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Mox1 and the glycoprotein gp91-phox are largely related proteins that are essential components of the NADPH oxidase. The superoxide-generating NADPH oxidase complex expresses in phagocytes, neuroepithelial bodies, vascular smooth muscle cells, and endothelial cells. It includes a membrane bound flavocytochrome containing two subunits, gp91-phox and p22-phox, and the cytosolic proteins p47-phox and p67-phox. The p22- and gp91-phox subunits also function as surface O2 sensors that initiate cellular signaling in response to hypoxic conditions. Mox1 and gp91 contain identical C-terminal sequence identity, yet possess distinct expression patterns. gp91-phox expresses in eosinophils, neutrophils, monocytes, and B-lymphocytes, whereas Mox1 is predominantly detected in the colon, with low expression in the uterus and prostate.
AMCBX2; C88302; Cgd; CGD91-phox; Cybb; Cyd; cytochrome b(558) subunit beta; cytochrome b-245 beta chain; cytochrome b-245 beta polypeptide; cytochrome b-245 heavy chain; cytochrome b-245, beta polypeptide; cytochrome b558 subunit beta; endothelial type gp91-phox; GP91 PHOX; GP911; GP91-1; GP91PHOX; gp91-phox; Heme-binding membrane glycoprotein gp91phox; IMD34; NADPH oxidase 2; neutrophil cytochrome b 91 kDa polypeptide; Nox2; p22 phagocyte B-cytochrome; p91PHOX; p91-PHOX; superoxide-generating NADPH oxidase heavy chain subunit
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