NOX3

NOX3
Identifiers
Aliases	NOX3, GP91-3, MOX-2, NADPH oxidase 3
External IDs	MGI: 2681162 HomoloGene: 49435 GeneCards: NOX3
Gene ontology Molecular function • oxidoreductase activity • superoxide-generating NADPH oxidase activity Cellular component • cytoplasm • integral component of membrane • plasma membrane • NADPH oxidase complex • extracellular exosome • membrane Biological process • response to gravity • temperature homeostasis • detection of gravity • otolith development • oxidation-reduction process • superoxide anion generation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	50508	224480
Ensembl	ENSG00000074771	ENSMUSG00000023802
UniProt	Q9HBY0	Q672J9
RefSeq (mRNA)	NM_015718	NM_198958
RefSeq (protein)	NP_056533.1	NP_945196.2
Location (UCSC)	Chr 6: 155.4 – 155.46 Mb	Chr 17: 3.64 – 3.7 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene.^[3][4]

Function

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]^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "Entrez Gene: NOX3 NADPH oxidase 3".

Further reading

• Lachgar A, Sojic N, Arbault S, Bruce D, Sarasin A, Amatore C, Bizzini B, Zagury D, Vuillaume M (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.
• 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.
• 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 (2004). "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.
• Ueno N, Takeya R, Miyano K, Kikuchi H, Sumimoto H (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.
• 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, Dinauer MC, Allen LA, Nauseef WM (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.
• Chen G, Adeyemo AA, Zhou J, Chen Y, Doumatey A, Lashley K, Huang H, Amoah A, Agyenim-Boateng K, Eghan BA, Okafor G, Acheampong J, Oli J, Fasanmade O, Johnson T, Rotimi C (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.