Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin. Contrary to other SAPs, SAP7 is insensitive to pepstatin A inhibition, which is due restriction of the accessibility of pepstatin A to the active site by Met-242 and Thr-467. Optimum pH is 6.5. Expression is regulated by SSN6 and induced during host infection. N-glycosylated. O-glycosylated. Belongs to the peptidase A1 family.