PD2R2_MOUSE
ID PD2R2_MOUSE Reviewed; 382 AA.
AC Q9Z2J6; Q54A00;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Prostaglandin D2 receptor 2;
DE AltName: Full=Chemoattractant receptor-homologous molecule expressed on Th2 cells;
DE AltName: Full=G-protein coupled receptor 44;
DE AltName: CD_antigen=CD294;
GN Name=Ptgdr2; Synonyms=Crth2, Gpr44;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9931443; DOI=10.1016/s0378-1119(98)00599-x;
RA Abe H., Takeshita T., Nagata K., Arita T., Endo Y., Fujita T., Takayama H.,
RA Kubo M., Sugamura K.;
RT "Molecular cloning, chromosome mapping and characterization of the mouse
RT CRTH2 gene, a putative member of the leukocyte chemoattractant receptor
RT family.";
RL Gene 227:71-77(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION AS RECEPTOR FOR PGD2,
RP AND CHARACTERIZATION.
RX PubMed=12878180; DOI=10.1016/s0006-291x(03)01266-x;
RA Hirai H., Abe H., Tanaka K., Takatsu K., Sugamura K., Nakamura M.,
RA Nagata K.;
RT "Gene structure and functional properties of mouse CRTH2, a prostaglandin
RT D2 receptor.";
RL Biochem. Biophys. Res. Commun. 307:797-802(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16888024; DOI=10.4049/jimmunol.177.4.2621;
RA Satoh T., Moroi R., Aritake K., Urade Y., Kanai Y., Sumi K., Yokozeki H.,
RA Hirai H., Nagata K., Hara T., Utsuyama M., Hirokawa K., Sugamura K.,
RA Nishioka K., Nakamura M.;
RT "Prostaglandin D2 plays an essential role in chronic allergic inflammation
RT of the skin via CRTH2 receptor.";
RL J. Immunol. 177:2621-2629(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 ECO:0000269|PubMed:12878180, ECO:0000269|PubMed:16888024}.
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-346 is a major site for PKC-
CC induced internalization of the receptor (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are fertile and grew normally.
CC Ear-swelling responses induced by hapten-specific IgE are less
CC pronounced in deficient mice, giving 35-55% of the responses of normal
CC mice. The reduction in cutaneous responses is associated with decreased
CC infiltration of lymphocytes, eosinophils, and basophils and decreased
CC production of macrophage-derived chemokine and RANTES at inflammatory
CC sites. In models of chronic contact hypersensitivity induced by
CC repeated hapten application, CRTH2-deficient mice result in a reduction
CC by approximately half of skin responses and low levels (63% of control)
CC of serum IgE production. {ECO:0000269|PubMed:16888024}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF054507; AAD13525.1; -; Genomic_DNA.
DR EMBL; AB109091; BAC81436.1; -; Genomic_DNA.
DR EMBL; AB109092; BAC81437.1; -; mRNA.
DR EMBL; CH466534; EDL41395.1; -; Genomic_DNA.
DR EMBL; BC111906; AAI11907.1; -; mRNA.
DR CCDS; CCDS29592.1; -.
DR RefSeq; NP_034092.1; NM_009962.3.
DR RefSeq; XP_006526758.1; XM_006526695.3.
DR RefSeq; XP_006526759.1; XM_006526696.3.
DR RefSeq; XP_011245450.1; XM_011247148.2.
DR AlphaFoldDB; Q9Z2J6; -.
DR SMR; Q9Z2J6; -.
DR STRING; 10090.ENSMUSP00000036159; -.
DR BindingDB; Q9Z2J6; -.
DR ChEMBL; CHEMBL2291; -.
DR DrugCentral; Q9Z2J6; -.
DR GuidetoPHARMACOLOGY; 339; -.
DR GlyGen; Q9Z2J6; 3 sites.
DR iPTMnet; Q9Z2J6; -.
DR PhosphoSitePlus; Q9Z2J6; -.
DR PaxDb; Q9Z2J6; -.
DR PRIDE; Q9Z2J6; -.
DR ProteomicsDB; 289331; -.
DR Antibodypedia; 2960; 623 antibodies from 39 providers.
DR DNASU; 14764; -.
DR Ensembl; ENSMUST00000037261; ENSMUSP00000036159; ENSMUSG00000034117.
DR GeneID; 14764; -.
DR KEGG; mmu:14764; -.
DR UCSC; uc008gri.1; mouse.
DR CTD; 11251; -.
DR MGI; MGI:1330275; Ptgdr2.
DR VEuPathDB; HostDB:ENSMUSG00000034117; -.
DR eggNOG; ENOG502QTYS; Eukaryota.
DR GeneTree; ENSGT00940000162009; -.
DR HOGENOM; CLU_009579_8_0_1; -.
DR InParanoid; Q9Z2J6; -.
DR OMA; CPDLCRK; -.
DR OrthoDB; 1102944at2759; -.
DR PhylomeDB; Q9Z2J6; -.
DR TreeFam; TF330976; -.
DR Reactome; R-MMU-391908; Prostanoid ligand receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 14764; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9Z2J6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9Z2J6; protein.
DR Bgee; ENSMUSG00000034117; Expressed in tracheobronchial tree and 11 other tissues.
DR Genevisible; Q9Z2J6; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0004958; F:prostaglandin F receptor activity; IDA:MGI.
DR GO; GO:0001785; F:prostaglandin J receptor activity; IDA:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:MGI.
DR GO; GO:0006935; P:chemotaxis; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:MGI.
DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; IMP:MGI.
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; IDA:MGI.
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..382
FT /note="Prostaglandin D2 receptor 2"
FT /id="PRO_0000069573"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..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..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..307
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:Q6XKD3"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 382 AA; 42950 MW; 8CCB898B93795B04 CRC64;
MANVTLKPLC PLLEEMVQLP NHSNSSLRYI DHVSVLLHGL ASLLGLVENG LILFVVGCRM
RQTVVTTWVL HLALSDLLAA ASLPFFTYFL AVGHSWELGT TFCKLHSSVF FLNMFASGFL
LSAISLDRCL QVVRPVWAQN HRTVAVAHRV CLMLWALAVL NTIPYFVFRD TIPRLDGRIM
CYYNLLLWNP GPDRDTTCDY RQKALAVSKF LLAFMVPLAI IASSHVAVSL RLHHRGRQRT
GRFVRLVAAI VVAFVLCWGP YHIFSLLEAR AHSVTTLRQL ASRGLPFVTS LAFFNSVVNP
LLYVFTCPDM LYKLRRSLRA VLESVLVEDS DQSGGLRNRR RRASSTATPA STLLLADRIP
QLRPTRLIGW MRRGSAEVPQ RV
