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ADAMTS (a disintegrin and metalloproteinase domain with Thrombospondin type-1 modules) is a family of zinc-dependent proteases that are implicated in a variety of normal and pathological conditions, including arthritis and cancer (1-3). Embryogenesis, morphological growth changes, inflammation, tumor invasion and metastasis involve the breakdown and remodeling of the extracellular matrix. This degradation is due to the family of enzymes known as the matrix metalloproteinases (MMPs), which are related to ADAMTS subtypes. ADAMTS protein family members contain an amino-terminal propeptide domain, a metalloproteinase domain, a disintegrin-like domain and a carboxy-terminus that contains a varying number of thrombospondin type-1 (TSP-1) motifs (1-3). ADAMTS genes are primarily expressed in fetal tissues, including the lung, kidney and liver (1-3). The human ADAMTS10 gene maps to chromosome 19p13.3 (4). The human ADAMTS19 gene maps to chromosome 5q31 (1,5).
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Protein Aliases: a disintegrin and metalloproteinase; A disintegrin and metalloproteinase with thrombospondin motifs 10; a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 10; a disintegrin-like and metalloprotease with thrombospondin type 1 motif, 10; ADAM; ADAM metallopeptidase with thrombospondin type 1 motif, 10; ADAM-TS 10; ADAMs; metalloendopeptidases; zinc metalloendopeptidase
Gene Aliases: 9430006O18; ADAM-TS10; ADAMTS-10; ADAMTS10; AW045948; WMS; WMS1; Znmp
UniProt ID: (Human) Q9H324, (Mouse) P58459
Entrez Gene ID: (Human) 81794, (Mouse) 224697, (Rat) 314655
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