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GSTA3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1TDI, 2VCV
Identifiers
Aliases	GSTA3, GSTA3-3, GTA3, glutathione S-transferase alpha 3
External IDs	OMIM: 605449; MGI: 95856; HomoloGene: 37355; GeneCards: GSTA3; OMA:GSTA3 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6p12.2 Start 52,896,639 bp End 52,909,698 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 A4|1 6.5 cM Start 21,310,813 bp End 21,335,885 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube right adrenal gland right adrenal cortex bronchial epithelial cell left adrenal cortex placenta kidney tubule testicle epithelium of nasopharynx skin of abdomen Top expressed in left lobe of liver right lung lobe stroma of bone marrow lacrimal gland white adipose tissue right kidney parotid gland human kidney olfactory epithelium gastric mucosa More reference expression data BioGPS More reference expression data
Gene ontology Molecular function glutathione transferase activity transferase activity Cellular component extracellular exosome cytoplasm cytosol Biological process metabolism glutathione derivative biosynthetic process glutathione metabolic process xenobiotic metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2940 14859 Ensembl ENSG00000174156 ENSMUSG00000025934 UniProt Q16772 P30115 RefSeq (mRNA) NM_000847 NM_001363542 NM_001077353 NM_001288617 NM_010356 RefSeq (protein) NP_000838 NP_001350471 NP_001070821 NP_001275546 NP_034486 Location (UCSC) Chr 6: 52.9 – 52.91 Mb Chr 1: 21.31 – 21.34 Mb PubMed search
Wikidata
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Glutathione S-transferase A3 is an enzyme that in humans is encoded by the GSTA3 gene.

Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes are involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. At present, eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta and zeta. This gene encodes a glutathione S-transferase belonging to the alpha class genes that are located in a cluster mapped to chromosome 6. Genes of the alpha class are highly related and encode enzymes with glutathione peroxidase activity. However, during evolution, this alpha class gene diverged accumulating mutations in the active site that resulted in differences in substrate specificity and catalytic activity. The enzyme encoded by this gene catalyzes the double bond isomerization of precursors for progesterone and testosterone during the biosynthesis of steroid hormones. An additional transcript variant has been identified, but its full length sequence has not been determined.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000174156 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000025934 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Suzuki T, Johnston PN, Board PG (Mar 1994). "Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes". Genomics. 18 (3): 680–6. doi:10.1016/S0888-7543(05)80373-8. PMID 8307579.
6. Board PG (Apr 1998). "Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4". Biochem J. 330 (2): 827–31. doi:10.1042/bj3300827. PMC 1219212. PMID 9480897.
7. ^ "Entrez Gene: GSTA3 glutathione S-transferase A3".

Further reading

• Johansson AS, Mannervik B (2001). "Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones". J. Biol. Chem. 276 (35): 33061–5. doi:10.1074/jbc.M104539200. PMID 11418619.
• Johansson AS, Mannervik B (2002). "Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3". J. Biol. Chem. 277 (19): 16648–54. doi:10.1074/jbc.M201062200. PMID 11872752.
• 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.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
• Tetlow N, Coggan M, Casarotto MG, Board PG (2005). "Functional polymorphism of human glutathione transferase A3: effects on xenobiotic metabolism and steroid biosynthesis". Pharmacogenetics. 14 (10): 657–63. doi:10.1097/00008571-200410000-00003. PMID 15454730.
• 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.
• Gu Y, Guo J, Pal A, et al. (2005). "Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity". Biochemistry. 43 (50): 15673–9. doi:10.1021/bi048757g. PMID 15595823.
• Suzuki T, Delgado-Escueta AV, Alonso ME, et al. (2006). "Mutation analyses of genes on 6p12-p11 in patients with juvenile myoclonic epilepsy". Neurosci. Lett. 405 (1–2): 126–31. doi:10.1016/j.neulet.2006.06.038. PMID 16876319. S2CID 20526126.

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