NOX3

NOX3

Identifiers

NOX3, GP91-3, MOX-2, NADPH oxidase 3

External IDs

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

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6q25.3	Start	155,395,368 bp^[1]
Band	6q25.3	End	155,455,839 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17 A1\|17 2.05 cM	Start	3,685,515 bp^[2]
Band	17 A1\|17 2.05 cM	End	3,746,536 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

hippocampus proper

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

NADPH oxidase 3 is an enzyme that in humans is encoded by the NOX3 gene.^[5]^[6]^[7]

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]^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000074771 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000023802 – 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.
^ Herb M (February 2024). "NADPH oxidase 3: Beyond the innear ear". Antioxidants. 13 (2): 219. doi:10.3390/antiox13020219. PMC 10886416. PMID 38397817.
^ 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".

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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This page was last edited on 6 April 2024, at 22:24

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Function

References

Further reading