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Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase)

 HPGDS_HUMAN             Reviewed;         199 AA.
O60760; Q6FHT9;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 166.
RecName: Full=Hematopoietic prostaglandin D synthase;
Short=H-PGDS;
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};
AltName: Full=GST class-sigma;
AltName: Full=Glutathione S-transferase;
EC=2.5.1.18 {ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:15113825};
AltName: Full=Glutathione-dependent PGD synthase;
AltName: Full=Glutathione-requiring prostaglandin D synthase;
AltName: Full=Prostaglandin-H2 D-isomerase;
Name=HPGDS; Synonyms=GSTS, PGDS, PTGDS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=10824118; DOI=10.1046/j.1432-1327.2000.01362.x;
Kanaoka Y., Fujimori K., Kikuno R., Sakaguchi Y., Urade Y.,
Hayaishi O.;
"Structure and chromosomal localization of human and mouse genes for
hematopoietic prostaglandin D synthase.";
Eur. J. Biochem. 267:3315-3322(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=11672424; DOI=10.1042/0264-6021:3590507;
Jowsey I.R., Thomson A.M., Flanagan J.U., Murdock P.R., Moore G.B.,
Meyer D.J., Murphy G.J., Smith S.A., Hayes J.D.;
"Mammalian class Sigma glutathione S-transferases: catalytic
properties and tissue-specific expression of human and rat GSH-
dependent prostaglandin D2 synthases.";
Biochem. J. 359:507-516(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Substantia nigra;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Megakaryocyte;
PubMed=9425264; DOI=10.1006/bbrc.1997.7803;
Suzuki T., Watanabe K., Kanaoka Y., Sato T., Hayaishi O.;
"Induction of hematopoietic prostaglandin D synthase in human
megakaryocytic cells by phorbol ester.";
Biochem. Biophys. Res. Commun. 241:288-293(1997).
[8]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Megakaryocyte;
PubMed=9353279; DOI=10.1074/jbc.272.45.28263;
Mahmud I., Ueda N., Yamaguchi H., Yamashita R., Yamamoto S.,
Kanaoka Y., Urade Y., Hayaishi O.;
"Prostaglandin D synthase in human megakaryoblastic cells.";
J. Biol. Chem. 272:28263-28266(1997).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH CALCIUM IONS;
MAGNESIUM IONS AND GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
ASP-93; ASP-96 AND ASP-97.
PubMed=12627223; DOI=10.1038/nsb907;
Inoue T., Irikura D., Okazaki N., Kinugasa S., Matsumura H.,
Uodome N., Yamamoto M., Kumasaka T., Miyano M., Kai Y., Urade Y.;
"Mechanism of metal activation of human hematopoietic prostaglandin D
synthase.";
Nat. Struct. Biol. 10:291-296(2003).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE;
MAGNESIUM IONS AND THE SYNTHETIC INHIBITOR BSBT, FUNCTION, SUBUNIT,
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15113825; DOI=10.1093/jb/mvh033;
Inoue T., Okano Y., Kado Y., Aritake K., Irikura D., Uodome N.,
Okazaki N., Kinugasa S., Shishitani H., Matsumura H., Kai Y.,
Urade Y.;
"First determination of the inhibitor complex structure of human
hematopoietic prostaglandin D synthase.";
J. Biochem. 135:279-283(2004).
[11]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE;
MAGNESIUM IONS AND THE SYNTHETIC INHIBITOR HQL-79, FUNCTION, AND
CATALYTIC ACTIVITY.
PubMed=16547010; DOI=10.1074/jbc.M506431200;
Aritake K., Kado Y., Inoue T., Miyano M., Urade Y.;
"Structural and functional characterization of HQL-79, an orally
selective inhibitor of human hematopoietic prostaglandin D synthase.";
J. Biol. Chem. 281:15277-15286(2006).
[12]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE
AND SYNTHETIC INHIBITORS, AND SUBUNIT.
