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 09-APR-2025, entry version 209. DE RecName: Full=Hematopoietic prostaglandin D synthase {ECO:0000305}; DE Short=H-PGDS; DE EC=5.3.99.2 {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:19939518, ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}; DE AltName: Full=GST class-sigma; DE AltName: Full=Glutathione S-transferase; DE EC=2.5.1.18 {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:15113825}; 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|HGNC:HGNC:17890}; Synonyms=GSTS, PGDS, PTGDS2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, RP 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., 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 properties and RT tissue-specific expression of human and rat GSH-dependent prostaglandin D2 RT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, DEVELOPMENTAL RP 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 TISSUE RP 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., Kanaoka Y., RA Urade Y., Hayaishi O.; RT "Prostaglandin D synthase in human megakaryoblastic cells."; RL J. Biol. Chem. 272:28263-28266(1997). RN [9] RP CATALYTIC ACTIVITY. RX PubMed=12244105; DOI=10.1074/jbc.m206788200; RA Kozak K.R., Crews B.C., Morrow J.D., Wang L.H., Ma Y.H., Weinander R., RA Jakobsson P.J., Marnett L.J.; RT "Metabolism of the endocannabinoids, 2-arachidonylglycerol and anandamide, RT into prostaglandin, thromboxane, and prostacyclin glycerol esters and RT ethanolamides."; RL J. Biol. Chem. 277:44877-44885(2002). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH CALCIUM IONS; RP MAGNESIUM IONS AND GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY 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., Uodome N., RA 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 [11] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE; RP MAGNESIUM IONS AND THE SYNTHETIC INHIBITOR BSBT, FUNCTION, SUBUNIT, RP CATALYTIC 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., Okazaki N., RA Kinugasa S., Shishitani H., Matsumura H., Kai Y., 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 [12] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE; RP MAGNESIUM IONS AND THE SYNTHETIC INHIBITOR HQL-79, FUNCTION, AND CATALYTIC RP 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 selective RT inhibitor of human hematopoietic prostaglandin D synthase."; RL J. Biol. Chem. 281:15277-15286(2006). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE AND RP SYNTHETIC INHIBITORS, AND SUBUNIT. RX PubMed=18341273; DOI=10.1021/jm701509k; RA Hohwy M., Spadola L., Lundquist B., Hawtin P., Dahmen J., Groth-Clausen I., RA Nilsson E., Persdotter S., von Wachenfeldt K., Folmer R.H., Edman K.; RT "Novel prostaglandin D synthase inhibitors generated by fragment-based drug RT design."; RL J. Med. Chem. 51:2178-2186(2008). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND RP SYNTHETIC 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 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 towards cumene hydroperoxide. {ECO:0000269|PubMed:10824118, CC ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12244105, 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: 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, ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12244105, ECO:0000269|PubMed:12627223, CC ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:19939518, CC ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10601; CC Evidence={ECO:0000305|PubMed:10824118, ECO:0000305|PubMed:12244105}; CC -!- CATALYTIC ACTIVITY: CC Reaction=RX + glutathione = an S-substituted glutathione + a halide CC anion + 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, ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:15113825}; 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:0000269|PubMed:12244105}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51233; CC Evidence={ECO:0000305|PubMed:12244105}; CC -!- COFACTOR: CC Name=glutathione; Xref=ChEBI:CHEBI:57925; CC Evidence={ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}; CC Note=Glutathione is required for the prostaglandin D synthase activity. CC {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}; CC -!