Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (PubMed:10417725). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds (PubMed:14688293). Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds. Localized in lytic vacuoles of wounded leaves. Specific to vegetative organs, especially in senescent tissues. Also expressed in seeds and root tips. By senescence, wounding, jasmonic acid (JA), ethylene and salicylic acid (SA). Auto-catalytic activation. No macroscopic phenotype, probably due to functional redundancy. 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. Belongs to the peptidase C13 family. Truncated N-terminus.