ID HPGDS_HUMAN Reviewed; 199 AA. AC O60760; Q6FHT9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 14-OCT-2015, entry version 150. DE RecName: Full=Hematopoietic prostaglandin D synthase; DE Short=H-PGDS; DE EC=5.3.99.2; DE AltName: Full=GST class-sigma; DE AltName: Full=Glutathione S-transferase; DE EC=2.5.1.18; 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; Synonyms=GSTS, PGDS, PTGDS2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC RP ACTIVITY, COFACTOR, AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=10824118; DOI=10.1046/j.1432-1327.2000.01362.x; RA Kanaoka Y., Fujimori K., Kikuno R., Sakaguchi Y., Urade Y., RA 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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=11672424; DOI=10.1042/0264-6021:3590507; RA Jowsey I.R., Thomson A.M., Flanagan J.U., Murdock P.R., Moore G.B., RA Meyer D.J., Murphy G.J., Smith S.A., Hayes J.D.; RT "Mammalian class Sigma glutathione S-transferases: catalytic RT properties and tissue-specific expression of human and rat GSH- RT dependent prostaglandin D2 synthases."; RL Biochem. J. 359:507-516(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Substantia nigra; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND INDUCTION. RC TISSUE=Megakaryocyte; RX PubMed=9425264; DOI=10.1006/bbrc.1997.7803; RA Suzuki T., Watanabe K., Kanaoka Y., Sato T., Hayaishi O.; RT "Induction of hematopoietic prostaglandin D synthase in human RT megakaryocytic cells by phorbol ester."; RL Biochem. Biophys. Res. Commun. 241:288-293(1997). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Megakaryocyte; RX PubMed=9353279; DOI=10.1074/jbc.272.45.28263; RA Mahmud I., Ueda N., Yamaguchi H., Yamashita R., Yamamoto S., RA Kanaoka Y., Urade Y., Hayaishi O.; RT "Prostaglandin D synthase in human megakaryoblastic cells."; RL J. Biol. Chem. 272:28263-28266(1997). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH CALCIUM IONS; RP MAGNESIUM IONS AND GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, ENZYME RP REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF RP ASP-93; ASP-96 AND ASP-97. RX PubMed=12627223; DOI=10.1038/nsb907; RA Inoue T., Irikura D., Okazaki N., Kinugasa S., Matsumura H., RA Uodome N., Yamamoto M., Kumasaka T., Miyano M., Kai Y., Urade Y.; RT "Mechanism of metal activation of human hematopoietic prostaglandin D RT synthase."; RL Nat. Struct. Biol. 10:291-296(2003). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS RP AND THE SYNTHETIC INHIBITOR BSBT, FUNCTION, SUBUNIT, CATALYTIC RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15113825; DOI=10.1093/jb/mvh033; RA Inoue T., Okano Y., Kado Y., Aritake K., Irikura D., Uodome N., RA Okazaki N., Kinugasa S., Shishitani H., Matsumura H., Kai Y., RA Urade Y.; RT "First determination of the inhibitor complex structure of human RT hematopoietic prostaglandin D synthase."; RL J. Biochem. 135:279-283(2004). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE; RP MAGNESIUM IONS AND THE SYNTHETIC INHIBITOR HQL-79, FUNCTION, AND RP CATALYTIC ACTIVITY. 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 RT selective inhibitor of human hematopoietic prostaglandin D synthase."; RL J. Biol. Chem. 281:15277-15286(2006). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH SYNTHETIC RP INHIBITORS, AND SUBUNIT. RX PubMed=18341273; DOI=10.1021/jm701509k; RA Hohwy M., Spadola L., Lundquist B., Hawtin P., Dahmen J., RA Groth-Clausen I., Nilsson E., Persdotter S., von Wachenfeldt K., RA Folmer R.H., Edman K.; RT "Novel prostaglandin D synthase inhibitors generated by fragment-based RT drug design."; RL J. Med. Chem. 51:2178-2186(2008). