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Protein

Hematopoietic prostaglandin D synthase

Gene

Hpgds

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.4 Publications
RX + glutathione = HX + R-S-glutathione.3 Publications

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
  1. Vmax=17.6 µmol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate2 Publications
  2. Vmax=9.2 µmol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate2 Publications
  3. Vmax=48.3 µmol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate2 Publications
  4. Vmax=17.9 µmol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate2 Publications
  5. Vmax=0.35 µmol/min/mg enzyme with cumene hydroperoxide as substrate2 Publications
  6. Vmax=10.2 µmol/min/mg enzyme with allyl isothiocyanate as substrate2 Publications
  7. Vmax=11.3 µmol/min/mg enzyme with benzyl isothiocyanate as substrate2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8Glutathione1 Publication1
Binding sitei14Glutathione1 Publication1
Binding sitei39Glutathione1 Publication1

GO - Molecular functioni

GO - Biological processi

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

BRENDAi5.3.99.2. 5301.
ReactomeiR-RNO-156590. Glutathione conjugation.
R-RNO-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RKO35543.

Names & Taxonomyi

Protein namesi
Recommended name:
Hematopoietic prostaglandin D synthase (EC:5.3.99.24 Publications)
Short name:
H-PGDS
Alternative name(s):
GST class-sigma
Glutathione S-transferase (EC:2.5.1.183 Publications)
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
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi69251. Hpgds.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi8Y → F: Moderate reduction of protein expression levels. Abolishes both prostaglandin D synthase and glutathione-conjugating activities. 1 Publication1
Mutagenesisi14R → E: Moderate reduction of protein expression levels. Abolishes both prostaglandin D synthase and glutathione-conjugating activities. 1 Publication1
Mutagenesisi14R → K: Moderate reduction of protein expression levels. Abolishes both prostaglandin D synthase and glutathione-conjugating activities. 1 Publication1
Mutagenesisi104W → I: No significant effect on protein expression levels. Abolishes both prostaglandin D synthase and glutathione-conjugating activities. 1 Publication1
Mutagenesisi112K → E: Significant reduction of protein expression levels. Significantly reduces prostaglandin D synthase and moderately reduces glutathione-conjugating activities. 1 Publication1
Mutagenesisi152Y → F: Significant reduction of protein expression levels. Moderately reduces prostaglandin D synthase activity. 1 Publication1
Mutagenesisi156C → L: No significant effect on protein expression levels. Abolishes prostaglandin D synthase and significantly reduces glutathione-conjugating activities. 1 Publication1
Mutagenesisi156C → Y: Significant reduction of protein expression levels. Abolishes prostaglandin D synthase and significantly reduces glutathione-conjugating activities. 1 Publication1
Mutagenesisi198K → E: Moderate reduction of protein expression levels. No significant effect on catalytic activities. 1 Publication1
Mutagenesisi199L → F: Moderate reduction of protein expression levels. No significant effect on catalytic activities. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001859361 – 199Hematopoietic prostaglandin D synthaseAdd BLAST199

Proteomic databases

PaxDbiO35543.
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

BgeeiENSRNOG00000006583.
GenevisibleiO35543. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008826.

Structurei

Secondary structure

1199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Turni13 – 15Combined sources3
Helixi16 – 24Combined sources9
Beta strandi30 – 34Combined sources5
Turni36 – 38Combined sources3
Helixi39 – 42Combined sources4
Helixi43 – 45Combined sources3
Beta strandi53 – 56Combined sources4
Beta strandi59 – 62Combined sources4
Helixi64 – 71Combined sources8
Turni72 – 74Combined sources3
Helixi76 – 78Combined sources3
Helixi82 – 99Combined sources18
Helixi109 – 122Combined sources14
Helixi124 – 135Combined sources12
Beta strandi139 – 145Combined sources7
Helixi148 – 163Combined sources16
Turni165 – 170Combined sources6
Helixi172 – 183Combined sources12
Helixi185 – 193Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO35543.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 79GST N-terminalAdd BLAST78
Domaini81 – 199GST C-terminalAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 51Glutathione binding1 Publication3
Regioni63 – 64Glutathione binding1 Publication2

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

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115733.
HOVERGENiHBG105321.
InParanoidiO35543.
KOiK04097.
OMAiAIAAWIQ.
OrthoDBiEOG091G0MBB.
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]
PfamiPF14497. GST_C_3. 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 differs from that shown. Reason: Frameshift at positions 73 and 113.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti194R → S in AAB72099 (Ref. 4) Curated1

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.
RefSeqiNP_113832.1. NM_031644.2.
UniGeneiRn.10837.

3D structure databases

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000008826.

Proteomic databases

PaxDbiO35543.
PRIDEiO35543.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi27306.
RGDi69251. Hpgds.

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115733.
HOVERGENiHBG105321.
InParanoidiO35543.
KOiK04097.
OMAiAIAAWIQ.
OrthoDBiEOG091G0MBB.
PhylomeDBiO35543.
TreeFamiTF105321.

Enzyme and pathway databases

BRENDAi5.3.99.2. 5301.
ReactomeiR-RNO-156590. Glutathione conjugation.
R-RNO-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RKO35543.

Miscellaneous databases

EvolutionaryTraceiO35543.
PROiO35543.

Gene expression databases

BgeeiENSRNOG00000006583.
GenevisibleiO35543. RN.

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]
PfamiPF14497. GST_C_3. 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]
ProtoNetiSearch...

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 2, 2016
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.