Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (By similarity). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds (PubMed:12417707, PubMed:14688293). Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds. Seed specific. Also expressed in the flowers and buds. Auto-catalytic activation. No macroscopic phenotype, probably due to functional redundancy (PubMed:12417707, PubMed:14688293). Slight differences in polypeptide accumulation in seeds with an increased amount of propolypeptide forms of legumin-type globulins (PubMed:12417707). In plants lacking all vacuolar-processing enzyme isozymes (e.g. alpha, beta, gamma and delta) shift of storage protein accumulation from normally processed polypeptides to a finite number of prominent alternatively processed polypeptides cleaved at sites other than the conserved Asn residues targeted by VPE (PubMed:14688293). Belongs to the peptidase C13 family.