Glutathione peroxidase 6

GPX6
Identifiers
Aliases	GPX6, GPX5p, GPXP3, GPx-6, GSHPx-6, dJ1186N24, dJ1186N24.1, glutathione peroxidase 6
External IDs	OMIM: 607913; MGI: 1922762; HomoloGene: 130008; GeneCards: GPX6; OMA:GPX6 - orthologs
Gene location (Human)
Chr.	Chromosome 6 (human)
End	28,528,215 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	21,503,794 bp
RNA expression pattern
	Top expressed in
	testicle; ; gonad; ; olfactory zone of nasal mucosa; ; right testis; ; left testis; ; islet of Langerhans; ; lung; ; colon; ; wall of intestine; ; muscle layer of sigmoid colon;
	Top expressed in
	olfactory epithelium; ; spermatid; ; right kidney; ; zygote; ; outer renal medulla; ; seminiferous tubule; ; secondary oocyte; ; human kidney; ; primary oocyte; ; urethra;
	More reference expression data
	n/a
Gene ontology
Molecular function	oxidoreductase activity; glutathione peroxidase activity; peroxidase activity;
Cellular component	extracellular region;
Biological process	cellular oxidant detoxification; response to oxidative stress;
	Sources:Amigo / QuickGO
Orthologs
	257202
	75512
	ENSG00000281185; ENSG00000198704
	ENSMUSG00000004341
	P59796
	Q91WR8
	NM_182701
	NM_145451
	NP_874360
	NP_663426
	Wikidata
View/Edit Human	View/Edit Mouse

Glutathione peroxidase 6 (GPx-6) is an enzyme that in humans is encoded by the GPX6 gene.^[5]^[6]

This gene product belongs 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. Expression of this gene is restricted to embryos and adult olfactory epithelium.^[5]

References

^ ^a ^b ^c ENSG00000198704 GRCh38: Ensembl release 89: ENSG00000281185, ENSG00000198704 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000004341 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: glutathione peroxidase 6 (olfactory)".
^ Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigó R, Gladyshev VN (May 2003). "Characterization of mammalian selenoproteomes". Science. 300 (5624): 1439–43. Bibcode:2003Sci...300.1439K. doi:10.1126/science.1083516. PMID 12775843. S2CID 10363908.

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.
Richard MJ, Guiraud P, Didier C, et al. (2001). "Human immunodeficiency virus type 1 Tat protein impairs selenoglutathione peroxidase expression and activity by a mechanism independent of cellular selenium uptake: consequences on cellular resistance to UV-A radiation". Arch. Biochem. Biophys. 386 (2): 213–20. doi:10.1006/abbi.2000.2197. PMID 11368344.
Opalenik SR, Ding Q, Mallery SR, Thompson JA (1998). "Glutathione depletion associated with the HIV-1 TAT protein mediates the extracellular appearance of acidic fibroblast growth factor". Arch. Biochem. Biophys. 351 (1): 17–26. doi:10.1006/abbi.1997.0566. PMID 9501919.
Choi J, Liu RM, Kundu RK, et al. (2000). "Molecular mechanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice". J. Biol. Chem. 275 (5): 3693–8. doi:10.1074/jbc.275.5.3693. PMID 10652368.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
Price TO, Ercal N, Nakaoke R, Banks WA (2005). "HIV-1 viral proteins gp120 and Tat induce oxidative stress in brain endothelial cells". Brain Res. 1045 (1–2): 57–63. doi:10.1016/j.brainres.2005.03.031. PMID 15910762. S2CID 7362454.
Bailey SD, Xie C, Do R, et al. (2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study". Diabetes Care. 33 (10): 2250–3. doi:10.2337/dc10-0452. PMC 2945168. PMID 20628086.
Moyer AM, Sun Z, Batzler AJ, et al. (2010). "Glutathione pathway genetic polymorphisms and lung cancer survival after platinum-based chemotherapy". Cancer Epidemiol. Biomarkers Prev. 19 (3): 811–21. doi:10.1158/1055-9965.EPI-09-0871. PMC 2837367. PMID 20200426.

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] ENSG00000198704 GRCh38: Ensembl release 89: ENSG00000281185, ENSG00000198704 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000004341 – 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.

[entrez-5] "Entrez Gene: glutathione peroxidase 6 (olfactory)".

[pmid12775843-6] Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigó R, Gladyshev VN (May 2003). "Characterization of mammalian selenoproteomes". Science. 300 (5624): 1439–43. Bibcode:2003Sci...300.1439K. doi:10.1126/science.1083516. PMID 12775843. S2CID 10363908.

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v t e Oxidoreductases: peroxidases (EC 1.11)
1.11.1.1-14	NADH peroxidase NADPH peroxidase Fatty-acid peroxidase 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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Glutathione peroxidase 6

References

Further reading