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH SYNTHETIC RP INHIBITOR, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=19939518; DOI=10.1016/j.ejmech.2009.10.025; RA Weber J.E., Oakley A.J., Christ A.N., Clark A.G., Hayes J.D., Hall R., RA Hume D.A., Board P.G., Smythe M.L., Flanagan J.U.; RT "Identification and characterisation of new inhibitors for the human RT hematopoietic prostaglandin D2 synthase."; RL Eur. J. Med. Chem. 45:447-454(2010). CC -!- FUNCTION: Bifunctional enzyme which catalyzes both the conversion CC of PGH2 to PGD2, a prostaglandin involved in smooth muscle CC contraction/relaxation and a potent inhibitor of platelet CC aggregation, and the conjugation of glutathione with a wide range CC of aryl halides and organic isothiocyanates. Also exhibits low CC glutathione-peroxidase activity towards cumene hydroperoxide. CC {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, CC ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:19939518, CC ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}. CC -!- CATALYTIC ACTIVITY: (5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15- CC hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy- CC 11-oxoprosta-5,13-dienoate. CC -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione. CC -!- COFACTOR: CC Name=glutathione; Xref=ChEBI:CHEBI:57925; CC Evidence={ECO:0000269|PubMed:10824118, CC ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:9353279, CC ECO:0000269|PubMed:9425264}; CC Note=Glutathione is required for the prostaglandin D synthase CC activity. {ECO:0000269|PubMed:10824118, CC ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:9353279, CC ECO:0000269|PubMed:9425264}; CC -!- ENZYME REGULATION: Prostaglandin PGD2 synthesis is stimulated by CC calcium and magnesium ions. One calcium or magnesium ion is bound CC between the subunits of the homodimer. The interactions with the CC protein are for the most part mediated via water molecules. CC Magnesium increases the affinity for glutathione, while calcium CC has no effect on the affinity for glutathione. CC {ECO:0000269|PubMed:12627223}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8 mM for glutathione for the glutathione-conjugating activity CC {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, CC ECO:0000269|PubMed:15113825}; CC KM=0.6 mM for glutathione for the prostaglandin D synthase CC activity in the presence of EDTA {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; CC KM=0.14 mM for glutathione for the prostaglandin D synthase CC activity in the presence of magnesium ions CC {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, CC ECO:0000269|PubMed:15113825}; CC Vmax=8.6 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as CC substrate {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; CC Vmax=5.1 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as CC substrate {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; CC Vmax=44.3 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as CC substrate {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; CC Vmax=10.7 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as CC substrate {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; CC Vmax=6.8 umol/min/mg enzyme with allyl isothiocyanate as CC substrate {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; CC Vmax=6.3 umol/min/mg enzyme with benzyl isothiocyanate as CC substrate {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; CC Vmax=0.05 umol/min/mg enzyme with cumene hydroperoxide as CC substrate {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12627223, CC ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, CC ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518}. CC -!