PE2R4_RAT
ID PE2R4_RAT Reviewed; 488 AA.
AC P43114; O08728;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Prostaglandin E2 receptor EP4 subtype;
DE Short=PGE receptor EP4 subtype;
DE Short=PGE2 receptor EP4 subtype;
DE AltName: Full=Prostanoid EP4 receptor;
GN Name=Ptger4;
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 TISSUE=Lung;
RX PubMed=8185583; DOI=10.1006/bbrc.1994.1596;
RA Sando T., Usui T., Tanaka I., Mori K., Sasaki Y., Fukuda Y., Namba T.,
RA Sugimoto Y., Ichikawa A., Narumiya S., Nakao K.;
RT "Molecular cloning and expression of rat prostaglandin E receptor EP2
RT subtype.";
RL Biochem. Biophys. Res. Commun. 200:1329-1333(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
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).
CC -!- FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this
CC receptor is mediated by G(s) proteins that stimulate adenylate cyclase.
CC Has a relaxing effect on smooth muscle. May play an important role in
CC regulating renal hemodynamics, intestinal epithelial transport, adrenal
CC aldosterone secretion, and uterine function.
CC -!- SUBUNIT: Interacts with FEM1A. {ECO:0000250|UniProtKB:P35408}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphorylation mediates agonist-mediated desensitization by
CC promoting cytoplasmic retention. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally designated as the EP2 subtype. {ECO:0000305}.
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DR EMBL; D28860; BAA06011.1; -; mRNA.
DR EMBL; U94709; AAB53326.1; -; mRNA.
DR PIR; JC2241; JC2241.
DR RefSeq; NP_114465.3; NM_032076.3.
DR RefSeq; XP_006232058.1; XM_006231996.3.
DR AlphaFoldDB; P43114; -.
DR SMR; P43114; -.
DR STRING; 10116.ENSRNOP00000017886; -.
DR BindingDB; P43114; -.
DR ChEMBL; CHEMBL4086; -.
DR DrugCentral; P43114; -.
DR GuidetoPHARMACOLOGY; 343; -.
DR GlyGen; P43114; 1 site.
DR PhosphoSitePlus; P43114; -.
DR PaxDb; P43114; -.
DR GeneID; 84023; -.
DR KEGG; rno:84023; -.
DR CTD; 5734; -.
DR RGD; 628641; Ptger4.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P43114; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; P43114; -.
DR TreeFam; TF324982; -.
DR Reactome; R-RNO-391908; Prostanoid ligand receptors.
DR PRO; PR:P43114; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0004957; F:prostaglandin E receptor activity; IDA:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060348; P:bone development; IDA:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEP:RGD.
DR GO; GO:0042466; P:chemokinesis; IMP:RGD.
DR GO; GO:0097070; P:ductus arteriosus closure; IMP:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0006955; P:immune response; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
DR GO; GO:0060137; P:maternal process involved in parturition; IEP:RGD.
DR GO; GO:0042322; P:negative regulation of circadian sleep/wake cycle, REM sleep; IMP:RGD.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:1904336; P:negative regulation of ductus arteriosus closure; IMP:RGD.
DR GO; GO:1904471; P:negative regulation of endothelin production; IMP:RGD.
DR GO; GO:2000420; P:negative regulation of eosinophil extravasation; ISS:UniProtKB.
DR GO; GO:0010727; P:negative regulation of hydrogen peroxide metabolic process; IMP:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0033624; P:negative regulation of integrin activation; ISS:UniProtKB.
DR GO; GO:0032690; P:negative regulation of interleukin-1 alpha production; IMP:RGD.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IMP:RGD.
DR GO; GO:0002792; P:negative regulation of peptide secretion; IMP:RGD.
DR GO; GO:1904348; P:negative regulation of small intestine smooth muscle contraction; IMP:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:2000388; P:positive regulation of antral ovarian follicle growth; IMP:RGD.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:RGD.
DR GO; GO:1904364; P:positive regulation of calcitonin secretion; IMP:RGD.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IMP:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:1904367; P:positive regulation of chemokinesis; IMP:RGD.
DR GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IMP:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; IMP:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:RGD.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:RGD.
DR GO; GO:1904466; P:positive regulation of matrix metallopeptidase secretion; IMP:RGD.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:RGD.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IMP:RGD.
DR GO; GO:0045778; P:positive regulation of ossification; IMP:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:RGD.
DR GO; GO:2000386; P:positive regulation of ovarian follicle development; IMP:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:RGD.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IMP:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
DR GO; GO:1904460; P:positive regulation of substance P secretion; IMP:RGD.
DR GO; GO:1904496; P:positive regulation of substance P secretion, neurotransmission; IMP:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:RGD.
DR GO; GO:0035810; P:positive regulation of urine volume; IMP:RGD.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:RGD.
DR GO; GO:0010840; P:regulation of circadian sleep/wake cycle, wakefulness; IMP:RGD.
DR GO; GO:0030278; P:regulation of ossification; ISO:RGD.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; ISO:RGD.
DR GO; GO:0009624; P:response to nematode; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0034695; P:response to prostaglandin E; IEP:RGD.
DR GO; GO:1902074; P:response to salt; IEP:RGD.
DR GO; GO:1990785; P:response to water-immersion restraint stress; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042093; P:T-helper cell differentiation; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001758; Prost_EP4_rcpt.
DR InterPro; IPR008365; Prostanoid_rcpt.
DR InterPro; IPR001244; Prostglndn_DP_rcpt.
DR PANTHER; PTHR11866; PTHR11866; 1.
DR PANTHER; PTHR11866:SF6; PTHR11866:SF6; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00428; PROSTAGLNDNR.
DR PRINTS; PR01788; PROSTANOIDR.
DR PRINTS; PR00586; PRSTNOIDEP4R.
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..488
FT /note="Prostaglandin E2 receptor EP4 subtype"
FT /id="PRO_0000070068"
FT TOPO_DOM 1..19
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..160
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..298
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..315
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..335
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 358..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35408"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35408"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35408"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35408"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 214
FT /note="L -> H (in Ref. 2; AAB53326)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="H -> Q (in Ref. 2; AAB53326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 53366 MW; C2EE713018723FF4 CRC64;
MSIPGVNASF SSTPERLNSP VTIPAVMFIF GVVGNLVAIV VLCKSRKEQK ETTFYTLVCG
LAVTDLLGTL LVSPVTIATY MKGQWPGDQA LCDYSTFILL FFGLSGLSII CAMSIERYLA
INHAYFYSHY VDKRLAGLTL FAVYASNVLF CALPNMGLGR SERQYPGTWC FIDWTTNVTA
YAAFSYMYAG FSSFLILATV LCNVLVCGAL LRMLRQFMRR TSLGTEQHHA AAAAAVASVA
CRGHAAASPA LQRLSDFRRR RSFRRIAGAE IQMVILLIAT SLVVLICSIP LVVRVFINQL
YQPSVVKDIS RNPDLQAIRI ASVNPILDPW IYILLRKTVL SKAIEKIKCL FCRIGGSGRD
GSAQHCSESR RTSSAMSGHS RSFLSRELRE ISSTSHTLLY LPDLTESSLG GKNLLPGTHG
MGLTQADTTS LRTLRISETS DSSQGQDSES VLLVDEVSGS QREEPASKGN SLQVTFPSET
LKLSEKCI
