Bone morphogenetic protein 1 (BMP-1), also known as procollagen C-proteinase (PCP), is a zinc protease of the astacin family. BMP-1/PCP plays a key role in formation of extracellular matrix (ECM) by converting precursor proteins into their mature and functional forms. The precursor proteins identified as substrates for BMP-1/PCP include collagens, biglycan, laminin 5, dentin matrix protein-1, and lysyl oxidase. There are six alternatively spliced forms known to be derived from the BMP-1 gene, and isoform 1 consisting of residues 1 to 730 was expressed. The secreted and purified protein does not contain the signal peptide (amino acid residues 1?22) and pro domain (residues 23?120), but contain protease (residues 121?321), CUB I (residues 322?434), CUB II (residues 435?546), EGF-like (residues 547?588) and CUB III (residues 591?703) domains. The pro domain is apparently cleaved by a furin-like proprotein convertase. The purified BMP-1/PCP is an active protease and its peptidase activity can be determined as described above. The purified BMP-1/PCP is predicted to possess procollagen C-proteinase activity because it contains the minimal domain structure required.

BMP-1; BMP1; Bone morphogenetic protein 1; Mammalian tolloid protein; mTld; OI13; PCOLC; PCP; PCP2; procollagen C-endopeptidase; Procollagen C-proteinase; procollagen C-proteinase 3; TLD