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Protein

Hematopoietic prostaglandin D synthase

Gene

Hpgds

Organism
Mus musculus (Mouse)
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.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

glutathione1 PublicationNote: Glutathione is 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

GO - Biological processi

  • negative regulation of male germ cell proliferation Source: MGI
  • prostaglandin biosynthetic process Source: UniProtKB-KW
  • prostaglandin metabolic process Source: MGI
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_317599. Glutathione conjugation.
REACT_349058. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

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 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1859384. Hpgds.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.
GenevisibleiQ9JHF7. MM.

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.
InParanoidiQ9JHF7.
KOiK01830.
OMAiTEMEQCH.
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

        10         20         30         40         50
MPNYKLLYFN MRGRAEIIRY IFAYLDIKYE DHRIEQADWP KIKPTLPFGK
60 70 80 90 100
IPVLEVEGLT IHQSLAIARY LTKNTDLAGK TALEQCQADA VVDTLDDFMS
110 120 130 140 150
LFPWAEKDQD LKERMFNELL THQAPRLLKD LDTYLGDKEW FIGNYVTWAD
160 170 180 190
FYWDICSTTL LVLKPGLLDI YPKLVSLRNK VQAIPAISAW ILKRPQTKL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031982.

Chemistry

BindingDBiQ9JHF7.

PTM databases

PhosphoSiteiQ9JHF7.

Proteomic databases

MaxQBiQ9JHF7.
PaxDbiQ9JHF7.
PRIDEiQ9JHF7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi27306.
MGIiMGI:1859384. Hpgds.

Phylogenomic databases

eggNOGiNOG122057.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115733.
HOVERGENiHBG105321.
InParanoidiQ9JHF7.
KOiK01830.
OMAiTEMEQCH.
OrthoDBiEOG78WKT1.
PhylomeDBiQ9JHF7.
TreeFamiTF105321.

Enzyme and pathway databases

ReactomeiREACT_317599. Glutathione conjugation.
REACT_349058. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

NextBioi311352.
PROiQ9JHF7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHF7.
CleanExiMM_PTGDS2.
GenevisibleiQ9JHF7. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 116 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

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 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.