PD2RL_RAT
ID PD2RL_RAT Reviewed; 357 AA.
AC O35932;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Prostaglandin D2 receptor-like;
DE Short=PGD receptor-like;
DE Short=PGD2 receptor-like;
DE AltName: Full=Prostanoid DP receptor-like;
GN Name=Ptgdrl; Synonyms=Ptgdr2;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Retina;
RX PubMed=9721719; DOI=10.1046/j.1471-4159.1998.71030937.x;
RA Gerashchenko D., Beuckmann C.T., Kanaoka Y., Eguchi N., Gordon W.C.,
RA Urade Y., Bazan N.G., Hayaishi O.;
RT "Dominant expression of rat prostanoid DP receptor mRNA in leptomeninges,
RT inner segments of photoreceptor cells, iris epithelium, and ciliary
RT processes.";
RL J. Neurochem. 71:937-945(1998).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=6302737; DOI=10.1016/0090-6980(83)90131-4;
RA Town M.H., Casals-Stenzel J., Schillinger E.;
RT "Pharmacological and cardiovascular properties of a hydantoin derivative,
RT BW 245 C, with high affinity and selectivity for PGD2 receptors.";
RL Prostaglandins 25:13-28(1983).
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). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in eye and gastrointestinal
CC tract (GIT), moderately in the brain and oviduct and weakly in the
CC epididymis. In the eye, expressed in the epithelium of the iris and
CC ciliary body and in photoreceptor cells of the retina. In the brain,
CC expressed in leptomeninges, choroid plexus and spinal cord (sensory and
CC motor neurons of the dorsal and ventral horns). In the stomach,
CC expressed in the mucous-secreting goblet cells and the columnar
CC epithelium. Expressed in platelets. {ECO:0000269|PubMed:6302737,
CC ECO:0000269|PubMed:9721719}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U92289; AAB71762.1; -; mRNA.
DR RefSeq; NP_071577.1; NM_022241.1.
DR AlphaFoldDB; O35932; -.
DR SMR; O35932; -.
DR GlyGen; O35932; 2 sites.
DR GeneID; 63889; -.
DR KEGG; rno:63889; -.
DR CTD; 5729; -.
DR RGD; 1565108; Ptgdrl.
DR InParanoid; O35932; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; O35932; -.
DR Reactome; R-RNO-391908; Prostanoid ligand receptors.
DR PRO; PR:O35932; -.
DR Proteomes; UP000002494; 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:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0051239; P:regulation of multicellular organismal process; IEA:UniProt.
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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..357
FT /note="Prostaglandin D2 receptor-like"
FT /id="PRO_0000370712"
FT TOPO_DOM 1..20
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 357 AA; 39803 MW; DB966276DD68184C CRC64;
MNESYRCQAA TWVERGSSAT MGGVLFSAGL LGNLLALVLL ARSGLGSCRP GPLHPPPSVF
YVLVCGLTVT HLLGKCLISP MVLAAYAQNR SLKELLPASG NQLCEAFAFL MSFFGLASTL
QLLAMALECW LSLGHPFFYQ RHITARRGVL VAPVAGAFSL AFCALPFAGF GKFVQYCPGT
WCFIQMIHKK RSFSVIGFSV LYSSLMALLV LATVVCNLGA MSNLYAMHRR QRHHPRRCSR
DRAQSGSDYR HGSPNPLEEL DHFVLLALTT VLFTMCSLPL IYRAYYGAFK LVDRADGDSE
DLQALRFLSV ISIVDPWIFI IFRTSVFRML FHKAFTRPLI YRNWCSHSWQ TNMESTL
