PE2R1_MOUSE
ID PE2R1_MOUSE Reviewed; 405 AA.
AC P35375;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 162.
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; Synonyms=Ptgerep1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ddY; TISSUE=Kidney;
RX PubMed=7690750; DOI=10.1016/s0021-9258(20)80710-8;
RA Watabe A., Sugimoto Y., Honda A., Irie A., Namba T., Negishi M., Ito S.,
RA Narumiya S., Ichikawa A.;
RT "Cloning and expression of cDNA for a mouse EP1 subtype of prostaglandin E
RT receptor.";
RL J. Biol. Chem. 268:20175-20178(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=7649181; DOI=10.1111/j.1432-1033.1995.tb20765.x;
RA Batshake B., Nilsson C., Sundelin J.;
RT "Molecular characterization of the mouse prostanoid EP1 receptor gene.";
RL Eur. J. Biochem. 231:809-814(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=8858105; DOI=10.1006/bbrc.1996.1469;
RA Batshake B., Sundelin S.;
RT "The mouse genes for the EP1 prostanoid receptor and the PKN protein kinase
RT overlap.";
RL Biochem. Biophys. Res. Commun. 227:70-76(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. Implicated the smooth
CC muscle contractile response to PGE2 in various tissues.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Abundant in kidney and in a lesser amount in lung.
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; D16338; BAA03842.1; -; mRNA.
DR EMBL; Z49987; CAA90278.1; -; Genomic_DNA.
DR EMBL; Y07611; CAA68884.1; -; Genomic_DNA.
DR CCDS; CCDS22458.1; -.
DR PIR; S66525; S66525.
DR RefSeq; NP_038669.1; NM_013641.2.
DR AlphaFoldDB; P35375; -.
DR SMR; P35375; -.
DR BioGRID; 202454; 1.
DR STRING; 10090.ENSMUSP00000019608; -.
DR BindingDB; P35375; -.
DR ChEMBL; CHEMBL2181; -.
DR DrugCentral; P35375; -.
DR GuidetoPHARMACOLOGY; 340; -.
DR GlyGen; P35375; 3 sites.
DR iPTMnet; P35375; -.
DR PhosphoSitePlus; P35375; -.
DR PaxDb; P35375; -.
DR PRIDE; P35375; -.
DR Antibodypedia; 13701; 263 antibodies from 32 providers.
DR DNASU; 19216; -.
DR Ensembl; ENSMUST00000019608; ENSMUSP00000019608; ENSMUSG00000019464.
DR GeneID; 19216; -.
DR KEGG; mmu:19216; -.
DR UCSC; uc009mkt.1; mouse.
DR CTD; 5731; -.
DR MGI; MGI:97793; Ptger1.
DR VEuPathDB; HostDB:ENSMUSG00000019464; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234559; -.
DR HOGENOM; CLU_045991_3_0_1; -.
DR InParanoid; P35375; -.
DR OMA; IYLIAKC; -.
DR PhylomeDB; P35375; -.
DR TreeFam; TF324982; -.
DR Reactome; R-MMU-391908; Prostanoid ligand receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 19216; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ptger1; mouse.
DR PRO; PR:P35375; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P35375; protein.
DR Bgee; ENSMUSG00000019464; Expressed in lumbar dorsal root ganglion and 79 other tissues.
DR ExpressionAtlas; P35375; baseline and differential.
DR Genevisible; P35375; MM.
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; IPI:UniProtKB.
DR GO; GO:0004957; F:prostaglandin E receptor activity; ISO:MGI.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..405
FT /note="Prostaglandin E2 receptor EP1 subtype"
FT /id="PRO_0000070051"
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 REGION 243..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 405 AA; 42966 MW; 2E64D421005CF8D6 CRC64;
MSPCGLNLSL ADEAATCATP RLPNTSVVLP TGDNGTSPAL PIFSMTLGAV SNVLALALLA
QVAGRMRRRR SAATFLLFVA SLLAIDLAGH VIPGALVLRL YTAGRAPAGG ACHFLGGCMV
FFGLCPLLLG CGMAVERCVG VTQPLIHAAR VSVARARLAL AVLAAMALAV ALLPLVHVGR
YELQYPGTWC FISLGPRGGW RQALLAGLFA GLGLAALLAA LVCNTLSGLA LLRARWRRRR
SRRFRKTAGP DDRRRWGSRG PRLASASSAS SITSATATLR SSRGGGSARR VHAHDVEMVG
QLVGIMVVSC ICWSPLLVLV VLAIGGWNSN SLQRPLFLAV RLASWNQILD PWVYILLRQA
MLRQLLRLLP LRVSAKGGPT ELGLTKSAWE ASSLRSSRHS GFSHL
