PD2R_BOVIN
ID PD2R_BOVIN Reviewed; 361 AA.
AC A5D7K8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Prostaglandin D2 receptor;
DE Short=PGD receptor;
DE Short=PGD2 receptor;
DE AltName: Full=Prostanoid DP receptor;
GN Name=PTGDR;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for prostaglandin D2 (PGD2). The activity of this
CC receptor is mainly mediated by G(s) proteins that stimulate adenylate
CC cyclase, resulting in an elevation of intracellular cAMP. A
CC mobilization of calcium is also observed, but without formation of
CC inositol 1,4,5-trisphosphate (By similarity). Involved in PLA2G3-
CC dependent maturation of mast cells. PLA2G3 is secreted by immature mast
CC cells and acts on nearby fibroblasts upstream to PTDGS to synthesize
CC PGD2, which in turn promotes mast cell maturation and degranulation via
CC PTGDR (By similarity). {ECO:0000250|UniProtKB:P70263,
CC ECO:0000250|UniProtKB:Q9R261}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {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; BC140594; AAI40595.1; -; mRNA.
DR RefSeq; NP_001091503.1; NM_001098034.1.
DR AlphaFoldDB; A5D7K8; -.
DR SMR; A5D7K8; -.
DR STRING; 9913.ENSBTAP00000008808; -.
DR PaxDb; A5D7K8; -.
DR GeneID; 515331; -.
DR KEGG; bta:515331; -.
DR CTD; 5729; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_045991_0_2_1; -.
DR InParanoid; A5D7K8; -.
DR OrthoDB; 972015at2759; -.
DR TreeFam; TF324982; -.
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:0004956; F:prostaglandin D receptor activity; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
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; IPR000376; Pglndn_D_rcpt.
DR InterPro; IPR008365; Prostanoid_rcpt.
DR PANTHER; PTHR11866; PTHR11866; 1.
DR PANTHER; PTHR11866:SF14; PTHR11866:SF14; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01788; PROSTANOIDR.
DR PRINTS; PR00854; PRSTNOIDDPR.
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 Mast cell degranulation; Membrane; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..361
FT /note="Prostaglandin D2 receptor"
FT /id="PRO_0000370710"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 361 AA; 40372 MW; DF0C341605C1CAD5 CRC64;
MRPLFYRCHN TTSVEKGNSA TMGGVLFSTG LVGNLLALGL LARSGLGSCP PRSPRPPPSV
FYVLVFGLTI TDLLGKCLVS PFVLSAYAQN RSLRELVPGS DSSLCQAFAF IMSFFGLAST
LQLLAMALEC WLSLGHPFFH RRHLTPRRGA MVAPVVGAFC LAFCALPLVG FGKFVQYCPG
TWCFFQMVHE ERSLSVLSYS VLYASLMLLL VLAIVLCNLS AMRNLYAMHL RLRGLLRPGS
RERAEPGAGE REATPLHLEE LDHLLLLALM TVLFTMCSLP LIYRAYYGAF KAVPEQNGTT
EETEDLRALR FLSVISIVDP WIFIIFRTSV FRMFFRKIFI RPLIYRNWHS NSCQTNMESS
L
