Fig. 2

Schematic representation of NOX4/NOX4-art and p22-phox proteins with partial regions of the alignment of important loops and segments. The six hydrophobic helixes of the ferric reductase domain are depicted in pink with the four histidine residues. The dehydrogenase domain is colored in green and yellow (FAD1-2 and NADPH1-4 respectively). The red asterisk in NADPH1 shows where the VXGPFG-motif is located. The C-terminal region, important for the interaction with p22-phox, is dark orange. Segments and loops are black with loops identified by capital letters. The protein p22-phox with its two transmembrane helixes and proline-rich region (PRR) is illustrated in blue. Partial alignments of important regions are highlighted in blue for p22-phox (where no arthropod species are present) and grey for NOX4/NOX4-art. Within the alignments important residues are colored in red. Hs - Homo sapiens, Xt - Xenopus tropicalis, Ol - Oryzias latipes, Bf - Branchiostoma floridae, Lg - Lottia gigantea, Nv - Nematostella vectensis, Pt - Parasteatoda tepidariorum, Cs - Centruroides sculpturatus, Dp - Daphnia pulex, As - Argulus siamensis, Ca - Catajapyx aquilonaris, Ov – Okanagana villosa, Cc - Corydalus cornutus, Of - Osmylus fulvicephalus, Xx - Xanthostigma xanthostigma, Ag - Anopheles gambiae, Cq - Culex quinquefasciatus, Nd - Nemophora degeerella, Ms. - Manduca sexta, Bm - Bombyx mori, Ac - Aplysia californica, Aq - Amphimedon queenslandica, Bg - Biomphalaria glabrata, Cf - Canis familiaris, Cg - Crassostrea gigas, Ci - Ciona intestinalis, Ct - Capitella teleta, Hr - Helobdella robusta, Hv - Hydra vulgaris, Mb - Monosiga brevicollis, Sp - Strongylocentrotus purpuratus, Tr - Takifugu rubripes