HPGDS_MOUSE
ID HPGDS_MOUSE Reviewed; 199 AA.
AC Q9JHF7; Q14AR4; Q8CA80;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Hematopoietic prostaglandin D synthase;
DE Short=H-PGDS;
DE EC=5.3.99.2 {ECO:0000269|PubMed:10824118};
DE AltName: Full=GST class-sigma;
DE AltName: Full=Glutathione S-transferase;
DE EC=2.5.1.18 {ECO:0000269|PubMed:10824118};
DE AltName: Full=Glutathione-dependent PGD synthase;
DE AltName: Full=Glutathione-requiring prostaglandin D synthase;
DE AltName: Full=Prostaglandin-H2 D-isomerase;
GN Name=Hpgds {ECO:0000312|MGI:MGI:1859384}; Synonyms=Gsts, Pgds, Ptgds2;
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 / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv, and C57BL/6J; TISSUE=Oviduct;
RX PubMed=10824118; DOI=10.1046/j.1432-1327.2000.01362.x;
RA Kanaoka Y., Fujimori K., Kikuno R., Sakaguchi Y., Urade Y., Hayaishi O.;
RT "Structure and chromosomal localization of human and mouse genes for
RT hematopoietic prostaglandin D synthase.";
RL Eur. J. Biochem. 267:3315-3322(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, and Spinal cord;
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 [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].
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 [5]
RP FUNCTION.
RX PubMed=16547010; DOI=10.1074/jbc.m506431200;
RA Aritake K., Kado Y., Inoue T., Miyano M., Urade Y.;
RT "Structural and functional characterization of HQL-79, an orally selective
RT inhibitor of human hematopoietic prostaglandin D synthase.";
RL J. Biol. Chem. 281:15277-15286(2006).
RN [6]
RP IDENTIFICATION BY 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: Bifunctional enzyme which catalyzes both the conversion of
CC PGH2 to PGD2, a prostaglandin involved in smooth muscle
CC contraction/relaxation and a potent inhibitor of platelet aggregation,
CC and the conjugation of glutathione with a wide range of aryl halides
CC and organic isothiocyanates. Also exhibits low glutathione-peroxidase
CC activity. {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:16547010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2;
CC Evidence={ECO:0000269|PubMed:10824118};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10601;
CC Evidence={ECO:0000305|PubMed:10824118};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:10824118};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin D2;
CC Xref=Rhea:RHEA:51232, ChEBI:CHEBI:85166, ChEBI:CHEBI:133979;
CC Evidence={ECO:0000250|UniProtKB:O60760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51233;
CC Evidence={ECO:0000250|UniProtKB:O60760};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000269|PubMed:10824118};
CC Note=Glutathione is required for the prostaglandin D synthase activity.
CC {ECO:0000269|PubMed:10824118};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Expressed in skin and oviduct.
CC {ECO:0000269|PubMed:10824118}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC {ECO:0000305}.
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DR EMBL; AB008824; BAA97557.1; -; Genomic_DNA.
DR EMBL; D82072; BAA96845.1; -; mRNA.
DR EMBL; AK020246; BAB32037.1; -; mRNA.
DR EMBL; AK039392; BAC30336.1; -; mRNA.
DR EMBL; CH466523; EDK98774.1; -; Genomic_DNA.
DR EMBL; BC116735; AAI16736.1; -; mRNA.
DR EMBL; BC116737; AAI16738.1; -; mRNA.
DR CCDS; CCDS20205.1; -.
DR RefSeq; NP_062328.3; NM_019455.4.
DR AlphaFoldDB; Q9JHF7; -.
DR SMR; Q9JHF7; -.
DR STRING; 10090.ENSMUSP00000031982; -.
DR BindingDB; Q9JHF7; -.
DR ChEMBL; CHEMBL3309049; -.
DR SwissLipids; SLP:000000829; -.
DR iPTMnet; Q9JHF7; -.
DR PhosphoSitePlus; Q9JHF7; -.
DR MaxQB; Q9JHF7; -.
DR PaxDb; Q9JHF7; -.
DR PeptideAtlas; Q9JHF7; -.
DR PRIDE; Q9JHF7; -.
DR ProteomicsDB; 267014; -.
DR Antibodypedia; 14738; 109 antibodies from 27 providers.
DR DNASU; 54486; -.
DR Ensembl; ENSMUST00000031982; ENSMUSP00000031982; ENSMUSG00000029919.
DR GeneID; 54486; -.
DR KEGG; mmu:54486; -.
DR UCSC; uc009cee.2; mouse.
DR CTD; 27306; -.
DR MGI; MGI:1859384; Hpgds.
DR VEuPathDB; HostDB:ENSMUSG00000029919; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000160278; -.
DR HOGENOM; CLU_039475_1_0_1; -.
DR InParanoid; Q9JHF7; -.
DR OMA; ELEQCEV; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; Q9JHF7; -.
DR TreeFam; TF105321; -.
DR BRENDA; 5.3.99.2; 3474.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR SABIO-RK; Q9JHF7; -.
DR BioGRID-ORCS; 54486; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Hpgds; mouse.
DR PRO; PR:Q9JHF7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JHF7; protein.
DR Bgee; ENSMUSG00000029919; Expressed in undifferentiated genital tubercle and 110 other tissues.
DR Genevisible; Q9JHF7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004667; F:prostaglandin-D synthase activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; IGI:MGI.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:MGI.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome; Transferase.
FT CHAIN 1..199
FT /note="Hematopoietic prostaglandin D synthase"
FT /id="PRO_0000185935"
FT DOMAIN 2..79
FT /note="GST N-terminal"
FT DOMAIN 81..199
FT /note="GST C-terminal"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 49..51
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 63..64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT CONFLICT 108
FT /note="D -> G (in Ref. 2; BAC30336)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 23227 MW; E5E7E4B56493F720 CRC64;
MPNYKLLYFN MRGRAEIIRY IFAYLDIKYE DHRIEQADWP KIKPTLPFGK IPVLEVEGLT
IHQSLAIARY LTKNTDLAGK TALEQCQADA VVDTLDDFMS LFPWAEKDQD LKERMFNELL
THQAPRLLKD LDTYLGDKEW FIGNYVTWAD FYWDICSTTL LVLKPGLLDI YPKLVSLRNK
VQAIPAISAW ILKRPQTKL
