Figure 2.
Structure of typical preproinsulin-like peptides (A) and sequence alignment of insulin-like peptide from Tribolium castaneum, Apis mellifera, Anopheles gambiae, Drosophila melanogaster, and one Bombyx mori Bombyxin (BBXA1, P33718) (B–D). Conserved cysteines are marked by “C” on the top of putative A- and B-chains (double lines, =) with canonical dibasic cleavage sites as vertical bars (|) and unknown cleavage sites as question marks (?). Tribolium and Apis sequences are from their genome database, Drosophila genes are from FlyBase, and Anopheles sequences are from Riehle et al. (2002).
