NOX3

NADPH oxidase 3

Identifiers

NOX3 ; GP91-3; MOX-2

External IDs

OMIM: 607105 MGI: 2681162 HomoloGene: 49435 ChEMBL: 1741216 GeneCards: NOX3 Gene

Gene ontology
Molecular function	• superoxide-generating NADPH oxidase activity
Cellular component	• cytoplasm • NADPH oxidase complex • extracellular vesicular exosome
Biological process	• temperature homeostasis • detection of gravity • superoxide anion generation • otolith development • oxidation-reduction process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000074771

ENSMUSG00000023802

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
155.72 – 155.78 Mb

Chr 17:
3.64 – 3.7 Mb

PubMed search

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

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]^[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. CS1 maint: Date and year (link)
↑ 2.0 2.1 "Entrez Gene: NOX3 NADPH oxidase 3".

Further reading

Lachgar A, Sojic N, Arbault S, Bruce D, Sarasin A, Amatore C 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.
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 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.