- ACTIVITY 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. Magnesium CC increases the affinity for glutathione, while calcium has no effect on CC the affinity for glutathione. {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 activity CC 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 activity CC in the presence of magnesium ions {ECO:0000269|PubMed:11672424, CC ECO:0000269|PubMed:12627223, 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, ECO:0000269|PubMed:12627223, CC 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, ECO:0000269|PubMed:12627223, CC 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, ECO:0000269|PubMed:12627223, CC 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, ECO:0000269|PubMed:12627223, CC ECO:0000269|PubMed:15113825}; CC Vmax=6.8 umol/min/mg enzyme with allyl isothiocyanate as substrate CC {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, CC ECO:0000269|PubMed:15113825}; CC Vmax=6.3 umol/min/mg enzyme with benzyl isothiocyanate as substrate CC {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, CC ECO:0000269|PubMed:15113825}; CC Vmax=0.05 umol/min/mg enzyme with cumene hydroperoxide as substrate CC {ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223, CC 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 O60760; Q96GS6: ABHD17A; NbExp=4; IntAct=EBI-10187349, EBI-2870273; CC O60760; Q96B67: ARRDC3; NbExp=9; IntAct=EBI-10187349, EBI-2875665; CC O60760; P15018: LIF; NbExp=3; IntAct=EBI-10187349, EBI-1037189; CC O60760; P08582-2: MELTF; NbExp=3; IntAct=EBI-10187349, EBI-10195914; CC O60760; Q13370: PDE3B; NbExp=3; IntAct=EBI-10187349, EBI-6172856; CC O60760; Q8N1H7: SIX6OS1; NbExp=3; IntAct=EBI-10187349, EBI-12182077; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353279}. CC -!- TISSUE SPECIFICITY: Expressed in a number of megakaryocytic cell lines CC but not in platelets. Highly expressed in adipose tissue, macrophages CC and placenta. Also expressed at lower levels in lung, heart, lymph CC 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 cells. CC 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 --------------------------------------------------------------------------- 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_014485.3. 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 PDB; 5YWE; X-ray; 1.68 A; A/B/C/D=2-199. DR PDB; 5YWX; X-ray; 1.74 A; A/B/C/D=2-199. DR PDB; 5YX1; X-ray; 1.39 A; A/B/C/D=2-199. DR PDB; 6N4E; X-ray; 1.65 A; A=1-199. DR PDB; 6W58; X-ray; 2.40 A; A/B=1-199. DR PDB; 6W8H; X-ray; 1.97 A; A/C=1-199. DR PDB; 6ZTC; X-ray; 1.84 A; A/B=1-199. DR PDB; 7JR6; X-ray; 1.88 A; A/B=1-199. DR PDB; 7JR8; X-ray; 1.13 A; A/B=1-199. 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 PDBsum; 5YWE; -. DR PDBsum; 5YWX; -. DR PDBsum; 5YX1; -. DR PDBsum; 6N4E; -. DR PDBsum; 6W58; -. DR PDBsum; 6W8H; -. DR PDBsum; 6ZTC; -. DR PDBsum; 7JR6; -. DR PDBsum; 7JR8; -. DR AlphaFoldDB; O60760; -. DR SMR; O60760; -. DR BioGRID; 118128; 8. DR IntAct; O60760; 7. DR STRING; 9606.ENSP00000295256; -. DR BindingDB; O60760; -. DR ChEMBL; CHEMBL5879; -. DR DrugBank; DB08790; 1-PHENYL-1H-PYRAZOLE-4-CARBOXYLIC ACID. DR DrugBank; DB01897; 2-(2f-Benzothiazolyl)-5-Styryl-3-(4f-Phthalhydrazidyl)Tetrazolium Chloride. DR DrugBank; DB08695; 3-(4-nitrophenyl)-1H-pyrazole. DR DrugBank; DB07613; 3-phenyl-5-(1H-pyrazol-3-yl)isoxazole. DR DrugBank; DB07917; 4-(BENZHYDRYLOXY)-1-[3-(1H-TETRAAZOL-5-YL)PROPYL]PIPERIDINE. DR DrugBank; DB07616; 4-{[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino}-2-hydroxybenzoic acid. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB00291; Chlorambucil. DR DrugBank; DB03619; Deoxycholic acid. DR DrugBank; DB00143; Glutathione. DR DrugBank; DB03310; Glutathione disulfide. DR DrugBank; DB08313; Nocodazole. DR DrugBank; DB07614; PHENYL-5-(1H-PYRAZOL-3-YL)-1,3-THIAZOLE. DR DrugBank; DB07615; Tranilast. DR DrugCentral; O60760; -. DR GuidetoPHARMACOLOGY; 1381; -. DR SwissLipids; SLP:000000828; -. DR GlyGen; O60760; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O60760; -. DR PhosphoSitePlus; O60760; -. DR BioMuta; HPGDS; -. DR MassIVE; O60760; -. DR PaxDb; 9606-ENSP00000295256; -. DR PeptideAtlas; O60760; -. DR ProteomicsDB; 49588; -. DR Antibodypedia; 14738; 123 antibodies from 27 providers. DR DNASU; 27306; -. DR Ensembl; ENST00000295256.10; ENSP00000295256.5; ENSG00000163106.11. DR GeneID; 27306; -. DR KEGG; hsa:27306; -. DR MANE-Select; ENST00000295256.10; ENSP00000295256.5; NM_014485.3; NP_055300.1. DR UCSC; uc003hte.2; human. DR AGR; HGNC:17890; -. DR CTD; 27306; -. DR DisGeNET; 27306; -. DR GeneCards; HPGDS; -. DR HGNC; HGNC:17890; HPGDS. DR HPA; ENSG00000163106; Tissue enhanced (placenta). DR MIM; 602598; gene. DR neXtProt; NX_O60760; -. DR OpenTargets; ENSG00000163106; -. DR PharmGKB; PA165664133; -. DR VEuPathDB; HostDB:ENSG00000163106; -. DR eggNOG; KOG1695; Eukaryota. DR GeneTree; ENSGT00940000160278; -. DR HOGENOM; CLU_039475_1_0_1; -. DR InParanoid; O60760; -. DR OMA; TEMEQCH; -. DR OrthoDB; 414243at2759; -. 