NOX3

NADPH oxidase 3

Identifiers

NOX3; GP91-3; MOX-2

External IDs

OMIM: 607105 MGI: 2681162 HomoloGene: 49435 GeneCards: NOX3 Gene

Gene Ontology
Molecular function	• iron ion binding • electron carrier activity • superoxide-generating NADPH oxidase activity • oxidoreductase activity • flavin adenine dinucleotide binding
Cellular component	• cytoplasm • membrane • integral to membrane • NADPH oxidase complex
Biological process	• temperature homeostasis • detection of gravity • superoxide anion generation • otolith development
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
155.72 – 155.78 Mb

Chr 17:
3.64 – 3.7 Mb

PubMed search

[1]

[2]

NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene.^[1]^[2]

NADPH oxidases, such as NOX3, are plasma membrane-associated enzymes found in many cell types. They catalyze the production of superoxide by a 1-electron reduction of oxygen, using NADPH as the electron donor.[supplied by OMIM]^[2]

References

^ Cheng G, Cao Z, Xu X, van Meir EG, Lambeth JD (May 2001). "Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5". Gene 269 (1–2): 131–40. doi:10.1016/S0378-1119(01)00449-8. PMID 11376945.
^ ^a ^b "Entrez Gene: NOX3 NADPH oxidase 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50508.

Lachgar A, Sojic N, Arbault S, et al. (1999). "Amplification of the Inflammatory Cellular Redox State by Human Immunodeficiency Virus Type 1-Immunosuppressive Tat and gp160 Proteins". J. Virol. 73 (2): 1447–52. PMC 103969. PMID 9882350. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=103969.
Kikuchi H, Hikage M, Miyashita H, Fukumoto M (2000). "NADPH oxidase subunit, gp91(phox) homologue, preferentially expressed in human colon epithelial cells". Gene 254 (1–2): 237–43. doi:10.1016/S0378-1119(00)00258-4. PMID 10974555.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Cheng G, Ritsick D, Lambeth JD (2004). "Nox3 regulation by NOXO1, p47phox, and p67phox". J. Biol. Chem. 279 (33): 34250–5. doi:10.1074/jbc.M400660200. PMID 15181005.
Jana A, Pahan K (2005). "Human Immunodeficiency Virus Type 1 gp120 Induces Apoptosis in Human Primary Neurons through Redox-Regulated Activation of Neutral Sphingomyelinase". J. Neurosci. 24 (43): 9531–40. doi:10.1523/JNEUROSCI.3085-04.2004. PMC 1955476. PMID 15509740. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1955476.
Ueno N, Takeya R, Miyano K, et al. (2005). "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators". J. Biol. Chem. 280 (24): 23328–39. doi:10.1074/jbc.M414548200. PMID 15824103.
Ueyama T, Geiszt M, Leto TL (2006). "Involvement of Rac1 in Activation of Multicomponent Nox1- and Nox3-Based NADPH Oxidases". Mol. Cell. Biol. 26 (6): 2160–74. doi:10.1128/MCB.26.6.2160-2174.2006. PMC 1430270. PMID 16507994. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1430270.
Carnesecchi S, Carpentier JL, Foti M, Szanto I (2006). "Insulin-induced vascular endothelial growth factor expression is mediated by the NADPH oxidase NOX3". Exp. Cell Res. 312 (17): 3413–24. doi:10.1016/j.yexcr.2006.07.003. PMID 16949073.
Nakano Y, Banfi B, Jesaitis AJ, et al. (2007). "Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3". Biochem. J. 403 (1): 97–108. doi:10.1042/BJ20060819. PMC 1828898. PMID 17140397. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1828898.
Chen G, Adeyemo AA, Zhou J, et al. (2007). "A genome-wide search for linkage to renal function phenotypes in West Africans with type 2 diabetes". Am. J. Kidney Dis. 49 (3): 394–400. doi:10.1053/j.ajkd.2006.12.011. PMID 17336700.

NOX3

References

Further reading