Endothelin-converting enzymes, such as ECE2 are type II metalloproteases that generate functionally pleiotropic members of the endothelin vasoactive peptide family.The deduced protein contains 765 amino acids. ECE2 had an apparent molecular mass of 81 kD by SDS-PAGE.The ECE2A variant contains exons 1A and 2A and encodes a deduced 787-amino acid protein with a calculated molecular mass of 89.1 kD. ECE2A has an intracytoplasmic tail, a transmembrane domain, and a large extracellular catalytic domain with a zinc-binding motif conserved in Zn(2+) metalloproteases. It has 9 N-glycosylation sites. The ECE2B variant contains exons 1B and 2B and encodes a deduced 682-amino acid protein with a calculated molecular mass of 86.4 kD. ECE2B differs from ECE2A only in the intracytoplasmic tail.