Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite. May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion. Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides. Activation may be calcium-dependent. Inhibited by the non-covalent interaction with the cleaved propeptide. In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:10339607). Immediately after schizont rupture, secreted from the micronemes to the merozoite surface where it redistributes in an actin-dependent manner to accumulate at the posterior end of newly released merozoites (By similarity). Expressed during the parasite blood stage, specifically in schizonts and merozoites (at protein level). The propeptide domain acts as an intramolecular chaperone for the folding of the catalytic domain (By similarity). Also acts as an inhibitor of the catalytic domain thereby regulating SUB2 activity during secretion (By similarity). The transmembrane domain is required for SUB2 progression through the secretory pathway. The cytoplasmic domain is required for the correct redistribution at the merozoite surface and posterior capping but is dispensable for its progression through the secretory pathway. Proteolytically cleaved at the N-terminus to generate a 74kDa intermediate which is further processed into a 72kDa form (PubMed:10339607). The first maturation cleavage is autocatalytic, occurs in the ER and is necessary for the subsequent SUB2 trafficking to the microneme (By similarity). The second cleavage may be mediated by PMX/plasmepsin X (By similarity). Belongs to the peptidase S8 family.