PE2R4_RABIT
ID PE2R4_RABIT Reviewed; 488 AA.
AC Q28691;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney cortex;
RX PubMed=8780252; DOI=10.1152/ajprenal.1996.270.3.f485;
RA Breyer R.M., Davis L.S., Nian C., Redha R., Stillman B., Jacobson H.R.,
RA Breyer M.D.;
RT "Cloning and expression of the rabbit prostaglandin EP4 receptor.";
RL Am. J. Physiol. 270:F485-F493(1996).
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 -!- TISSUE SPECIFICITY: Highly expressed in intestine, duodenal epithelium,
CC uterus, thymus and adrenal cortex. Lower but significant expression in
CC whole adrenal, lung, spleen, stomach, and kidney. In this latter organ,
CC the receptor is localized in the glomeruli and the transitional
CC epithelium of the renal calyx.
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}.
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DR EMBL; L47207; AAC37330.1; -; mRNA.
DR RefSeq; NP_001075728.1; NM_001082259.1.
DR AlphaFoldDB; Q28691; -.
DR SMR; Q28691; -.
DR STRING; 9986.ENSOCUP00000000773; -.
DR BindingDB; Q28691; -.
DR ChEMBL; CHEMBL1926498; -.
DR PRIDE; Q28691; -.
DR Ensembl; ENSOCUT00000000895; ENSOCUP00000000773; ENSOCUG00000000895.
DR GeneID; 100009081; -.
DR KEGG; ocu:100009081; -.
DR CTD; 5734; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244902; -.
DR InParanoid; Q28691; -.
DR OrthoDB; 972015at2759; -.
DR PRO; PR:Q28691; -.
DR Proteomes; UP000001811; Chromosome 11.
DR Bgee; ENSOCUG00000000895; Expressed in blood and 15 other tissues.
DR ExpressionAtlas; Q28691; baseline.
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:0004957; F:prostaglandin E receptor activity; ISS:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0001818; P:negative regulation of cytokine production; IEA:Ensembl.
DR GO; GO:2000420; P:negative regulation of eosinophil extravasation; ISS:UniProtKB.
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:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0030278; P:regulation of ossification; IEA:Ensembl.
DR GO; GO:0051492; P:regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009624; P:response to nematode; IEA:Ensembl.
DR GO; GO:0042093; P:T-helper cell differentiation; IEA:Ensembl.
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_0000070067"
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..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..475
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 CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 488 AA; 53363 MW; F1217B5B0149D3C9 CRC64;
MSTPVANASA SSMPELLNNP VTIPAVMFIF GVVGNLVAIV VLCKSRKEQK ETTFYTLVCG
LAVTDLLGTL LVSPVTIATY MKGQWPGGQA LCDYSTFILL FFGLSGLSII CAMSIERYLA
INHAYFYSHY VDKRLAGLTL FAVYASNVLF CALPNMGLGR SRLQFPDTWC FIDWRTNVTA
HAAFSYMYAG FSSFLILATV LCNVLVCGAL LRMHRQFMRR TSLGTEQHHA AAAAAVTSAA
CRGHPTASPA LPRLSDFRRR RSFRRIAGAE IQMVILLIAT SLVVLICSIP LVVRVFINQL
YQPDLVREIS QNPDLQAIRI ASVNPILDPW IYILLRKTVL SKAIEKIKCL FCRIGGSRRD
RSGQHCSDSR RTSSAMSTHS RSFLSRELKE ISSTSQTLLY LPELSENSLA GRNLLPGVPL
VGLAQADTTS LRTWRGSETS DSSQGQDSES VLLVDEVGGG GRAGPTPKGS SLQVTFPSET
LNLSEKCI
