ID:NOX1_HUMAN DESCRIPTION: RecName: Full=NADPH oxidase 1; Short=NOX-1; EC=1.-.-.-; AltName: Full=Mitogenic oxidase 1; Short=MOX-1; AltName: Full=NADH/NADPH mitogenic oxidase subunit P65-MOX; AltName: Full=NOH-1; FUNCTION: NOH-1S is a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues. It participates in the regulation of cellular pH and is blocked by zinc. NOH-1L is a pyridine nucleotide-dependent oxidoreductase that generates superoxide and might conduct H(+) ions as part of its electron transport mechanism, whereas NOH-1S does not contain an electron transport chain. COFACTOR: NADP (Potential). COFACTOR: FAD (Potential). ENZYME REGULATION: The oxidase activity is potentiated by NOXA1 and NOXO1. SUBUNIT: NOX1, NOXA1, NOXO1, RAC1 and CYBA forms a functional multimeric complex supporting ROS production. Interacts with NOXA1 and NOXO1. SUBCELLULAR LOCATION: Cell projection, invadopodium membrane; Multi-pass membrane protein. TISSUE SPECIFICITY: NOH-1L is detected in colon, uterus, prostate, and colon carcinoma, but not in peripheral blood leukocytes. NOH- 1S is detected only in colon and colon carcinoma cells. SIMILARITY: Contains 1 FAD-binding FR-type domain. SIMILARITY: Contains 1 ferric oxidoreductase domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9Y5S8
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.