PGDS

HPGDS
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1IYH, 1IYI, 1V40, 2CVD, 2VCQ, 2VCW, 2VCX, 2VCZ, 2VD0, 2VD1, 3EE2, 3KXO, 3VI5, 3VI7, 4EC0, 4EDY, 4EDZ, 4EE0, 5AIS, 5AIV, 5AIX
Identifiers
Aliases	HPGDS, GSTS, GSTS1-1, PGD2, PGDS, GSTS1, hematopoietic prostaglandin D synthase
External IDs	OMIM: 602598 MGI: 1859384 HomoloGene: 113741 GeneCards: HPGDS
EC number	2.5.1.18
Gene location (Human) Chr. Chromosome 4 (human) Band 4q22.3 Start 94,298,535 bp End 94,342,876 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 C1 Start 65,094,277 bp End 65,121,892 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in placenta Achilles tendon gallbladder synovial membrane amniotic fluid rectum synovial joint upper lobe of left lung optic nerve right coronary artery Top expressed in calvaria Sertoli cell yolk sac ooblast cornea uterus thyroid gland superior frontal gyrus neural tube thymus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity calcium ion binding protein homodimerization activity isomerase activity metal ion binding prostaglandin-D synthase activity protein binding magnesium ion binding glutathione transferase activity Cellular component cytoplasm cytosol Biological process prostaglandin metabolic process locomotory behavior lipid metabolism cyclooxygenase pathway fatty acid metabolic process fatty acid biosynthetic process prostaglandin biosynthetic process glutathione derivative biosynthetic process signal transduction negative regulation of male germ cell proliferation glutathione metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27306 54486 Ensembl ENSG00000163106 ENSMUSG00000029919 UniProt O60760 Q9JHF7 RefSeq (mRNA) NM_014485 NM_019455 RefSeq (protein) NP_055300 NP_062328 Location (UCSC) Chr 4: 94.3 – 94.34 Mb Chr 6: 65.09 – 65.12 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

PGDS protein is a protein that in humans is encoded by the HPGDS gene.

Prostaglandin-D synthase is a sigma class glutathione-S-transferase family member. The enzyme catalyzes the conversion of PGH2 to PGD2 and plays a role in the production of prostanoids in the immune system and mast cells. The presence of this enzyme can be used to identify the differentiation stage of human megakaryocytes.

See also

• Prostaglandin D2 synthase PTGDS

Further reading

• Kanaoka Y, Urade Y (2004). "Hematopoietic prostaglandin D synthase". Prostaglandins Leukot. Essent. Fatty Acids. 69 (2–3): 163–7. doi:10.1016/S0952-3278(03)00077-2. PMID 12895599.
• Suzuki T, Watanabe K, Kanaoka Y, et al. (1998). "Induction of hematopoietic prostaglandin D synthase in human megakaryocytic cells by phorbol ester". Biochem. Biophys. Res. Commun. 241 (2): 288–93. doi:10.1006/bbrc.1997.7803. PMID 9425264.
• Tokugawa Y, Kunishige I, Kubota Y, et al. (1998). "Lipocalin-type prostaglandin D synthase in human male reproductive organs and seminal plasma". Biol. Reprod. 58 (2): 600–7. doi:10.1095/biolreprod58.2.600. PMID 9475419.
• Pinzar E, Kanaoka Y, Inui T, et al. (2000). "Prostaglandin D synthase gene is involved in the regulation of non-rapid eye movement sleep". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4903–7. Bibcode:2000PNAS...97.4903P. doi:10.1073/pnas.090093997. PMC 18330. PMID 10781097.
• Kanaoka Y, Fujimori K, Kikuno R, et al. (2000). "Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase. Conservation of the ancestral genomic structure of sigma-class glutathione S-transferase". Eur. J. Biochem. 267 (11): 3315–22. doi:10.1046/j.1432-1327.2000.01362.x. PMID 10824118.
• Fujimori K, Kanaoka Y, Sakaguchi Y, Urade Y (2001). "Transcriptional activation of the human hematopoietic prostaglandin D synthase gene in megakaryoblastic cells. Roles of the oct-1 element in the 5'-flanking region and the AP-2 element in the untranslated exon 1". J. Biol. Chem. 275 (51): 40511–6. doi:10.1074/jbc.M007688200. PMID 10998423.
• Sui D, Wilson JE (2000). "Interaction of insulin-like growth factor binding protein-4, Miz-1, leptin, lipocalin-type prostaglandin D synthase, and granulin precursor with the N-terminal half of type III hexokinase". Arch. Biochem. Biophys. 382 (2): 262–74. doi:10.1006/abbi.2000.2019. PMID 11068878.
• Noguchi E, Shibasaki M, Kamioka M, et al. (2002). "New polymorphisms of haematopoietic prostaglandin D synthase and human prostanoid DP receptor genes". Clin. Exp. Allergy. 32 (1): 93–6. doi:10.1046/j.0022-0477.2001.01261.x. PMID 12002745. S2CID 24779233.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Inoue T, Irikura D, Okazaki N, et al. (2003). "Mechanism of metal activation of human hematopoietic prostaglandin D synthase". Nat. Struct. Biol. 10 (4): 291–6. doi:10.1038/nsb907. PMID 12627223. S2CID 25214344.
• Ando M, Murakami Y, Kojima F, et al. (2003). "Retrovirally introduced prostaglandin D2 synthase suppresses lung injury induced by bleomycin". Am. J. Respir. Cell Mol. Biol. 28 (5): 582–91. doi:10.1165/rcmb.2002-0162OC. PMID 12707014.
• Inoue T, Okano Y, Kado Y, et al. (2005). "First determination of the inhibitor complex structure of human hematopoietic prostaglandin D synthase". J. Biochem. 135 (3): 279–83. doi:10.1093/jb/mvh033. PMID 15113825.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.