A tripeptide motif (VGE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding. The cysteine-rich domain encodes putative cell-fusion peptides, which could be involved in sperm-egg fusion. 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.
Has no obvious cleavage site for furin endopeptidase, suggesting that the proteolytic processing is regulated.