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O35543

- HPGDS_RAT

UniProt

O35543 - HPGDS_RAT

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Protein

Hematopoietic prostaglandin D synthase

Gene

Hpgds

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

(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.
RX + glutathione = HX + R-S-glutathione.

Cofactori

glutathione2 PublicationsNote: Glutathione is required for the prostaglandin D synthase activity.2 Publications

Kineticsi

  1. KM=100 µM for glutathione for the prostaglandin D synthase activity2 Publications
  2. KM=500 µM for glutathione for the glutathione-conjugating activity2 Publications
  3. KM=500 µM for PGH2 for the prostaglandin D synthase activity2 Publications
  4. KM=3 mM for 1-chloro-2,4-dinitrobenzene2 Publications

Vmax=17.6 µmol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate2 Publications

Vmax=9.2 µmol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate2 Publications

Vmax=48.3 µmol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate2 Publications

Vmax=17.9 µmol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate2 Publications

Vmax=0.35 µmol/min/mg enzyme with cumene hydroperoxide as substrate2 Publications

Vmax=10.2 µmol/min/mg enzyme with allyl isothiocyanate as substrate2 Publications

Vmax=11.3 µmol/min/mg enzyme with benzyl isothiocyanate as substrate2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Glutathione1 Publication
Binding sitei14 – 141Glutathione1 Publication
Binding sitei39 – 391Glutathione1 Publication
Binding sitei51 – 511Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. glutathione transferase activity Source: UniProtKB-EC
  3. magnesium ion binding Source: UniProtKB
  4. prostaglandin-D synthase activity Source: UniProtKB

GO - Biological processi

  1. prostaglandin biosynthetic process Source: RGD
  2. prostaglandin metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Enzyme and pathway databases

ReactomeiREACT_194948. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_251519. Glutathione conjugation.
SABIO-RKO35543.

Names & Taxonomyi

Protein namesi
Recommended name:
Hematopoietic prostaglandin D synthase (EC:5.3.99.2)
Short name:
H-PGDS
Alternative name(s):
GST class-sigma
Glutathione S-transferase (EC:2.5.1.18)
Glutathione-dependent PGD synthase
Glutathione-requiring prostaglandin D synthase
Prostaglandin-H2 D-isomerase
Gene namesi
Name:Hpgds
Synonyms:Gsts, Pgds, Ptgds2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 4

Organism-specific databases

RGDi69251. Hpgds.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81Y → F: Moderate reduction of protein expression levels. Abolishes both prostaglandin D synthase and glutathione-conjugating activities. 1 Publication
Mutagenesisi14 – 141R → E: Moderate reduction of protein expression levels. Abolishes both prostaglandin D synthase and glutathione-conjugating activities. 1 Publication
Mutagenesisi14 – 141R → K: Moderate reduction of protein expression levels. Abolishes both prostaglandin D synthase and glutathione-conjugating activities. 1 Publication
Mutagenesisi104 – 1041W → I: No significant effect on protein expression levels. Abolishes both prostaglandin D synthase and glutathione-conjugating activities. 1 Publication
Mutagenesisi112 – 1121K → E: Significant reduction of protein expression levels. Significantly reduces prostaglandin D synthase and moderately reduces glutathione-conjugating activities. 1 Publication
Mutagenesisi152 – 1521Y → F: Significant reduction of protein expression levels. Moderately reduces prostaglandin D synthase activity. 1 Publication
Mutagenesisi156 – 1561C → L: No significant effect on protein expression levels. Abolishes prostaglandin D synthase and significantly reduces glutathione-conjugating activities. 1 Publication
Mutagenesisi156 – 1561C → Y: Significant reduction of protein expression levels. Abolishes prostaglandin D synthase and significantly reduces glutathione-conjugating activities. 1 Publication
Mutagenesisi198 – 1981K → E: Moderate reduction of protein expression levels. No significant effect on catalytic activities. 1 Publication
Mutagenesisi199 – 1991L → F: Moderate reduction of protein expression levels. No significant effect on catalytic activities. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Hematopoietic prostaglandin D synthasePRO_0000185936Add
BLAST

Proteomic databases

PRIDEiO35543.

