PE2R1_CANLF
ID PE2R1_CANLF Reviewed; 403 AA.
AC Q9BGL8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 96.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Abramovitz M., Bastien L., Carriere M.-C., Stocco R.;
RT "Cloning of dog EP1 and EP3 prostanoid receptors.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF266477; AAK07512.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9BGL8; -.
DR SMR; Q9BGL8; -.
DR STRING; 9615.ENSCAFP00000024002; -.
DR PaxDb; Q9BGL8; -.
DR Ensembl; ENSCAFT00030013172; ENSCAFP00030011514; ENSCAFG00030007187.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9BGL8; -.
DR Reactome; R-CFA-391908; Prostanoid ligand receptors.
DR Reactome; R-CFA-416476; G alpha (q) signalling events.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IEA:Ensembl.
DR GO; GO:0004957; F:prostaglandin E receptor activity; IEA:InterPro.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..403
FT /note="Prostaglandin E2 receptor EP1 subtype"
FT /id="PRO_0000070049"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..322
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..355
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 243..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 113..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 403 AA; 42063 MW; FE590C1EB04FD305 CRC64;
MSLCGPLNLS LAGEATPCAE PGAPNASAWP PSGRASASPA LPIFSMTLGA VSNVLALALL
AQAAGRLRRR RSAATFLLFV ASLLATDLAG HVIPGALVLR LYAAGRSPAG GACHFLGGCM
VFFGLCPLLL GCGMAVERCV GVTRPLLHAA RVSAARARLA LAVLAALALA VALLPLARVG
RYELQYPGTW CFIGLRPAGG WRQALLAGLF AGLGLAALLA ALVCNTLSGL ALLRARWRRR
RSRRRPQACG PDGRRHWGAR APRSASASSS SSVASVPGGS PGRGSARRAR AHDVEMVGQL
VGIMVVSCIC WSPLLVLVVL AVGGWGSSSL QRPLFLAVRL ASWNQILDPW VYILLRQAVL
RQLLRLLPPR PGAKGSPAGL ALTRSAWEAS SLRSSRHSSL SHL