PubMed=18341273; DOI=10.1021/jm701509k;
Hohwy M., Spadola L., Lundquist B., Hawtin P., Dahmen J.,
Groth-Clausen I., Nilsson E., Persdotter S., von Wachenfeldt K.,
Folmer R.H., Edman K.;
"Novel prostaglandin D synthase inhibitors generated by fragment-based
drug design.";
J. Med. Chem. 51:2178-2186(2008).
[13]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND
SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=19939518; DOI=10.1016/j.ejmech.2009.10.025;
Weber J.E., Oakley A.J., Christ A.N., Clark A.G., Hayes J.D., Hall R.,
Hume D.A., Board P.G., Smythe M.L., Flanagan J.U.;
"Identification and characterisation of new inhibitors for the human
hematopoietic prostaglandin D2 synthase.";
Eur. J. Med. Chem. 45:447-454(2010).
-!- FUNCTION: Bifunctional enzyme which catalyzes both the conversion
of PGH2 to PGD2, a prostaglandin involved in smooth muscle
contraction/relaxation and a potent inhibitor of platelet
aggregation, and the conjugation of glutathione with a wide range
of aryl halides and organic isothiocyanates. Also exhibits low
glutathione-peroxidase activity towards cumene hydroperoxide.
{ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825,
ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:19939518,
ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}.
-!- CATALYTIC ACTIVITY: (5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-
hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-
11-oxoprosta-5,13-dienoate. {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}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:15113825}.
-!- COFACTOR:
Name=glutathione; Xref=ChEBI:CHEBI:57925;
Evidence={ECO:0000269|PubMed:10824118,
ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:9353279,
ECO:0000269|PubMed:9425264};
Note=Glutathione is required for the prostaglandin D synthase
activity. {ECO:0000269|PubMed:10824118,
ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:9353279,
ECO:0000269|PubMed:9425264};
-!- ENZYME REGULATION: Prostaglandin PGD2 synthesis is stimulated by
calcium and magnesium ions. One calcium or magnesium ion is bound
between the subunits of the homodimer. The interactions with the
protein are for the most part mediated via water molecules.
Magnesium increases the affinity for glutathione, while calcium
has no effect on the affinity for glutathione.
{ECO:0000269|PubMed:12627223}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=8 mM for glutathione for the glutathione-conjugating activity
{ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825};
KM=0.6 mM for glutathione for the prostaglandin D synthase
activity in the presence of EDTA {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
KM=0.14 mM for glutathione for the prostaglandin D synthase
activity in the presence of magnesium ions
{ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825};
Vmax=8.6 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
Vmax=5.1 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
Vmax=44.3 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
Vmax=10.7 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
Vmax=6.8 umol/min/mg enzyme with allyl isothiocyanate as
substrate {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
Vmax=6.3 umol/min/mg enzyme with benzyl isothiocyanate as
substrate {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
Vmax=0.05 umol/min/mg enzyme with cumene hydroperoxide as
substrate {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518}.
-!- INTERACTION:
Q96GS6:ABHD17A; NbExp=3; IntAct=EBI-10187349, EBI-2870273;
Q96B67:ARRDC3; NbExp=7; IntAct=EBI-10187349, EBI-2875665;
P08582-2:MELTF; NbExp=3; IntAct=EBI-10187349, EBI-10195914;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353279}.
-!- TISSUE SPECIFICITY: Expressed in a number of megakaryocytic cell
lines but not in platelets. Highly expressed in adipose tissue,
macrophages and placenta. Also expressed at lower levels in lung,
heart, lymph nodes, appendix, bone marrow and fetal liver.
{ECO:0000269|PubMed:10824118, ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:9353279, ECO:0000269|PubMed:9425264}.
-!- DEVELOPMENTAL STAGE: Highest levels in immature megakaryocytic
cells. Disappears after final differentiation to platelets.
{ECO:0000269|PubMed:9425264}.
-!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA).
{ECO:0000269|PubMed:9425264}.
-!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
{ECO:0000305}.
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EMBL; D82073; BAA25545.1; -; mRNA.
EMBL; AB008830; BAA96854.1; -; Genomic_DNA.
EMBL; AK290075; BAF82764.1; -; mRNA.
EMBL; CR541662; CAG46463.1; -; mRNA.
EMBL; CR541679; CAG46480.1; -; mRNA.
EMBL; CH471057; EAX06052.1; -; Genomic_DNA.
EMBL; BC020734; AAH20734.1; -; mRNA.
CCDS; CCDS3640.1; -.
RefSeq; NP_055300.1; NM_014485.2.
UniGene; Hs.128433; -.
