Metalloprotease which, together with cadherin cdh-3 and hemicentin him-4, plays a role in anchor cell (AC) invasion during postembryonic vulval development probably by promoting the degradation of the basement membrane separating the gonad from the vulva epithelium. Localizes to puncta on the cell surface that are often concentrated at the invasive basolateral membrane of the anchor cell. Expressed in the anchor cell (PubMed:11060231, PubMed:15960981). Expressed in the anchor cell throughout the L3 and the early L4 stage, but not in vulva precursor cells P6.p, P6.px, or P6.pxx (PubMed:11060231). Expression in P6.pxxx cells begins in late-L4 stage. During L4 lethargus, expressed in all four vulE cells, but not in vulF cells (PubMed:11060231). The expression in vulE cells persists in adulthood (PubMed:11060231). In males, expressed in the linker cell (LC) from the early L4 stage until LC death during the L4-to-adult molt (PubMed:19906858). The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. No defect in anchor cell invasion. In 7 percent of cdh-3 and zmp-1 double mutants and in 25 percent of cdh-3, him-4 and zmp-1 triple mutants, anchor cell invasion is delayed. Displays very low catalytic activity compared to zmp-2 towards synthetic substrate Mca-Pro-Leu-Gly-Leu-Gly-Leu-Dpa-Ala-Arg-NH2 in vitro. Belongs to the peptidase M10A family.