Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (PubMed:7579169). 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. Specific to vegetative organs, especially in senescent tissues. Expressed in developing seeds, rosette leaves, cauline leaves and stems. Not expressed in the siliques. Also present at the branching points of the roots and in vascular tissues. By senescence, wounding, 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.