PDB; 1IYH; X-ray; 1.70 A; A/B/C/D=2-199.
PDB; 1IYI; X-ray; 1.80 A; A/B/C/D=2-199.
PDB; 1V40; X-ray; 1.90 A; A/B/C/D=2-199.
PDB; 2CVD; X-ray; 1.45 A; A/B/C/D=2-199.
PDB; 2VCQ; X-ray; 1.95 A; A/B/C/D=1-199.
PDB; 2VCW; X-ray; 1.95 A; A/B/C/D=1-199.
PDB; 2VCX; X-ray; 2.10 A; A/B/C/D=1-199.
PDB; 2VCZ; X-ray; 1.95 A; A/B/C/D=1-199.
PDB; 2VD0; X-ray; 2.20 A; A/B/C/D=1-199.
PDB; 2VD1; X-ray; 2.25 A; A/B/C/D=1-199.
PDB; 3EE2; X-ray; 1.91 A; A/B=1-199.
PDB; 3KXO; X-ray; 2.10 A; A/B=1-199.
PDB; 3VI5; X-ray; 2.00 A; A/B/C/D=2-199.
PDB; 3VI7; X-ray; 2.00 A; A/B/C/D=2-199.
PDB; 4EC0; X-ray; 1.85 A; A/B=1-199.
PDB; 4EDY; X-ray; 1.72 A; A/B=2-199.
PDB; 4EDZ; X-ray; 2.00 A; A/B/C/D=2-199.
PDB; 4EE0; X-ray; 1.75 A; A/B=2-199.
PDB; 5AIS; X-ray; 1.85 A; A/B/C/D=2-199.
PDB; 5AIV; X-ray; 2.04 A; A/B/C/D=2-199.
PDB; 5AIX; X-ray; 2.10 A; A/B/C/D=2-199.
PDBsum; 1IYH; -.
PDBsum; 1IYI; -.
PDBsum; 1V40; -.
PDBsum; 2CVD; -.
PDBsum; 2VCQ; -.
PDBsum; 2VCW; -.
PDBsum; 2VCX; -.
PDBsum; 2VCZ; -.
PDBsum; 2VD0; -.
PDBsum; 2VD1; -.
PDBsum; 3EE2; -.
PDBsum; 3KXO; -.
PDBsum; 3VI5; -.
PDBsum; 3VI7; -.
PDBsum; 4EC0; -.
PDBsum; 4EDY; -.
PDBsum; 4EDZ; -.
PDBsum; 4EE0; -.
PDBsum; 5AIS; -.
PDBsum; 5AIV; -.
PDBsum; 5AIX; -.
ProteinModelPortal; O60760; -.
SMR; O60760; -.
BioGrid; 118128; 4.
IntAct; O60760; 6.
STRING; 9606.ENSP00000295256; -.
BindingDB; O60760; -.
ChEMBL; CHEMBL5879; -.
DrugBank; DB08790; 1-PHENYL-1H-PYRAZOLE-4-CARBOXYLIC ACID.
DrugBank; DB01897; 2-(2f-Benzothiazolyl)-5-Styryl-3-(4f-Phthalhydrazidyl)Tetrazolium Chloride.
DrugBank; DB08695; 3-(4-nitrophenyl)-1H-pyrazole.
DrugBank; DB07613; 3-phenyl-5-(1H-pyrazol-3-yl)isoxazole.
DrugBank; DB07917; 4-(BENZHYDRYLOXY)-1-[3-(1H-TETRAAZOL-5-YL)PROPYL]PIPERIDINE.
DrugBank; DB00143; Glutathione.
DrugBank; DB04077; Glycerol.
DrugBank; DB08313; nocodazole.
DrugBank; DB07615; Tranilast.
GuidetoPHARMACOLOGY; 1381; -.
SwissLipids; SLP:000000828; -.
PhosphoSitePlus; O60760; -.
BioMuta; HPGDS; -.
PaxDb; O60760; -.
PeptideAtlas; O60760; -.
PRIDE; O60760; -.
Ensembl; ENST00000295256; ENSP00000295256; ENSG00000163106.
GeneID; 27306; -.
KEGG; hsa:27306; -.
UCSC; uc003hte.2; human.
CTD; 27306; -.
DisGeNET; 27306; -.
EuPathDB; HostDB:ENSG00000163106.10; -.