Expressioni

Tissue specificityi

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).2 Publications

Gene expression databases

GenevestigatoriO35543.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Turni13 – 153Combined sources
Helixi16 – 249Combined sources
Beta strandi30 – 345Combined sources
Turni36 – 383Combined sources
Helixi39 – 424Combined sources
Helixi43 – 453Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 624Combined sources
Helixi64 – 718Combined sources
Turni72 – 743Combined sources
Helixi76 – 783Combined sources
Helixi82 – 9918Combined sources
Helixi109 – 12214Combined sources
Helixi124 – 13512Combined sources
Beta strandi139 – 1457Combined sources
Helixi148 – 16316Combined sources
Turni165 – 1706Combined sources
Helixi172 – 18312Combined sources
Helixi185 – 1939Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PD2X-ray2.301/21-199[»]
ProteinModelPortaliO35543.
SMRiO35543. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35543.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7978GST N-terminalAdd
BLAST
Domaini81 – 199119GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni63 – 642Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Sigma family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG122057.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115733.
HOVERGENiHBG105321.
InParanoidiO35543.
KOiK01830.
OMAiNIEMKAN.
OrthoDBiEOG78WKT1.
PhylomeDBiO35543.
TreeFamiTF105321.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35543-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPNYKLLYFN MRGRAEIIRY IFAYLDIKYE DHRIEQADWP KIKPTLPFGK
60 70 80 90 100
IPVLEVEGLT LHQSLAIARY LTKNTDLAGK TELEQCQVDA VVDTLDDFMS
110 120 130 140 150
LFPWAEENQD LKERTFNDLL TRQAPHLLKD LDTYLGDKEW FIGNYVTWAD
160 170 180 190
FYWDICSTTL LVLKPDLLGI YPRLVSLRNK VQAIPAISAW ILKRPQTKL
Length:199
Mass (Da):23,297
Last modified:January 23, 2007 - v3
Checksum:iE5EF934D89DC240F
GO

Sequence cautioni

The sequence AAB72099.1 differs from that shown. Reason: Frameshift at positions 73 and 113. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti194 – 1941R → S in AAB72099. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82071 mRNA. Translation: BAA22898.1.
BC087590 mRNA. Translation: AAH87590.1.
AF021882 mRNA. Translation: AAB72099.1. Frameshift.
RefSeqiNP_113832.1. NM_031644.2.
UniGeneiRn.10837.

Genome annotation databases

EnsembliENSRNOT00000008826; ENSRNOP00000008826; ENSRNOG00000006583.
GeneIDi58962.
KEGGirno:58962.
UCSCiRGD:69251. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82071 mRNA. Translation: BAA22898.1 .
BC087590 mRNA. Translation: AAH87590.1 .
AF021882 mRNA. Translation: AAB72099.1 . Frameshift.
RefSeqi NP_113832.1. NM_031644.2.
UniGenei Rn.10837.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PD2 X-ray 2.30 1/2 1-199 [» ]
ProteinModelPortali O35543.
SMRi O35543. Positions 1-199.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi O35543.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000008826 ; ENSRNOP00000008826 ; ENSRNOG00000006583 .
GeneIDi 58962.
KEGGi rno:58962.
UCSCi RGD:69251. rat.

Organism-specific databases

CTDi 27306.
RGDi 69251. Hpgds.

Phylogenomic databases

eggNOGi NOG122057.
GeneTreei ENSGT00670000097856.
HOGENOMi HOG000115733.
HOVERGENi HBG105321.
InParanoidi O35543.
KOi K01830.
OMAi NIEMKAN.
OrthoDBi EOG78WKT1.
PhylomeDBi O35543.
TreeFami TF105321.

Enzyme and pathway databases

Reactomei REACT_194948. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_251519. Glutathione conjugation.
SABIO-RK O35543.

Miscellaneous databases

EvolutionaryTracei O35543.
NextBioi 611604.
PROi O35543.

Gene expression databases

Genevestigatori O35543.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and crystal structure of hematopoietic prostaglandin D synthase."
    Kanaoka Y., Ago H., Inagaki E., Nanayama T., Miyano M., Kikuno R., Fujii Y., Eguchi N., Toh H., Urade Y., Hayaishi O.
    Cell 90:1085-1095(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Spleen.
  2. "Mammalian class Sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases."
    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.
    Biochem. J. 359:507-516(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Spleen.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  4. "Purification and cloning of rat glutathione-dependent prostaglandin D synthase."
    Yuan Y., Reddy R.G., Kim H.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 39-198.
    Strain: Sprague-Dawley.
    Tissue: Spleen.
  5. "Structural basis of hematopoietic prostaglandin D synthase activity elucidated by site-directed mutagenesis."
    Pinzar E., Miyano M., Kanaoka Y., Urade Y., Hayaishi O.
    J. Biol. Chem. 275:31239-31244(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-8; ARG-14; TRP-104; LYS-112; TYR-152; CYS-156; LYS-198 AND LEU-199.
  6. "Structural and functional characterization of HQL-79, an orally selective inhibitor of human hematopoietic prostaglandin D synthase."
    Aritake K., Kado Y., Inoue T., Miyano M., Urade Y.
    J. Biol. Chem. 281:15277-15286(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiHPGDS_RAT
AccessioniPrimary (citable) accession number: O35543
Secondary accession number(s): O35351
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3