 SUBTYPE; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00428; PROSTAGLNDNR. DR PRINTS; PR01788; PROSTANOIDR. DR PRINTS; PR00580; PRSTNOIDEP1R. 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; P70597; RN. PE 2: Evidence at transcript level; KW Alternative splicing; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; KW Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..405 FT /note="Prostaglandin E2 receptor EP1 subtype" FT /id="PRO_0000070052" FT TOPO_DOM 1..39 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 40..62 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 63..80 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 81..99 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 100..113 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 114..135 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 136..157 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 158..179 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 180..202 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 203..228 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 229..301 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 302..323 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 324..337 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 338..357 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 358..405 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 7 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 24 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 112..190 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VAR_SEQ 319..366 FT /note="LVVLAIGGWNSNSLQRPLFLAVRLASWNQILDPWVYILLRQAMLRQLL -> FT RGAVAPQAKLFSAPSWPLPAKDPACRQKPAPLLSRTLTFFTLFGNLCK (in FT isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_001927" FT VAR_SEQ 367..405 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_001928" SQ SEQUENCE 405 AA; 43048 MW; E8312388B619F9EC CRC64; MSPYGLNLSL VDEATTCVTP RVPNTSVVLP TGGNGTSPAL PIFSMTLGAV SNVLALALLA QVAGRLRRRR STATFLLFVA SLLAIDLAGH VIPGALVLRL YTAGRAPAGG ACHFLGGCMV FFGLCPLLLG CGMAVERCVG VTQPLIHAAR VSVARARLAL ALLAAMALAV ALLPLVHVGH YELQYPGTWC FISLGPPGGW RQALLAGLFA GLGLAALLAA LVCNTLSGLA LLRARWRRRR SRRFRENAGP DDRRRWGSRG LRLASASSAS SITSTTAALR SSRGGGSARR VHAHDVEMVG QLVGIMVVSC ICWSPLLVLV VLAIGGWNSN SLQRPLFLAV RLASWNQILD PWVYILLRQA MLRQLLRLLP LRVSAKGGPT ELSLTKSAWE ASSLRSSRHS GFSHL //