ID   PD2R_MOUSE              Reviewed;         357 AA.
AC   P70263; A2RSY4; Q8CCM3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Prostaglandin D2 receptor;
DE            Short=PGD receptor;
DE            Short=PGD2 receptor;
DE   AltName: Full=Prostanoid DP receptor;
GN   Name=Ptgdr;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv; TISSUE=Lung;
RX   PubMed=7972033; DOI=10.1073/pnas.91.23.11192;
RA   Hirata M., Kakizuka A., Aizawa M., Ushikubi F., Narumiya S.;
RT   "Molecular characterization of a mouse prostaglandin D receptor and
RT   functional expression of the cloned gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:11192-11196(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23624557; DOI=10.1038/ni.2586;
RA   Taketomi Y., Ueno N., Kojima T., Sato H., Murase R., Yamamoto K.,
RA   Tanaka S., Sakanaka M., Nakamura M., Nishito Y., Kawana M., Kambe N.,
RA   Ikeda K., Taguchi R., Nakamizo S., Kabashima K., Gelb M.H., Arita M.,
RA   Yokomizo T., Nakamura M., Watanabe K., Hirai H., Nakamura M., Okayama Y.,
RA   Ra C., Aritake K., Urade Y., Morimoto K., Sugimoto Y., Shimizu T.,
RA   Narumiya S., Hara S., Murakami M.;
RT   "Mast cell maturation is driven via a group III phospholipase A2-
RT   prostaglandin D2-DP1 receptor paracrine axis.";
RL   Nat. Immunol. 14:554-563(2013).
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 (PubMed:23624557). {ECO:0000250|UniProtKB:Q9R261,
CC       ECO:0000269|PubMed:23624557}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Most abundantly expressed in the ileum, followed by
CC       lung, stomach and uterus.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice show decreased susceptibility to
CC       passive cutaneous anaphylaxis associated with decreased mast cell
CC       degranulation. {ECO:0000269|PubMed:23624557}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AK032488; BAC27895.1; -; mRNA.
DR   EMBL; D29765; BAA06168.1; -; Genomic_DNA.
DR   EMBL; BC132297; AAI32298.1; -; mRNA.
DR   CCDS; CCDS26971.1; -.
DR   PIR; I59269; I59269.
DR   PIR; I80042; I80042.
DR   RefSeq; NP_032988.3; NM_008962.4.
DR   AlphaFoldDB; P70263; -.
DR   SMR; P70263; -.
DR   IntAct; P70263; 1.
DR   STRING; 10090.ENSMUSP00000093653; -.
DR   BindingDB; P70263; -.
DR   ChEMBL; CHEMBL3933; -.
DR   GuidetoPHARMACOLOGY; 338; -.
DR   GlyCosmos; P70263; 2 sites, No reported glycans.
DR   GlyGen; P70263; 2 sites.
DR   PhosphoSitePlus; P70263; -.
DR   PaxDb; 10090-ENSMUSP00000093653; -.
DR   ProteomicsDB; 287897; -.
DR   Antibodypedia; 10764; 233 antibodies from 28 providers.
DR   DNASU; 19214; -.
DR   Ensembl; ENSMUST00000095959.2; ENSMUSP00000093653.2; ENSMUSG00000071489.2.
DR   GeneID; 19214; -.
DR   KEGG; mmu:19214; -.
DR   UCSC; uc007ter.1; mouse.
DR   AGR; MGI:102966; -.
DR   CTD; 5729; -.
DR   MGI; MGI:102966; Ptgdr.
DR   VEuPathDB; HostDB:ENSMUSG00000071489; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244902; -.
DR   HOGENOM; CLU_045991_0_2_1; -.
DR   InParanoid; P70263; -.
DR   OMA; NWHSNSC; -.
DR   OrthoDB; 5355693at2759; -.
DR   PhylomeDB; P70263; -.
DR   TreeFam; TF324982; -.
DR   Reactome; R-MMU-391908; Prostanoid ligand receptors.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   BioGRID-ORCS; 19214; 2 hits in 76 CRISPR screens.
DR   PRO; PR:P70263; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P70263; Protein.
DR   Bgee; ENSMUSG00000071489; Expressed in lumbar dorsal root ganglion and 35 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004956; F:prostaglandin D receptor activity; IDA:MGI.
DR   GO; GO:0001785; F:prostaglandin J receptor activity; IDA:MGI.
DR   GO; GO:0046085; P:adenosine metabolic process; IMP:MGI.
DR   GO; GO:0071799; P:cellular response to prostaglandin D stimulus; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0030238; P:male sex determination; IMP:MGI.
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   GO; GO:0030431; P:sleep; IMP:MGI.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; G-PROTEIN COUPLED RECEPTOR FAMILY 1 MEMBER; 1.
DR   PANTHER; PTHR11866:SF14; PROSTAGLANDIN D2 RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01788; PROSTANOIDR.
DR   PRINTS; PR00854; PRSTNOIDDPR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P70263; MM.
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..357
FT                   /note="Prostaglandin D2 receptor"
FT                   /id="PRO_0000070048"
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..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..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"
FT   CONFLICT        75
FT                   /note="K -> N (in Ref. 1; BAC27895)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   357 AA;  40005 MW;  91CBFF7A5936EB05 CRC64;
     MNESYRCQTS TWVERGSSAT MGAVLFGAGL LGNLLALVLL ARSGLGSCRP GPLHPPPSVF
     YVLVCGLTVT DLLGKCLISP MVLAAYAQNQ SLKELLPASG NQLCETFAFL MSFFGLASTL
     QLLAMAVECW LSLGHPFFYQ RHVTLRRGVL VAPVVAAFCL AFCALPFAGF GKFVQYCPGT
     WCFIQMIHKE RSFSVIGFSV LYSSLMALLV LATVVCNLGA MYNLYDMHRR QRHYPHRCSR
     DRAQSGSDYR HGSLHPLEEL DHFVLLALMT VLFTMCSLPL IYRAYYGAFK LENKAEGDSE
     DLQALRFLSV ISIVDPWIFI IFRTSVFRML FHKVFTRPLI YRNWSSHSQQ SNVESTL
//