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O35543

- HPGDS_RAT

UniProt

O35543 - HPGDS_RAT

Protein

Hematopoietic prostaglandin D synthase

Gene

Hpgds

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    Glutathione. 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

    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).
    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-SubCell
    2. nucleus Source: Ensembl

    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 – 129
    Turni13 – 153
    Helixi16 – 249
    Beta strandi30 – 345
    Turni36 – 383
    Helixi39 – 424
    Helixi43 – 453
    Beta strandi53 – 564
    Beta strandi59 – 624
    Helixi64 – 718
    Turni72 – 743
    Helixi76 – 783
    Helixi82 – 9918
    Helixi109 – 12214
    Helixi124 – 13512
    Beta strandi139 – 1457
    Helixi148 – 16316
    Turni165 – 1706
    Helixi172 – 18312
    Helixi185 – 1939

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MPNYKLLYFN MRGRAEIIRY IFAYLDIKYE DHRIEQADWP KIKPTLPFGK    50
    IPVLEVEGLT LHQSLAIARY LTKNTDLAGK TELEQCQVDA VVDTLDDFMS 100
    LFPWAEENQD LKERTFNDLL TRQAPHLLKD LDTYLGDKEW FIGNYVTWAD 150
    FYWDICSTTL LVLKPDLLGI YPRLVSLRNK VQAIPAISAW ILKRPQTKL 199
    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.

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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).
    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

    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: October 1, 2014
    This is version 125 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