Alignment of κ-casein between human, mouse, and cow. The sequences of casoxin peptides A, B, and C are in the pink colored boxes. Cleavage sites are to the right of the red residues, while green residues are the corresponding residues that are not cleavable by the same enzyme in human and mouse. Casoxin-A and C are cleaved by a pepsin-trypsin digest for the former, and a trypsin digest for the later . The peptide Casoplatelin  that inhibits ADP-induced platelet aggregation and fibrinogen binding is also represented on the figure together with the chymosin/rennin cleavage site between the F and M residues in red (while the same positions are in green in human and mouse). Horizontal lines represent gaps. Stars indicate sites that were predicted to be under positive selection (see results). Orange residues have been shown in the literature to undergo phosphorylation. Blue residues have been shown in the literature to undergo glycosylation. One potential phosphorylation site indicated in lavender in mouse.