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   24-JAN-2024, entry version 169.
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   GlyCosmos; P35375; 3 sites, No reported glycans.
DR   GlyGen; P35375; 3 sites.
DR   iPTMnet; P35375; -.
DR   PhosphoSitePlus; P35375; -.
DR   PaxDb; 10090-ENSMUSP00000019608; -.
DR   Antibodypedia; 13701; 313 antibodies from 32 providers.
DR   DNASU; 19216; -.
DR   Ensembl; ENSMUST00000019608.7; ENSMUSP00000019608.6; ENSMUSG00000019464.7.
DR   GeneID; 19216; -.
DR   KEGG; mmu:19216; -.
DR   UCSC; uc009mkt.1; mouse.
DR   AGR; MGI:97793; -.
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   OrthoDB; 5400441at2759; -.
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 78 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 80 other cell types or tissues.
DR   ExpressionAtlas; P35375; baseline and differential.
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:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
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; P35375; MM.
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
//