A disintegrin and metalloproteinase with thrombospondin motifs 1
(ADAMTS-1) is known to cleave extracellular matrix in acutely inflamed tissues.
The ADAMs belong to a disintegrin-like and metalloproteinase-containing protein family that are
zinc-dependent metalloproteinases. These proteins share all or some of the following domain
structure: a signal peptide, a propeptide, a metalloproteinase, a disintegrin, a cysteine-rich, and an
epidermal growth factor (EGF)-like domains, a transmembrane region, and a cytoplasmic tail.
ADAMs are widely distributed in many organs. These proteins are capable of four
potential functions: proteolysis, adhesion, fusion, and intracellular signaling Stone et al 1999 .
NCBI Summary:
This gene encodes a disintegrin and metalloproteinase with thrombospondin (ADAMTS) motifs-13, which is a member of the ADAMTS protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene is the von Willebrand Factor (vWF)-cleaving protease, which is responsible for cleaving at the site of Tyr842-Met843 of the vWF molecule. A deficiency of this enzyme is associated with thrombotic thrombocytopenic purpura. Alternative splicing of this gene generates at least 4 transcript variants encoding different isoforms.
General function
Cell adhesion molecule, Enzyme
Comment
Levy et al. (2001) isolated a full-length cDNA encoding ADAMTS13. ADAMTS13
encodes a predicted 1,427-amino acid protein. The ADAMTS13 protein has a signal peptide followed by a short
propeptide domain ending in a potential propeptide convertase cleavage site at amino acids 71 to 74 (RQRR),
suggesting that proteolytic processing, either in the trans Golgi or the cell surface, is required for activation. The
protease domain that follows has a perfect match for the HEXGHXXGXXHD (where X is any amino acid) consensus
sequence of the extended catalytic site shared between snake venom metalloproteinases and the ADAM family
members. The catalytic domain is followed by a thrombospondin-1-like (TSP1) domain and spacer domains
characteristic of members of the ADAMTS family. An RGD sequence, present in only 1 other mature ADAMTS protein
(ADAMTS2; OMIM 604539), is located immediately C terminal to the first TSP1 domain of ADAMTS13. The C terminus of
ADAMTS13 contains 6 additional TSP1 repeats, followed by a segment homologous to the CUB domain of several
developmentally regulated proteins.
Cellular localization
Extracellular Matrix, Secreted
Comment
Ovarian function
Comment
Expression regulated by
Comment
Ovarian localization
Comment
Levy et al. (2001) found the expression of ADAMTS13 in the ovary based on RT-PCR.