- INTERACTION: CC Q96GS6:ABHD17A; NbExp=3; IntAct=EBI-10187349, EBI-2870273; CC Q96B67:ARRDC3; NbExp=3; IntAct=EBI-10187349, EBI-2875665; CC P08582-2:MFI2; NbExp=3; IntAct=EBI-10187349, EBI-10195914; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353279}. CC -!- TISSUE SPECIFICITY: Expressed in a number of megakaryocytic cell CC lines but not in platelets. Highly expressed in adipose tissue, CC macrophages and placenta. Also expressed at lower levels in lung, CC heart, lymph nodes, appendix, bone marrow and fetal liver. CC {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}. CC -!- DEVELOPMENTAL STAGE: Highest levels in immature megakaryocytic CC cells. Disappears after final differentiation to platelets. CC {ECO:0000269|PubMed:9425264}. CC -!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA). CC {ECO:0000269|PubMed:9425264}. CC -!- SIMILARITY: Belongs to the GST superfamily. Sigma family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GST C-terminal domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GST N-terminal domain. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D82073; BAA25545.1; -; mRNA. DR EMBL; AB008830; BAA96854.1; -; Genomic_DNA. DR EMBL; AK290075; BAF82764.1; -; mRNA. DR EMBL; CR541662; CAG46463.1; -; mRNA. DR EMBL; CR541679; CAG46480.1; -; mRNA. DR EMBL; CH471057; EAX06052.1; -; Genomic_DNA. DR EMBL; BC020734; AAH20734.1; -; mRNA. DR CCDS; CCDS3640.1; -. DR RefSeq; NP_055300.1; NM_014485.2. DR UniGene; Hs.128433; -. DR PDB; 1IYH; X-ray; 1.70 A; A/B/C/D=2-199. DR PDB; 1IYI; X-ray; 1.80 A; A/B/C/D=2-199. DR PDB; 1V40; X-ray; 1.90 A; A/B/C/D=2-199. DR PDB; 2CVD; X-ray; 1.45 A; A/B/C/D=2-199. DR PDB; 2VCQ; X-ray; 1.95 A; A/B/C/D=1-199. DR PDB; 2VCW; X-ray; 1.95 A; A/B/C/D=1-199. DR PDB; 2VCX; X-ray; 2.10 A; A/B/C/D=1-199. DR PDB; 2VCZ; X-ray; 1.95 A; A/B/C/D=1-199. DR PDB; 2VD0; X-ray; 2.20 A; A/B/C/D=1-199. DR PDB; 2VD1; X-ray; 2.25 A; A/B/C/D=1-199. DR PDB; 3EE2; X-ray; 1.91 A; A/B=1-199. DR PDB; 3KXO; X-ray; 2.10 A; A/B=1-199. DR PDB; 3VI5; X-ray; 2.00 A; A/B/C/D=2-199. DR PDB; 3VI7; X-ray; 2.00 A; A/B/C/D=2-199. DR PDB; 4EC0; X-ray; 1.85 A; A/B=1-199. DR PDB; 4EDY; X-ray; 1.72 A; A/B=2-199. DR PDB; 4EDZ; X-ray; 2.00 A; A/B/C/D=2-199. DR PDB; 4EE0; X-ray; 1.75 A; A/B=2-199. DR PDB; 5AIS; X-ray; 1.85 A; A/B/C/D=2-199. DR PDB; 5AIV; X-ray; 2.04 A; A/B/C/D=2-199. DR PDB; 5AIX; X-ray; 2.10 A; A/B/C/D=2-199. DR PDBsum; 1IYH; -. DR PDBsum; 1IYI; -. DR PDBsum; 1V40; -. DR PDBsum; 2CVD; -. DR PDBsum; 2VCQ; -. DR PDBsum; 2VCW; -. DR PDBsum; 2VCX; -. DR PDBsum; 2VCZ; -. DR PDBsum; 2VD0; -. DR PDBsum; 2VD1; -. DR PDBsum; 3EE2; -. DR PDBsum; 3KXO; -. DR PDBsum; 3VI5; -. DR PDBsum; 3VI7; -. DR PDBsum; 4EC0; -. DR PDBsum; 4EDY; -. DR PDBsum; 4EDZ; -. DR PDBsum; 4EE0; -. DR PDBsum; 5AIS; -. DR PDBsum; 5AIV; -. DR PDBsum; 5AIX; -. DR ProteinModelPortal; O60760; -. DR SMR; O60760; 2-199. DR BioGrid; 118128; 4. DR IntAct; O60760; 3. DR STRING; 9606.ENSP00000295256; -. DR BindingDB; O60760; -. DR ChEMBL; CHEMBL5879; -. DR DrugBank; DB00143; Glutathione. DR GuidetoPHARMACOLOGY; 1381; -. DR PhosphoSite; O60760; -. DR BioMuta; HPGDS; -. DR PaxDb; O60760; -. DR PRIDE; O60760; -. DR Ensembl; ENST00000295256; ENSP00000295256; ENSG00000163106. DR GeneID; 27306; -. DR KEGG; hsa:27306; -. DR UCSC; uc003hte.1; human. DR CTD; 27306; -. DR GeneCards; HPGDS; -. DR