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 PathwayCommons; O60760; -. DR Reactome; R-HSA-156590; Glutathione conjugation. DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX). DR SABIO-RK; O60760; -. DR SignaLink; O60760; -. DR BioGRID-ORCS; 27306; 11 hits in 1117 CRISPR screens. DR ChiTaRS; HPGDS; human. DR EvolutionaryTrace; O60760; -. DR GeneWiki; PGDS; -. DR GenomeRNAi; 27306; -. DR Pharos; O60760; Tchem. DR PRO; PR:O60760; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O60760; protein. DR Bgee; ENSG00000163106; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 149 other cell types or tissues. DR ExpressionAtlas; O60760; baseline and differential. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central. 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:0006749; P:glutathione metabolic process; IBA:GO_Central. 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:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB. DR GO; GO:0009624; P:response to nematode; IEA:Ensembl. DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR CDD; cd10295; GST_C_Sigma; 1. DR CDD; cd03039; GST_N_Sigma_like; 1. DR FunFam; 1.20.1050.10:FF:000035; Hematopoietic prostaglandin D synthase; 1. DR FunFam; 3.40.30.10:FF:000035; hematopoietic prostaglandin D synthase; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR050213; GST_superfamily. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF224; HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE; 1. DR Pfam; PF14497; GST_C_3; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDG01205; AMPS.1; 1. DR SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Isomerase; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Metal-binding; Prostaglandin biosynthesis; KW Prostaglandin metabolism; Proteomics identification; Reference proteome; KW Transferase. FT CHAIN 1..199 FT /note="Hematopoietic prostaglandin D synthase" FT /id="PRO_0000185934" 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:0000269|PubMed:12627223, FT ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, FT ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518" FT BINDING 14 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12627223, FT ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, FT ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518" FT BINDING 39 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12627223, FT ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, FT ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518" FT BINDING 49..51 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12627223, FT ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, FT ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518" FT BINDING 63..64 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12627223, FT ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, FT ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518" FT MUTAGEN 93 FT /note="D->N: Loss of activation by calcium or magnesium FT ions." FT /evidence="ECO:0000269|PubMed:12627223" FT MUTAGEN 96 FT /note="D->N: Increases PGD2 synthesis. Loss of activation FT by calcium or magnesium ions." FT /evidence="ECO:0000269|PubMed:12627223" FT MUTAGEN 97 FT /note="D->N: Reduces PGD2 synthesis by 99%. Loss of FT activation by calcium or magnesium ions." FT /evidence="ECO:0000269|PubMed:12627223" FT CONFLICT 187 FT /note="V -> I (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT STRAND 4..12 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 16..24 FT /evidence="ECO:0007829|PDB:7JR8" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 39..42 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:7JR8" FT STRAND 46..49 FT /evidence="ECO:0007829|PDB:7JR8" FT STRAND 53..56 FT /evidence="ECO:0007829|PDB:7JR8" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 64..72 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:5AIS" FT HELIX 82..101 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 109..122 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 124..135 FT /evidence="ECO:0007829|PDB:7JR8" FT STRAND 139..142 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 148..163 FT /evidence="ECO:0007829|PDB:7JR8" FT TURN 165..170 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 172..183 FT /evidence="ECO:0007829|PDB:7JR8" FT HELIX 185..193 FT /evidence="ECO:0007829|PDB:7JR8" 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 //