NADPH oxidase 3 (NOX3) is a type of NADPH oxidase , a cell membrane oxidoreductase that forms a superoxide radical when an electron is transferred from NADP to oxygen . Opened in 2000, it is similar to NOX2 (56% amino acid sequence identity), as well as NOX1 .
| NADPH oxidase 3 | |
|---|---|
| Designations | |
| Characters | NOX3 ; GP91-3 |
| Entrez gene | 50508 |
| Hgnc | 7890 |
| Omim | 607105 |
| Refseq | NM_015718 |
| Uniprot | Q9HBY0 |
| Other data | |
| Cipher cf | 1.6.3.1 |
| Locus | 6th , 6q25.3 |
Structure
NOX3 is a protein of 568 amino acids with a molecular weight of 64.9 kDa. It has significant similarity with NOX2 in amino acid sequence (56% identity), transmembrane domain structure, extracellular fragment length, NADP and FAD binding sites, as well as the position of histidines in the heme-binding site. Cellular localization is unknown.
Enzymatic complex
Like all other NADPH oxidases, NOX3 requires the formation of a protein complex for the manifestation of oxidase activity. It is known that the activity of NOX3 depends on interaction with another p22phox membrane protein and the cytosolic protein NOXO1 . Other cytosolic proteins involved in the activation of NOX2 , p47phox and p67phox are able to activate NOX3 in model cells, but their physiological role in the body is not clear. Alternative splicing for NOX3 is not shown.
Tissue localization and function
The highest level of NOX3 expression was found in the inner ear , in particular in the sensory epithelium of the cochlear and vestibular apparatus and in the spiral ganglion. It plays a role in the biogenesis of otoliths . In addition, the gene is expressed in the brain and fetal spleen and kidneys . A mutation in the NOX3 gene in a mouse leads to a head tilt syndrome.
Bibliography
- van der Vliet A. NADPH oxidases in lung biology and pathology: host defense enzymes, and more (English) // Free Radical Biology and Medicine : journal. - 2008 .-- March ( vol. 44 , no. 6 ). - P. 938-955 . - DOI : 10.1016 / j.freeradbiomed.2007.11.01.01 . - PMID 18164271 .
- Bedard K., Krause KH The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology (Eng.) // Physiological Reviews : journal. - 2007 .-- January ( vol. 87 , no. 1 ). - P. 245-313 . - DOI : 10.1152 / physrev.00044.2005 . - PMID 17237347 .