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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.
26-FEB-2020, entry version 182.
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, ACTIVITY
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:
Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600,
ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2;
Evidence={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:
Reaction=glutathione + RX = a halide anion + an S-substituted
glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
ChEBI:CHEBI:90779; EC=2.5.1.18;
Evidence={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};
-!- ACTIVITY 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.
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.
PDB; 5YWE; X-ray; 1.68 A; A/B/C/D=2-199.
PDB; 5YWX; X-ray; 1.74 A; A/B/C/D=2-199.
PDB; 5YX1; X-ray; 1.39 A; A/B/C/D=2-199.
PDB; 6N4E; X-ray; 1.65 A; A=1-199.
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; -.
PDBsum; 5YWE; -.
PDBsum; 5YWX; -.
PDBsum; 5YX1; -.
PDBsum; 6N4E; -.
SMR; O60760; -.
BioGrid; 118128; 4.
IntAct; O60760; 8.
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; DB07616; 4-{[4-(4-fluoro-3-methylphenyl)-1,3-thiazol-2-yl]amino}-2-hydroxybenzoic acid.
DrugBank; DB00143; Glutathione.
DrugBank; DB09462; Glycerin.
DrugBank; DB08313; nocodazole.
DrugBank; DB07614; PHENYL-5-(1H-PYRAZOL-3-YL)-1,3-THIAZOLE.
DrugBank; DB07615; Tranilast.
DrugBank; DB00755; Tretinoin.
DrugBank; DB00162; Vitamin A.
DrugCentral; O60760; -.
GuidetoPHARMACOLOGY; 1381; -.
SwissLipids; SLP:000000828; -.
PhosphoSitePlus; O60760; -.
BioMuta; HPGDS; -.
MassIVE; O60760; -.
PaxDb; O60760; -.
PeptideAtlas; O60760; -.
PRIDE; O60760; -.
ProteomicsDB; 49588; -.
Ensembl; ENST00000295256; ENSP00000295256; ENSG00000163106.
GeneID; 27306; -.
KEGG; hsa:27306; -.
UCSC; uc003hte.2; human.
CTD; 27306; -.
DisGeNET; 27306; -.
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; ENSGT00940000160278; -.
HOGENOM; CLU_039475_1_0_1; -.
InParanoid; O60760; -.
KO; K04097; -.
OMA; TEMEQCH; -.
OrthoDB; 1162336at2759; -.
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; -.
ChiTaRS; HPGDS; human.
EvolutionaryTrace; O60760; -.
GeneWiki; PGDS; -.
GenomeRNAi; 27306; -.
Pharos; O60760; Tchem.
PRO; PR:O60760; -.
Proteomes; UP000005640; Chromosome 4.
RNAct; O60760; protein.
Bgee; ENSG00000163106; Expressed in placenta and 167 other tissues.
ExpressionAtlas; O60760; baseline and differential.
Genevisible; O60760; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
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:0006749; P:glutathione metabolic process; IBA:GO_Central.
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.
Gene3D; 3.40.30.10; -; 1.
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; 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
/note="Hematopoietic prostaglandin D synthase"
/id="PRO_0000185934"
DOMAIN 2..79
/note="GST N-terminal"
DOMAIN 81..199
/note="GST C-terminal"
REGION 49..51
/note="Glutathione binding"
/evidence="ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518"
REGION 63..64
/note="Glutathione binding"
/evidence="ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518"
BINDING 8
/note="Glutathione"
/evidence="ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518"
BINDING 14
/note="Glutathione"
/evidence="ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518"
BINDING 39
/note="Glutathione"
/evidence="ECO:0000269|PubMed:12627223,
ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518"
MUTAGEN 93
/note="D->N: Loss of activation by calcium or magnesium
ions."
/evidence="ECO:0000269|PubMed:12627223"
MUTAGEN 96
/note="D->N: Increases PGD2 synthesis. Loss of activation
by calcium or magnesium ions."
/evidence="ECO:0000269|PubMed:12627223"
MUTAGEN 97
/note="D->N: Reduces PGD2 synthesis by 99%. Loss of
activation by calcium or magnesium ions."
/evidence="ECO:0000269|PubMed:12627223"
CONFLICT 187
/note="V -> I (in Ref. 2; no nucleotide entry)"
/evidence="ECO:0000305"
STRAND 4..12
/evidence="ECO:0000244|PDB:5YX1"
TURN 13..15
/evidence="ECO:0000244|PDB:5YX1"
HELIX 16..24
/evidence="ECO:0000244|PDB:5YX1"
STRAND 30..34
/evidence="ECO:0000244|PDB:5YX1"
HELIX 36..38
/evidence="ECO:0000244|PDB:5YX1"
HELIX 39..43
/evidence="ECO:0000244|PDB:5YX1"
STRAND 46..49
/evidence="ECO:0000244|PDB:5YWE"
STRAND 53..56
/evidence="ECO:0000244|PDB:5YX1"
STRAND 59..62
/evidence="ECO:0000244|PDB:5YX1"
HELIX 64..72
/evidence="ECO:0000244|PDB:5YX1"
HELIX 76..78
/evidence="ECO:0000244|PDB:5AIS"
HELIX 82..101
/evidence="ECO:0000244|PDB:5YX1"
HELIX 109..121
/evidence="ECO:0000244|PDB:5YX1"
HELIX 124..135
/evidence="ECO:0000244|PDB:5YX1"
STRAND 139..142
/evidence="ECO:0000244|PDB:5YX1"
HELIX 148..163
/evidence="ECO:0000244|PDB:5YX1"
TURN 165..170
/evidence="ECO:0000244|PDB:5YX1"
HELIX 172..183
/evidence="ECO:0000244|PDB:5YX1"
HELIX 185..193
/evidence="ECO:0000244|PDB:5YX1"
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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