Figure 5

Figure 5

Gelatinase A orthologues have highly conserved phosphorylation sites. Putative serine (solid lines), threonine (dashed lines), and tyrosine (dotted lines) phosphorylation sites conserved in 100% (black), 99% (dark grey), or 97% (light grey) of gelatinase A orthologues are shown with respect to a structural schematic of the gelatinase A protein, illustrating the signal sequence (1–29 (orange)), propeptide (30–107 (grey)), catalytic domain (118–446 (green)) with fibronectin-like repeats (light green), and hemopexin-like domain (463–657 (purple)). Cysteines are indicated with yellow spots, connected by horizontal lines if they are predicted to participate in intramolecular disulfide bonds. Conserved residues that have been empirically demonstrated to be phosphorylated in vivo in the human protein are indicated with asterisks.