GeneCards; HPGDS; -.
HGNC; HGNC:17890; HPGDS.
HPA; HPA024035; -.
MIM; 602598; gene.
neXtProt; NX_O60760; -.
OpenTargets; ENSG00000163106; -.
PharmGKB; PA165664133; -.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
GeneTree; ENSGT00670000097856; -.
HOGENOM; HOG000115733; -.
HOVERGEN; HBG105321; -.
InParanoid; O60760; -.
KO; K04097; -.
OMA; TTTWADF; -.
OrthoDB; EOG091G0MBB; -.
PhylomeDB; O60760; -.
TreeFam; TF105321; -.
BioCyc; MetaCyc:HS08788-MONOMER; -.
BRENDA; 2.5.1.18; 2681.
BRENDA; 5.3.99.2; 2681.
Reactome; R-HSA-156590; Glutathione conjugation.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RK; O60760; -.
EvolutionaryTrace; O60760; -.
GeneWiki; PGDS; -.
GenomeRNAi; 27306; -.
PRO; PR:O60760; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163106; -.
Genevisible; O60760; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004364; F:glutathione transferase activity; TAS:Reactome.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004667; F:prostaglandin-D synthase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0007626; P:locomotory behavior; TAS:ProtInc.
GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
GO; GO:0006693; P:prostaglandin metabolic process; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Cytoplasm;
Fatty acid biosynthesis; Fatty acid metabolism; Isomerase;
Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
Prostaglandin biosynthesis; Prostaglandin metabolism;
Reference proteome; Transferase.
CHAIN 1 199 Hematopoietic prostaglandin D synthase.
/FTId=PRO_0000185934.
DOMAIN 2 79 GST N-terminal.
DOMAIN 81 199 GST C-terminal.
REGION 49 51 Glutathione binding.
{ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825,
ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273,
ECO:0000269|PubMed:19939518}.
REGION 63 64 Glutathione binding.
{ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825,
ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273,
ECO:0000269|PubMed:19939518}.
BINDING 8 8 Glutathione.
{ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825,
ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273,
ECO:0000269|PubMed:19939518}.
BINDING 14 14 Glutathione.
{ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825,
ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273,
ECO:0000269|PubMed:19939518}.
BINDING 39 39 Glutathione.
{ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825,
ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273,
ECO:0000269|PubMed:19939518}.
MUTAGEN 93 93 D->N: Loss of activation by calcium or
magnesium ions.
{ECO:0000269|PubMed:12627223}.
MUTAGEN 96 96 D->N: Increases PGD2 synthesis. Loss of
activation by calcium or magnesium ions.
{ECO:0000269|PubMed:12627223}.
MUTAGEN 97 97 D->N: Reduces PGD2 synthesis by 99%. Loss
of activation by calcium or magnesium
ions. {ECO:0000269|PubMed:12627223}.
CONFLICT 187 187 V -> I (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
STRAND 4 12 {ECO:0000244|PDB:2CVD}.
HELIX 13 15 {ECO:0000244|PDB:2CVD}.
HELIX 16 24 {ECO:0000244|PDB:2CVD}.
STRAND 30 34 {ECO:0000244|PDB:2CVD}.
HELIX 36 38 {ECO:0000244|PDB:2CVD}.
HELIX 39 43 {ECO:0000244|PDB:2CVD}.
STRAND 46 49 {ECO:0000244|PDB:1IYH}.
STRAND 53 56 {ECO:0000244|PDB:2CVD}.
STRAND 59 62 {ECO:0000244|PDB:2CVD}.
HELIX 64 72 {ECO:0000244|PDB:2CVD}.
HELIX 76 78 {ECO:0000244|PDB:5AIS}.
HELIX 82 100 {ECO:0000244|PDB:2CVD}.
HELIX 109 121 {ECO:0000244|PDB:2CVD}.
HELIX 123 135 {ECO:0000244|PDB:2CVD}.
STRAND 139 142 {ECO:0000244|PDB:2CVD}.
HELIX 148 163 {ECO:0000244|PDB:2CVD}.
TURN 165 170 {ECO:0000244|PDB:2CVD}.
HELIX 172 182 {ECO:0000244|PDB:2CVD}.
HELIX 185 193 {ECO:0000244|PDB:2CVD}.
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


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