Figure 7
From: Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes
Identification of highly conserved residues of p22 phox. (A) Schematic domains structures of p22phox are shown; TM1 and TM2 represent the predicted 1st and 2nd transmembrane region; PRR, proline-rich region; basic, a lysine- and arginine-rich conserved domain. Indicated above the schematic structure are putative key amino acid residues that are conserved in p22phox orthologs, and the residue numbers correspond to those of human p22phox. Detailed alignment of the polybasic region (B) and the PRR (C) are shown. Letters in solid boxes indicate the residues that have been proven by mutational analyses to be important for binding to p47phox and/or activation of human Nox2 [53, 75, 127, 128]. (D) Molecular taxonomy was generated based on the alignment of amino acid sequences of full-length p22phox. Species name abbreviations are given in Figure 3.