NOX3

NOX3
Identifiers
Aliases	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)
End	155,455,839 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	3,746,536 bp
RNA expression pattern
	Top expressed in
	hippocampus proper;
	Top expressed in
	spermatid; ; testicle;
	More reference expression data
	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
	50508
	224480
	ENSG00000074771
	ENSMUSG00000023802
	Q9HBY0
	Q672J9
	NM_015718
	NM_198958
	NP_056533
	NP_945196
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 07, 2024

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]

Related Research Articles

Respiratory burst is the rapid release of the reactive oxygen species (ROS), superoxide anion and hydrogen peroxide, from different cell types.

NADPH oxidase is a membrane-bound enzyme complex that faces the extracellular space. It can be found in the plasma membrane as well as in the membranes of phagosomes used by neutrophil white blood cells to engulf microorganisms. Human isoforms of the catalytic component of the complex include NOX1, NOX2, NOX3, NOX4, NOX5, DUOX1, and DUOX2.

NADPH oxidase 2 (Nox2), also known as cytochrome b(558) subunit beta or Cytochrome b-245 heavy chain, is a protein that in humans is encoded by the NOX2 gene. The protein is a superoxide generating enzyme which forms reactive oxygen species (ROS).

Tartrate-resistant acid phosphatase, also called acid phosphatase 5, tartrate resistant (ACP5), is a glycosylated monomeric metalloprotein enzyme expressed in mammals. It has a molecular weight of approximately 35kDa, a basic isoelectric point (7.6–9.5), and optimal activity in acidic conditions. TRAP is synthesized as latent proenzyme and activated by proteolytic cleavage and reduction. It is differentiated from other mammalian acid phosphatases by its resistance to inhibition by tartrate and by its molecular weight.

Neutrophil cytosol factor 1, also known as p47phox, is a protein that in humans is encoded by the NCF1 gene.

NADPH oxidase 1 is an enzyme that in humans is encoded by the NOX1 gene.

NADPH oxidase 4 is an enzyme that in humans is encoded by the NOX4 gene, and is a member of the NOX family of NADPH oxidases.

Cytochrome b-245 light chain is a protein that in humans is encoded by the CYBA gene involved in superoxide production and phagocytosis.

Rac2 is a small signaling G protein, and is a member of the Rac subfamily of the family Rho family of GTPases. It is encoded by the gene RAC2.

Neutrophil cytosol factor 4 is a protein that in humans is encoded by the NCF4 gene.

General transcription factor IIH subunit 4 is a protein that in humans is encoded by the GTF2H4 gene.

HIV Tat-specific factor 1 is a protein that in humans is encoded by the HTATSF1 gene.

Dual oxidase 2, also known as DUOX2 or ThOX2, is an enzyme that in humans is encoded by the DUOX2 gene. Dual oxidase is an enzyme that was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. The protein location is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

Dual oxidase 1, also known as DUOX1 or ThOX1, is an enzyme which in humans is encoded by the DUOX1 gene. DUOX1 was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. Human DUOX protein localization is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

Nuclear transcription factor Y subunit gamma is a protein that in humans is encoded by the NFYC gene.

Glutathione peroxidase 2 is an enzyme that in humans is encoded by the GPX2 gene.

NADPH oxidase, EF-hand calcium binding domain 5, also known as NOX5, is a protein which in humans is encoded by the NOX5 gene.

NADPH oxidase organizer 1 is an enzyme that in humans is encoded by the NOXO1 gene.

NADPH oxidase activator 1 is an enzyme that in humans is encoded by the NOXA1 gene.

NADPH-dependent diflavin oxidoreductase 1 is an enzyme that in humans is encoded by the NDOR1 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000074771 - Ensembl, May 2017
1 2 3 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.
1 2 "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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000074771 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid11376945-6] 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.

[entrez-7] 1 2 "Entrez Gene: NOX3 NADPH oxidase 3".

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NOX3

Contents

Function

Related Research Articles

References

Further reading