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PE2R4_BOVIN
ID   PE2R4_BOVIN             Reviewed;         492 AA.
AC   Q8MJ08;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 104.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12810564; DOI=10.1210/en.2002-0088;
RA   Arosh J.A., Banu S.K., Chapdelaine P., Emond V., Kim J.J., MacLaren L.A.,
RA   Fortier M.A.;
RT   "Molecular cloning and characterization of bovine prostaglandin E2
RT   receptors EP2 and EP4: expression and regulation in endometrium and
RT   myometrium during the estrous cycle and early pregnancy.";
RL   Endocrinology 144:3076-3091(2003).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FEM1A. {ECO:0000250|UniProtKB:P35408}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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; AF539403; AAN01235.1; -; mRNA.
DR   RefSeq; NP_777014.1; NM_174589.2.
DR   AlphaFoldDB; Q8MJ08; -.
DR   SMR; Q8MJ08; -.
DR   STRING; 9913.ENSBTAP00000019930; -.
DR   PaxDb; Q8MJ08; -.
DR   GeneID; 282331; -.
DR   KEGG; bta:282331; -.
DR   CTD; 5734; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q8MJ08; -.
DR   OrthoDB; 972015at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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:0004957; F:prostaglandin E receptor activity; ISS:UniProtKB.
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:0071380; P:cellular response to prostaglandin E stimulus; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
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:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
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..492
FT                   /note="Prostaglandin E2 receptor EP4 subtype"
FT                   /id="PRO_0000289298"
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..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..301
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..318
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..338
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..492
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          361..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35408"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35408"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35408"
FT   MOD_RES         388
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"
SQ   SEQUENCE   492 AA;  53298 MW;  E9119F5E72D00873 CRC64;
     MSIPGTNASS SQASNPLNSP VTIPAVMFIF GVVGNLVAIV VLCKSRKEQK ETTFYTLVCG
     LAVTDLLGTL LVSPVTIATY LKGQWPGGHA LCEYSTFILL FFGLSGLSII CAMSIERYLA
     INHAYFYSHY VDKRLAGLTL FAVYASNVLF CALPSMGLGS SRLQYPATWC FIDWTTNVTA
     HAAFSYMYAG FSSFLILATV LCNVLVCGAL LRMHRQFMRR TSLGTEQQHH AAAAAVALAP
     TACRAPPAAS SPALPRLSDF RRRRSFRRIA GAEIQMVILL IATSLVVLIC SIPLVVRVFV
     NQLYRPQLEP VIGKNPDLQA IRIASVSPIL DPWIYILLRK TVLSKAIEKI KCLFCRIGGS
     RRERSGPHCS DSRRTSSAVS GHSRSFLSRE LKEISSTSQT LLYTPELSEN GLGGGRNLLP
     GVPGVGLTQI DSTSLRTLRI SETSDSSQGQ DSESFLLVDE VGGSCRAGPA PKGSSLQVTF
     PSETLNLSEK CI
 
 
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