HPGDS_HUMAN
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 03-AUG-2022, entry version 194.
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=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, 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}.
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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 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; 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 DrugBank; DB00755; Tretinoin.
DR DrugCentral; O60760; -.
DR GuidetoPHARMACOLOGY; 1381; -.
DR SwissLipids; SLP:000000828; -.
DR PhosphoSitePlus; O60760; -.
DR BioMuta; HPGDS; -.
DR MassIVE; O60760; -.
DR PaxDb; O60760; -.
DR PeptideAtlas; O60760; -.
DR PRIDE; O60760; -.
DR ProteomicsDB; 49588; -.
DR Antibodypedia; 14738; 109 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 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; 1162336at2759; -.
DR PhylomeDB; O60760; -.
DR TreeFam; TF105321; -.
DR BioCyc; MetaCyc:HS08788-MON; -.
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 1037 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 placenta and 147 other tissues.
DR ExpressionAtlas; O60760; baseline and differential.
DR Genevisible; O60760; HS.
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:0007165; P:signal transduction; NAS:ProtInc.
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; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
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; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Isomerase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome; 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
