Laeverin is a 990 amino acid member of the peptidase M1 family and contains an HEXXHX18E gluzincin motif and an H(G)AMEN motif. Expressed specifically in placenta on embryo-derived extravillous trophoblasts (EVTs), laeverin localizes to the cell membrane and is a single-pass type II membrane protein. Laeverin binds zinc and functions as a bestatin-sensitive leucine aminopeptidase with a potential role in EVT function. This suggests that laeverin may be involved in human placentation, during which EVTs invade maternal decidua and spiral areteries. More specifically, laeverin may function by regulating the activities of key peptides at the embryo-maternal interface. Laeverin has a broad substrate specificity but exhibits a preference for Leu-4-methylcoumaryl-7-amide. In addition, laeverin can form a homodimer with intermolecular disulfide bond(s).