Has chymotrypsin-like activity. Hydrolyzes the amide bonds of synthetic substrates having Tyr and Phe residues at the P1 position. Preferentially hydrolyzes the 'Tyr-4-|-Ile-5' bond of angiotensin I and the 'Phe-20-|-Ala-21' bond of amyloid beta-protein, and is less active towards the 'Phe-8-|-His-9' bond of angiotensin I and the 'Phe-4-|-Ala-5' and 'Tyr-10-|-Glu-11' bonds of amyloid beta-protein. Involved in thrombin regulation and fibronectin processing. Completely inhibited by serine protease inhibitors such as chymostatin, diisopropylfluorophosphate and phenylmethylsulfonyl fluoride, but not by p-tosyl-L-phenylalanine chloromethyl ketone, p-tosyl-L-lysine chloromethyl ketone, pepstatin, E-64, EDTA or o-phenanthroline. Also inhibited by lima bean trypsin inhibitor, soy bean trypsin inhibitor and human plasma alpha1-antichymotrypsin. Optimum pH is 9 at high salt concentrations. Monomer. Submucosal mast cells. In femoral muscle, detected in myocytes but not in mast cells. Mice display an impaired ability to inactivate thrombin or degrade fibronectin in peritoneal cells. Belongs to the peptidase S1 family. Granzyme subfamily.