NOX3

From Wikipedia, the free encyclopedia

NADPH oxidase 3

Identifiers

NOX3; GP91-3

External IDs

OMIM: 607105 MGI: 2681162 HomoloGene: 49435

Gene ontology
Molecular Function:	• iron ion binding • oxidoreductase activity • FAD binding
Cellular Component:	• membrane • integral to membrane
Biological Process:	• thermoregulation • electron transport • response to gravity

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_015718 (mRNA)
NP_056533 (protein)

NM_198958 (mRNA)
NP_945196 (protein)

Location

Chr 6: 155.76 - 155.82 Mb

Chr 17: 3.59 - 3.65 Mb

Pubmed search

[1]

[2]

NADPH oxidase 3, also known as NOX3, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: NOX3 NADPH oxidase 3.

[edit] Further reading

Lachgar A, Sojic N, Arbault S, 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. 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. PMID 10974555.
Cheng G, Cao Z, Xu X, et al. (2001). "Homologs of gp91phox: cloning and tissue expression of Nox3, Nox4, and Nox5.". Gene 269 (1-2): 131–40. PMID 11376945.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
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 (2005). "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. PMID 15509740.
Ueno N, Takeya R, Miyano K, et al. (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. 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, et al. (2007). "Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3.". Biochem. J. 403 (1): 97–108. doi:10.1042/BJ20060819. PMID 17140397.
Chen G, Adeyemo AA, Zhou J, 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.