Additional file 2: Figure S1. of Evolutionary origin of type IV classical cadherins in arthropods

Characterization and subdivision of the amino acid sequences of DN-, Pt1-, and Pt2-cadherins. A. Alignment of the EC1-EC17 regions of DN-, Pt1-, and Pt2-cadherins (abbreviated as DN, P1 and P2, respectively). The “-“character indicates introduced gaps. Conserved hydrophobic residues (blue), Ca2+-binding motifs or residues (red), and XPXF motif sequences (green) are aligned, all of which represent structural features of EC domains as shown schematically at the top. Thick blue arrows denote the seven β-strands (βA to βG). Each red arrow indicates the inter-EC linker to which the Ca2+-binding motif or residue belongs. No residues are omitted from the alignment, except for three sections where 7–12 residues of the DN-cadherin sequences are placed outside the alignment (parentheses). The N-terminal sequence (Nt) preceding the EC1 domain is also shown for each cadherin. B. Alignment of the NC and subsequent domains of the DN-, Pt1-, and Pt2-cadherins. In both A and B, conserved cysteine residues are highlighted in pink, and the residues bordering the start and end of the introns are highlighted with yellow and green. (PDF 362 kb)