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Q9JHF7 (HPGDS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Hematopoietic prostaglandin D synthase
Short name=H-PGDS
EC=5.3.99.2
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 names
Name:Hpgds
Synonyms:Gsts, Pgds, Ptgds2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5

Catalytic activity

(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. Ref.1

RX + glutathione = HX + R-S-glutathione. Ref.1

Cofactor

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in skin and oviduct. Ref.1

Sequence similarities

Belongs to the GST superfamily. Sigma family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 199198Hematopoietic prostaglandin D synthase
PRO_0000185935

Regions

Domain2 – 7978GST N-terminal
Domain81 – 199119GST C-terminal
Region63 – 642Glutathione binding By similarity

Sites

Binding site81Glutathione By similarity
Binding site141Glutathione By similarity
Binding site391Glutathione By similarity
Binding site511Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Experimental info

Sequence conflict1081D → G in BAC30336. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JHF7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E5E7E4B56493F720

FASTA19923,227
        10         20         30         40         50         60 
MPNYKLLYFN MRGRAEIIRY IFAYLDIKYE DHRIEQADWP KIKPTLPFGK IPVLEVEGLT 

        70         80         90        100        110        120 
IHQSLAIARY LTKNTDLAGK TALEQCQADA VVDTLDDFMS LFPWAEKDQD LKERMFNELL 

       130        140        150        160        170        180 
THQAPRLLKD LDTYLGDKEW FIGNYVTWAD FYWDICSTTL LVLKPGLLDI YPKLVSLRNK 

       190 
VQAIPAISAW ILKRPQTKL

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00331387.
RefSeqNP_062328.3. NM_019455.4.
UniGeneMm.410688.

3D structure databases

ProteinModelPortalQ9JHF7.
SMRQ9JHF7. Positions 1-199.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000031982.

PTM databases

PhosphoSiteQ9JHF7.

Proteomic databases

PaxDbQ9JHF7.
PRIDEQ9JHF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031982; ENSMUSP00000031982; ENSMUSG00000029919.
GeneID54486.
KEGGmmu:54486.
UCSCuc009cee.2. mouse.

Organism-specific databases

CTD27306.
MGIMGI:1859384. Hpgds.

Phylogenomic databases

eggNOGNOG122057.
GeneTreeENSGT00550000074559.
HOGENOMHOG000115733.
HOVERGENHBG105321.
InParanoidQ8CA80.
KOK01830.
OMAMSCFPWA.
OrthoDBEOG4H9XMH.

Gene expression databases

BgeeQ9JHF7.
CleanExMM_PTGDS2.
GenevestigatorQ9JHF7.
GermOnlineENSMUSG00000029919. Mus musculus.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ9JHF7.
NextBio311352.
SOURCESearch...

Entry information

Entry nameHPGDS_MOUSE
AccessionPrimary (citable) accession number: Q9JHF7
Secondary accession number(s): Q14AR4, Q8CA80
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents