PE2R1_RAT
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 03-AUG-2022, entry version 157.
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}.
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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 GlyGen; P70597; 3 sites.
DR PhosphoSitePlus; P70597; -.
DR PaxDb; P70597; -.
DR Ensembl; ENSRNOT00000005470; ENSRNOP00000005470; ENSRNOG00000004094. [P70597-1]
DR GeneID; 25637; -.
DR KEGG; rno:25637; -.
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 OMA; IYLIAKC; -.
DR OrthoDB; 972015at2759; -.
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 tissues.
DR Genevisible; P70597; RN.
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: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:0120061; P:negative regulation of gastric emptying; IMP:RGD.
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 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; PTHR11866; 1.
DR PANTHER; PTHR11866:SF3; PTHR11866:SF3; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00428; PROSTAGLNDNR.
DR PRINTS; PR01788; PROSTANOIDR.
DR PRINTS; PR00580; PRSTNOIDEP1R.
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 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
