A disintegrin and metalloproteinase with thrombospondin motifs 6
Domain
The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
Post-translational modifications
The precursor is cleaved by a furin endopeptidase.
Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Can also be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).
Tissue Specificity
Expressed at low levels in placenta and barely detectable in a number of other tissues.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
Alternative names
A disintegrin and metalloproteinase with thrombospondin motifs 6, ADAM-TS 6, ADAM-TS6, ADAMTS-6, ADAMTS6