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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_RAT               Reviewed;         199 AA.
O35543; O35351;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 148.
RecName: Full=Hematopoietic prostaglandin D synthase;
Short=H-PGDS;
EC=5.3.99.2 {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:9323136};
AltName: Full=GST class-sigma;
AltName: Full=Glutathione S-transferase;
EC=2.5.1.18 {ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:9323136};
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN
COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Spleen;
PubMed=9323136; DOI=10.1016/S0092-8674(00)80374-8;
Kanaoka Y., Ago H., Inagaki E., Nanayama T., Miyano M., Kikuno R.,
Fujii Y., Eguchi N., Toh H., Urade Y., Hayaishi O.;
"Cloning and crystal structure of hematopoietic prostaglandin D
synthase.";
Cell 90:1085-1095(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Spleen;
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=Ovary;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 39-198.
STRAIN=Sprague-Dawley; TISSUE=Spleen;
Yuan Y., Reddy R.G., Kim H.;
"Purification and cloning of rat glutathione-dependent prostaglandin D
synthase.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
AND MUTAGENESIS OF TYR-8; ARG-14; TRP-104; LYS-112; TYR-152; CYS-156;
LYS-198 AND LEU-199.
PubMed=10871602; DOI=10.1074/jbc.M000750200;
Pinzar E., Miyano M., Kanaoka Y., Urade Y., Hayaishi O.;
"Structural basis of hematopoietic prostaglandin D synthase activity
elucidated by site-directed mutagenesis.";
J. Biol. Chem. 275:31239-31244(2000).
[6]
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).
-!- 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:10871602, ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:9323136}.
-!- 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:10871602,
ECO:0000269|PubMed:11672424, ECO:0000269|PubMed:16547010,
ECO:0000269|PubMed:9323136}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:9323136}.
-!- COFACTOR:
Name=glutathione; Xref=ChEBI:CHEBI:57925;
Evidence={ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
Note=Glutathione is required for the prostaglandin D synthase
activity. {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=100 uM for glutathione for the prostaglandin D synthase
activity {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
KM=500 uM for glutathione for the glutathione-conjugating
activity {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
KM=500 uM for PGH2 for the prostaglandin D synthase activity
{ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424};
KM=3 mM for 1-chloro-2,4-dinitrobenzene
{ECO:0000269|PubMed:10871602, ECO:0000269|PubMed:11672424};
Vmax=17.6 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
Vmax=9.2 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
Vmax=48.3 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
Vmax=17.9 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
Vmax=0.35 umol/min/mg enzyme with cumene hydroperoxide as
substrate {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
Vmax=10.2 umol/min/mg enzyme with allyl isothiocyanate as
substrate {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
Vmax=11.3 umol/min/mg enzyme with benzyl isothiocyanate as
substrate {ECO:0000269|PubMed:10871602,
ECO:0000269|PubMed:11672424};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9323136}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Highly expressed in spleen and bone marrow.
Lower levels of expression in small intestine, colon, liver,
pancreas and skin. Not detected in brain, heart, lung or kidney
(at protein level). {ECO:0000269|PubMed:11672424,
ECO:0000269|PubMed:9323136}.
-!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB72099.1; Type=Frameshift; Positions=73, 113; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; D82071; BAA22898.1; -; mRNA.
EMBL; BC087590; AAH87590.1; -; mRNA.
EMBL; AF021882; AAB72099.1; ALT_FRAME; mRNA.
RefSeq; NP_113832.1; NM_031644.2.
UniGene; Rn.10837; -.
PDB; 1PD2; X-ray; 2.30 A; 1/2=1-199.
PDBsum; 1PD2; -.
ProteinModelPortal; O35543; -.
SMR; O35543; -.
STRING; 10116.ENSRNOP00000008826; -.
PaxDb; O35543; -.
PRIDE; O35543; -.
Ensembl; ENSRNOT00000008826; ENSRNOP00000008826; ENSRNOG00000006583.
GeneID; 58962; -.
KEGG; rno:58962; -.
UCSC; RGD:69251; rat.
CTD; 27306; -.
RGD; 69251; Hpgds.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
GeneTree; ENSGT00670000097856; -.
HOGENOM; HOG000115733; -.
HOVERGEN; HBG105321; -.
InParanoid; O35543; -.
KO; K04097; -.
OMA; TTTWADF; -.
OrthoDB; EOG091G0MBB; -.
PhylomeDB; O35543; -.
TreeFam; TF105321; -.
BRENDA; 5.3.99.2; 5301.
Reactome; R-RNO-156590; Glutathione conjugation.
Reactome; R-RNO-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RK; O35543; -.
EvolutionaryTrace; O35543; -.
PRO; PR:O35543; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000006583; -.
