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NOX3
Identifiers
Aliases	NOX3, GP91-3, MOX-2, NADPH oxidase 3
External IDs	OMIM: 607105; MGI: 2681162; HomoloGene: 49435; GeneCards: NOX3; OMA:NOX3 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6q25.3 Start 155,395,368 bp End 155,455,839 bp
Gene location (Mouse) Chr. Chromosome 17 (mouse) Band 17 A1|17 2.05 cM Start 3,685,515 bp End 3,746,536 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Cortex of frontal lobe hippocampus proper right frontal lobe Top expressed in spermatid testicle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function oxidoreductase activity superoxide-generating NAD(P)H 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 superoxide anion generation defense response Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 50508 224480 Ensembl ENSG00000074771 ENSMUSG00000023802 UniProt Q9HBY0 Q672J9 RefSeq (mRNA) NM_015718 NM_198958 RefSeq (protein) NP_056533 NP_945196 Location (UCSC) Chr 6: 155.4 – 155.46 Mb Chr 17: 3.69 – 3.75 Mb PubMed search
Wikidata
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NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene.

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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000074771 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000023802 – 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.
5. Herb M (February 2024). "NADPH oxidase 3: Beyond the innear ear". Antioxidants. 13 (2): 219. doi:10.3390/antiox13020219. PMC 10886416. PMID 38397817.
6. 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.
7. ^ "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. doi:10.1128/JVI.73.2.1447-1452.1999. 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" (PDF). Mol. Cell. Biol. 26 (6): 2160–74. doi:10.1128/MCB.26.6.2160-2174.2006. PMC 1430270. PMID 16507994. Archived from the original (PDF) on 2020-10-09. Retrieved 2018-11-04.
• 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.

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