ADAMTS7
From Wikipedia, the free encyclopedia
A disintegrin and metalloproteinase with thrombospondin motifs 7 (ADAMTS7) is an enzyme that in humans is encoded by the ADAMTS7 gene on chromosome 15.[1] It is ubiquitously expressed in many tissues and cell types.[2] This enzyme catalyzes the degradation of cartilage oligomeric matrix protein (COMP)[3] and TIMP1.[4] ADAMTS7 has been associated with cancer and arthritis in multiple tissue types.[5][6] The ADAMTS7 gene also contains one of 27 SNPs associated with increased risk of coronary artery disease.[7]
Gene
The ADAMTS7 gene resides on chromosome 15 at the band 15q24.2 and contains 25 exons.[1]
Protein
This 1686-amino acid protein belongs to the ADAMTS family and is one of 19 members known in humans. As an ADAMTS protein, ADAMTS7 contains a shared proteinase domain and an ancillary domain. The proteinase domain can be further divided into a signal peptide, a prodomain, a metalloproteinase domain, and a disintegrin-like domain.[8] In particular, the metalloproteinase domain contains a cysteine-switch motif in its binding site for binding the catalytic zinc ion (Zn2+).[9] A pharmacophore model consisting of four hydrogen bond donor sites and three hydrogen bond acceptor sites was proposed for this domain. Unlike the proteinase domain, the ancillary domain varies by ADAMTS protein and includes any number of thrombospondin (TSP) type 1 motifs, one cysteine-rich and spacer domain, and other domains specific to certain ADAMTS proteins.[8] ADAMTS7 in particular possesses 8 TSP type 1 motifs which, together with its spacer domain, participate in the protein’s tight interaction with the extracellular matrix.[9]