PD2R2_RAT
ID PD2R2_RAT Reviewed; 403 AA.
AC Q6XKD3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Prostaglandin D2 receptor 2;
DE AltName: Full=G protein-coupled receptor 44;
GN Name=Ptgdr2; Synonyms=Crth2, Gpr44;
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 STRAIN=Sprague-Dawley;
RA Encinas J.A., Inbe H., Sugimoto H., Bacon K.B.;
RT "Cloning and characterization of rat CRTH2.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-
CC protein. Receptor activation may result in pertussis toxin-sensitive
CC decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is
CC also implicated in mediating PTGDR2 effects. PGD2 induced receptor
CC internalization. CRTH2 internalization can be regulated by diverse
CC kinases such as, PKC, PKA, GRK2, GPRK5/GRK5 and GRK6. Receptor
CC activation is responsible, at least in part, in immune regulation and
CC allergic/inflammation responses (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Internalized receptors colocalized with
CC RAB11A. {ECO:0000250}.
CC -!- DOMAIN: The 329-DSEL-332 motif is involved in the recycling of PTGDR2
CC to the cell surface after agonist-induced internalization. This motif
CC seems to be required for GRK2 and GPRK5/GRK5 to promote agonist-induced
CC internalization (By similarity). Thr-351 is a major site for PKC-
CC induced internalization of the receptor (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. {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; AY228550; AAP57088.1; -; mRNA.
DR EMBL; CH473953; EDM12854.1; -; Genomic_DNA.
DR RefSeq; NP_001012070.1; NM_001012070.1.
DR RefSeq; XP_006231102.1; XM_006231040.3.
DR RefSeq; XP_008758453.1; XM_008760231.2.
DR RefSeq; XP_017444751.1; XM_017589262.1.
DR RefSeq; XP_017444752.1; XM_017589263.1.
DR RefSeq; XP_017444753.1; XM_017589264.1.
DR AlphaFoldDB; Q6XKD3; -.
DR SMR; Q6XKD3; -.
DR STRING; 10116.ENSRNOP00000066082; -.
DR BindingDB; Q6XKD3; -.
DR ChEMBL; CHEMBL1075112; -.
DR DrugCentral; Q6XKD3; -.
DR GuidetoPHARMACOLOGY; 339; -.
DR GlyGen; Q6XKD3; 3 sites.
DR iPTMnet; Q6XKD3; -.
DR PhosphoSitePlus; Q6XKD3; -.
DR PaxDb; Q6XKD3; -.
DR Ensembl; ENSRNOT00000054808; ENSRNOP00000066082; ENSRNOG00000036631.
DR GeneID; 309212; -.
DR KEGG; rno:309212; -.
DR UCSC; RGD:1311986; rat.
DR CTD; 11251; -.
DR RGD; 1311986; Ptgdr2.
DR eggNOG; ENOG502QTYS; Eukaryota.
DR GeneTree; ENSGT00940000162009; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; Q6XKD3; -.
DR OMA; CPDLCRK; -.
DR OrthoDB; 1102944at2759; -.
DR PhylomeDB; Q6XKD3; -.
DR Reactome; R-RNO-391908; Prostanoid ligand receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q6XKD3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000036631; Expressed in testis and 5 other tissues.
DR Genevisible; Q6XKD3; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0004956; F:prostaglandin D receptor activity; ISS:UniProtKB.
DR GO; GO:0004958; F:prostaglandin F receptor activity; ISO:RGD.
DR GO; GO:0001785; F:prostaglandin J receptor activity; ISO:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein 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..403
FT /note="Prostaglandin D2 receptor 2"
FT /id="PRO_0000415926"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 332..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 329..332
FT /note="Involved in the recycling of CRTH2"
FT /evidence="ECO:0000250"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J6"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 403 AA; 45316 MW; A89A0125DCB29885 CRC64;
MANITLKPLC PLLEEMVQLP NHSNSSLRYI DHVSVLLHGL ASLLGLVENG LILFVVGCRM
RQTVVTTWVL HLALSDLLAA ASLPFFTYFL AVGHSWELGT TFCKLHSSVF FLNMFASGFL
LSAISLDRCL QVVRPVWAQN HRTVAAAHRV CLMLWALAVL NTVPYFVFRD TIPRRDGRIM
CYYNMLLLNP GSDRDTTCDY RQKALAVSKF LLAFMVPLAI IASSHVAVSL QLHHRGRQRT
GRFVRLVAAI VVAFILCWGP YHIFSLLEAR AHSVTTLRQL ASRGLPFVTS LAFFNSVVNP
LLYVLTCPDM LHKLRRSLLT VLESVLVEDS DLSTGPGKRC RRRHRRRASS TTTPASTLLL
ADRFPQLRPA RLIGWMRRGS AELPRRVREQ SQEKQGSLSC TLD