Genevisible; O35543; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0004667; F:prostaglandin-D synthase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; TAS:RGD.
GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
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; Complete proteome; Cytoplasm; Fatty acid biosynthesis;
Fatty acid metabolism; Isomerase; Lipid biosynthesis;
Lipid metabolism; Prostaglandin biosynthesis;
Prostaglandin metabolism; Reference proteome; Transferase.
CHAIN 1 199 Hematopoietic prostaglandin D synthase.
/FTId=PRO_0000185936.
DOMAIN 2 79 GST N-terminal.
DOMAIN 81 199 GST C-terminal.
REGION 49 51 Glutathione binding.
{ECO:0000269|PubMed:9323136}.
REGION 63 64 Glutathione binding.
{ECO:0000269|PubMed:9323136}.
BINDING 8 8 Glutathione.
{ECO:0000269|PubMed:9323136}.
BINDING 14 14 Glutathione.
{ECO:0000269|PubMed:9323136}.
BINDING 39 39 Glutathione.
{ECO:0000269|PubMed:9323136}.
MUTAGEN 8 8 Y->F: Moderate reduction of protein
expression levels. Abolishes both
prostaglandin D synthase and glutathione-
conjugating activities.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 14 14 R->E: Moderate reduction of protein
expression levels. Abolishes both
prostaglandin D synthase and glutathione-
conjugating activities.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 14 14 R->K: Moderate reduction of protein
expression levels. Abolishes both
prostaglandin D synthase and glutathione-
conjugating activities.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 104 104 W->I: No significant effect on protein
expression levels. Abolishes both
prostaglandin D synthase and glutathione-
conjugating activities.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 112 112 K->E: Significant reduction of protein
expression levels. Significantly reduces
prostaglandin D synthase and moderately
reduces glutathione-conjugating
activities.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 152 152 Y->F: Significant reduction of protein
expression levels. Moderately reduces
prostaglandin D synthase activity.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 156 156 C->L: No significant effect on protein
expression levels. Abolishes
prostaglandin D synthase and
significantly reduces glutathione-
conjugating activities.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 156 156 C->Y: Significant reduction of protein
expression levels. Abolishes
prostaglandin D synthase and
significantly reduces glutathione-
conjugating activities.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 198 198 K->E: Moderate reduction of protein
expression levels. No significant effect
on catalytic activities.
{ECO:0000269|PubMed:10871602}.
MUTAGEN 199 199 L->F: Moderate reduction of protein
expression levels. No significant effect
on catalytic activities.
{ECO:0000269|PubMed:10871602}.
CONFLICT 194 194 R -> S (in Ref. 4; AAB72099).
{ECO:0000305}.
STRAND 4 12 {ECO:0000244|PDB:1PD2}.
TURN 13 15 {ECO:0000244|PDB:1PD2}.
HELIX 16 24 {ECO:0000244|PDB:1PD2}.
STRAND 30 34 {ECO:0000244|PDB:1PD2}.
TURN 36 38 {ECO:0000244|PDB:1PD2}.
HELIX 39 42 {ECO:0000244|PDB:1PD2}.
HELIX 43 45 {ECO:0000244|PDB:1PD2}.
STRAND 53 56 {ECO:0000244|PDB:1PD2}.
STRAND 59 62 {ECO:0000244|PDB:1PD2}.
HELIX 64 71 {ECO:0000244|PDB:1PD2}.
TURN 72 74 {ECO:0000244|PDB:1PD2}.
HELIX 76 78 {ECO:0000244|PDB:1PD2}.
HELIX 82 99 {ECO:0000244|PDB:1PD2}.
HELIX 109 122 {ECO:0000244|PDB:1PD2}.
HELIX 124 135 {ECO:0000244|PDB:1PD2}.
STRAND 139 145 {ECO:0000244|PDB:1PD2}.
HELIX 148 163 {ECO:0000244|PDB:1PD2}.
TURN 165 170 {ECO:0000244|PDB:1PD2}.
HELIX 172 183 {ECO:0000244|PDB:1PD2}.
HELIX 185 193 {ECO:0000244|PDB:1PD2}.
SEQUENCE 199 AA; 23297 MW; E5EF934D89DC240F CRC64;
MPNYKLLYFN MRGRAEIIRY IFAYLDIKYE DHRIEQADWP KIKPTLPFGK IPVLEVEGLT
LHQSLAIARY LTKNTDLAGK TELEQCQVDA VVDTLDDFMS LFPWAEENQD LKERTFNDLL
TRQAPHLLKD LDTYLGDKEW FIGNYVTWAD FYWDICSTTL LVLKPDLLGI YPRLVSLRNK
VQAIPAISAW ILKRPQTKL


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