GPX3

glutathione peroxidase 3 (plasma)

PDB rendering based on 2r37.

Available structures
PDB	2r37

Identifiers

Symbol

GPX3

External IDs

OMIM: 138321 MGI: 105102 HomoloGene: 20480 GeneCards: GPX3 Gene

EC number

1.11.1.9

Gene Ontology
Molecular function	• glutathione binding • glutathione peroxidase activity • selenium binding • transcription factor binding • oxidoreductase activity
Cellular component	• extracellular space • extracellular region • soluble fraction
Biological process	• response to oxidative stress • glutathione metabolic process • protein homotetramerization • response to lipid hydroperoxide • hydrogen peroxide catabolic process • oxidation reduction
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
150.38 – 150.39 Mb

Chr 11:
54.72 – 54.72 Mb

PubMed search

[1]

[2]

Glutathione peroxidase 3 (GPx-3), also known as plasma glutathione peroxidase (GPx-P) or extracellular glutathione peroxidase is an enzyme that in humans is encoded by the GPX3 gene.^[1]^[2]^[3]

GPx-3belongs to the glutathione peroxidase family, which functions in the detoxification of hydrogen peroxide. It contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon, which normally signals translation termination. The 3' UTR of Sec-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal.^[1]

References

^ ^a ^b "Entrez Gene: glutathione peroxidase 3 (plasma)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2878.
^ Takahashi K, Avissar N, Whitin J, Cohen H (August 1987). "Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme". Arch. Biochem. Biophys. 256 (2): 677–86. doi:10.1016/0003-9861(87)90624-2. PMID 3619451.
^ Chu FF (1994). "The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to chromosomes 14, 5, and 19, respectively". Cytogenet. Cell Genet. 66 (2): 96–8. doi:10.1159/000133675. PMID 8287691.

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Lin JC, Kuo WR, Chiang FY, et al. (2009). "Glutathione peroxidase 3 gene polymorphisms and risk of differentiated thyroid cancer.". Surgery 145 (5): 508–13. doi:10.1016/j.surg.2008.12.008. PMID 19375609.
Holtzman JL (2002). "The role of low levels of the serum glutathione-dependent peroxidase and glutathione and high levels of serum homocysteine in the development of cardiovascular disease.". Clin. Lab. 48 (3-4): 129–30. PMID 11934214.
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Mistry HD, Kurlak LO, Williams PJ, et al. (2010). "Differential expression and distribution of placental glutathione peroxidases 1, 3 and 4 in normal and preeclamptic pregnancy.". Placenta 31 (5): 401–8. doi:10.1016/j.placenta.2010.02.011. PMID 20303587.
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Iida R, Tsubota E, Yuasa I, et al. (2009). "Simultaneous genotyping of 11 non-synonymous SNPs in the 4 glutathione peroxidase genes using the multiplex single base extension method.". Clin. Chim. Acta 402 (1-2): 79–82. doi:10.1016/j.cca.2008.12.027. PMID 19161995.
Talmud PJ, Drenos F, Shah S, et al. (2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.". Am. J. Hum. Genet. 85 (5): 628–42. doi:10.1016/j.ajhg.2009.10.014. PMC 2775832. PMID 19913121. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2775832.
Wang JY, Yang IP, Wu DC, et al. (2010). "Functional glutathione peroxidase 3 polymorphisms associated with increased risk of Taiwanese patients with gastric cancer.". Clin. Chim. Acta 411 (19-20): 1432–6. doi:10.1016/j.cca.2010.05.026. PMID 20576521.
Westphal K, Stangl V, Fähling M, et al. (2009). "Human-specific induction of glutathione peroxidase-3 by proteasome inhibition in cardiovascular cells.". Free Radic. Biol. Med. 47 (11): 1652–60. doi:10.1016/j.freeradbiomed.2009.09.017. PMID 19766714.
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Saga Y, Ohwada M, Suzuki M, et al. (2008). "Glutathione peroxidase 3 is a candidate mechanism of anticancer drug resistance of ovarian clear cell adenocarcinoma.". Oncol. Rep. 20 (6): 1299–303. PMID 19020706.
Zhang X, Yang JJ, Kim YS, et al. (2010). "An 8-gene signature, including methylated and down-regulated glutathione peroxidase 3, of gastric cancer.". Int. J. Oncol. 36 (2): 405–14. PMID 20043075.
Chung SS, Kim M, Youn BS, et al. (2009). "Glutathione peroxidase 3 mediates the antioxidant effect of peroxisome proliferator-activated receptor gamma in human skeletal muscle cells.". Mol. Cell. Biol. 29 (1): 20–30. doi:10.1128/MCB.00544-08. PMID 18936159.
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Oxidoreductases: peroxidases (EC 1.11)

1.11.1.1-14	Catalase · Cytochrome c peroxidase · Eosinophil peroxidase · Glutathione peroxidase (GPX 1, 2, 3, 4, 5, 6, 7, 8) · Horseradish peroxidase · Lactoperoxidase · Myeloperoxidase · Thyroid peroxidase · Deiodinase (Iodothyronine deiodinase, Iodotyrosine deiodinase)

1.11.1.15 (peroxiredoxin)	1 · 2 · 3 · 4 · 5 · 6

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

GPX3

References

Further reading