HGNC; HGNC:17890; HPGDS. DR HPA; CAB020805; -. DR HPA; HPA024035; -. DR MIM; 602598; gene. DR neXtProt; NX_O60760; -. DR PharmGKB; PA165664133; -. DR eggNOG; NOG122057; -. DR GeneTree; ENSGT00670000097856; -. DR HOGENOM; HOG000115733; -. DR HOVERGEN; HBG105321; -. DR InParanoid; O60760; -. DR KO; K01830; -. DR OMA; TEMEQCH; -. DR OrthoDB; EOG78WKT1; -. DR PhylomeDB; O60760; -. DR TreeFam; TF105321; -. DR BioCyc; MetaCyc:HS08788-MONOMER; -. DR BRENDA; 2.5.1.18; 2681. DR BRENDA; 5.3.99.2; 2681. DR Reactome; R-HSA-156590; Glutathione conjugation. DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX). DR SABIO-RK; O60760; -. DR EvolutionaryTrace; O60760; -. DR GeneWiki; PGDS; -. DR GenomeRNAi; 27306; -. DR NextBio; 50305; -. DR PRO; PR:O60760; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; O60760; -. DR Genevisible; O60760; HS. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0004667; F:prostaglandin-D synthase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome. DR GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome. DR GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome. DR GO; GO:0007626; P:locomotory behavior; TAS:ProtInc. DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl. DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF02798; GST_N; 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 3D-structure; Calcium; Complete proteome; Cytoplasm; KW Fatty acid biosynthesis; Fatty acid metabolism; Isomerase; KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; KW Prostaglandin biosynthesis; Prostaglandin metabolism; KW Reference proteome; Transferase. FT CHAIN 1 199 Hematopoietic prostaglandin D synthase. FT /FTId=PRO_0000185934. FT DOMAIN 2 79 GST N-terminal. FT DOMAIN 81 199 GST C-terminal. FT REGION 63 64 Glutathione binding. FT BINDING 8 8 Glutathione. FT {ECO:0000269|PubMed:16547010}. FT BINDING 14 14 Glutathione. FT {ECO:0000269|PubMed:16547010}. FT BINDING 39 39 Glutathione. FT {ECO:0000269|PubMed:16547010}. FT BINDING 51 51 Glutathione; via amide nitrogen and FT carbonyl oxygen. FT {ECO:0000269|PubMed:16547010}. FT MUTAGEN 93 93 D->N: Loss of activation by calcium or FT magnesium ions. FT {ECO:0000269|PubMed:12627223}. FT MUTAGEN 96 96 D->N: Increases PGD2 synthesis. Loss of FT activation by calcium or magnesium ions. FT {ECO:0000269|PubMed:12627223}. FT MUTAGEN 97 97 D->N: Reduces PGD2 synthesis by 99%. Loss FT of activation by calcium or magnesium FT ions. {ECO:0000269|PubMed:12627223}. FT CONFLICT 187 187 V -> I (in Ref. 2; no nucleotide entry). FT {ECO:0000305}. FT STRAND 4 12 {ECO:0000244|PDB:2CVD}. FT HELIX 13 15 {ECO:0000244|PDB:2CVD}. FT HELIX 16 24 {ECO:0000244|PDB:2CVD}. FT STRAND 30 34 {ECO:0000244|PDB:2CVD}. FT HELIX 36 38 {ECO:0000244|PDB:2CVD}. FT HELIX 39 43 {ECO:0000244|PDB:2CVD}. FT STRAND 46 49 {ECO:0000244|PDB:1IYH}. FT STRAND 53 56 {ECO:0000244|PDB:2CVD}. FT STRAND 59 62 {ECO:0000244|PDB:2CVD}. FT HELIX 64 72 {ECO:0000244|PDB:2CVD}. FT HELIX 76 78 {ECO:0000244|PDB:5AIS}. FT HELIX 82 100 {ECO:0000244|PDB:2CVD}. FT HELIX 109 121 {ECO:0000244|PDB:2CVD}. FT HELIX 123 135 {ECO:0000244|PDB:2CVD}. FT STRAND 139 142 {ECO:0000244|PDB:2CVD}. FT HELIX 148 163 {ECO:0000244|PDB:2CVD}. FT TURN 165 170 {ECO:0000244|PDB:2CVD}. FT HELIX 172 182 {ECO:0000244|PDB:2CVD}. FT HELIX 185 193 {ECO:0000244|PDB:2CVD}. SQ SEQUENCE 199 AA; 23344 MW; A4ED2476B16CC5C3 CRC64; MPNYKLTYFN MRGRAEIIRY IFAYLDIQYE DHRIEQADWP EIKSTLPFGK IPILEVDGLT LHQSLAIARY LTKNTDLAGN TEMEQCHVDA IVDTLDDFMS CFPWAEKKQD VKEQMFNELL TYNAPHLMQD LDTYLGGREW LIGNSVTWAD FYWEICSTTL LVFKPDLLDN HPRLVTLRKK VQAIPAVANW IKRRPQTKL //