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Q9JHF7

- HPGDS_MOUSE

UniProt

Q9JHF7 - HPGDS_MOUSE

Protein

Hematopoietic prostaglandin D synthase

Gene

Hpgds

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (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.2 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.1 Publication
    RX + glutathione = HX + R-S-glutathione.1 Publication

    Cofactori

    Glutathione. Required for the prostaglandin D synthase activity.1 Publication

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. prostaglandin biosynthetic process Source: UniProtKB-KW
    2. prostaglandin metabolic process Source: MGI

    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_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_215316. Glutathione conjugation.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1859384. Hpgds.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 199199Hematopoietic prostaglandin D synthasePRO_0000185935Add
    BLAST

    Proteomic databases

    MaxQBiQ9JHF7.
    PaxDbiQ9JHF7.
    PRIDEiQ9JHF7.

    PTM databases

    PhosphoSiteiQ9JHF7.

    Expressioni

    Tissue specificityi

    Expressed in skin and oviduct.1 Publication

    Gene expression databases

    BgeeiQ9JHF7.
    CleanExiMM_PTGDS2.
    GenevestigatoriQ9JHF7.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000031982.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JHF7.
    SMRiQ9JHF7. Positions 1-199.
    ModBaseiSearch...
    MobiDBiSearch...

    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 bindingBy similarity

    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.
    InParanoidiQ8CA80.
    KOiK01830.
    OMAiMSCFPWA.
    OrthoDBiEOG78WKT1.
    PhylomeDBiQ9JHF7.
    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.

    Q9JHF7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNYKLLYFN MRGRAEIIRY IFAYLDIKYE DHRIEQADWP KIKPTLPFGK    50
    IPVLEVEGLT IHQSLAIARY LTKNTDLAGK TALEQCQADA VVDTLDDFMS 100
    LFPWAEKDQD LKERMFNELL THQAPRLLKD LDTYLGDKEW FIGNYVTWAD 150
    FYWDICSTTL LVLKPGLLDI YPKLVSLRNK VQAIPAISAW ILKRPQTKL 199
    Length:199
    Mass (Da):23,227
    Last modified:January 23, 2007 - v3
    Checksum:iE5E7E4B56493F720
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081D → G in BAC30336. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008824 Genomic DNA. Translation: BAA97557.1.
    D82072 mRNA. Translation: BAA96845.1.
    AK020246 mRNA. Translation: BAB32037.1.
    AK039392 mRNA. Translation: BAC30336.1.
    CH466523 Genomic DNA. Translation: EDK98774.1.
    BC116735 mRNA. Translation: AAI16736.1.
    BC116737 mRNA. Translation: AAI16738.1.
    CCDSiCCDS20205.1.
    RefSeqiNP_062328.3. NM_019455.4.
    UniGeneiMm.410688.

    Genome annotation databases

    EnsembliENSMUST00000031982; ENSMUSP00000031982; ENSMUSG00000029919.
    GeneIDi54486.
    KEGGimmu:54486.
    UCSCiuc009cee.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008824 Genomic DNA. Translation: BAA97557.1 .
    D82072 mRNA. Translation: BAA96845.1 .
    AK020246 mRNA. Translation: BAB32037.1 .
    AK039392 mRNA. Translation: BAC30336.1 .
    CH466523 Genomic DNA. Translation: EDK98774.1 .
    BC116735 mRNA. Translation: AAI16736.1 .
    BC116737 mRNA. Translation: AAI16738.1 .
    CCDSi CCDS20205.1.
    RefSeqi NP_062328.3. NM_019455.4.
    UniGenei Mm.410688.

    3D structure databases

    ProteinModelPortali Q9JHF7.
    SMRi Q9JHF7. Positions 1-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000031982.

    Chemistry

    BindingDBi Q9JHF7.

    PTM databases

    PhosphoSitei Q9JHF7.

    Proteomic databases

    MaxQBi Q9JHF7.
    PaxDbi Q9JHF7.
    PRIDEi Q9JHF7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031982 ; ENSMUSP00000031982 ; ENSMUSG00000029919 .
    GeneIDi 54486.
    KEGGi mmu:54486.
    UCSCi uc009cee.2. mouse.

    Organism-specific databases

    CTDi 27306.
    MGIi MGI:1859384. Hpgds.

    Phylogenomic databases

    eggNOGi NOG122057.
    GeneTreei ENSGT00670000097856.
    HOGENOMi HOG000115733.
    HOVERGENi HBG105321.
    InParanoidi Q8CA80.
    KOi K01830.
    OMAi MSCFPWA.
    OrthoDBi EOG78WKT1.
    PhylomeDBi Q9JHF7.
    TreeFami TF105321.

    Enzyme and pathway databases

    Reactomei REACT_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_215316. Glutathione conjugation.

    Miscellaneous databases

    NextBioi 311352.
    PROi Q9JHF7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JHF7.
    CleanExi MM_PTGDS2.
    Genevestigatori Q9JHF7.

    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. "Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase."
      Kanaoka Y., Fujimori K., Kikuno R., Sakaguchi Y., Urade Y., Hayaishi O.
      Eur. J. Biochem. 267:3315-3322(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY.
      Strain: 129/Sv and C57BL/6.
      Tissue: Oviduct.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Colon and Spinal cord.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. "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.

    Entry informationi

    Entry nameiHPGDS_MOUSE
    AccessioniPrimary (citable) accession number: Q9JHF7
    Secondary accession number(s): Q14AR4, Q8CA80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 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

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3