Controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Endopeptidase of broad specificity. Binds 1 zinc ion per subunit. Expressed maternally throughout the embryo and then becomes restricted to a pan-neural expression pattern. 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. The propeptide keeps the metalloprotease in a latent form via a cysteine switch mechanism. This mechanism may be mediated by a highly conserved cysteine (Cys-172) in the propeptide, which interacts and neutralizes the zinc-coordinating HEXGHXXGXXHD catalytic core of the metalloprotease domain. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. The precursor is cleaved by furin and PCSK7.