The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme (By similarity).
Metalloprotease that may play a role in the degradation of COMP.
Glycosylated (By similarity). 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. N- and C-glycosylations can also facilitate secretion. O-glycosylated proteoglycan. Contains chondroitin sulfate (By similarity).
May be cleaved by a furin endopeptidase. The precursor is sequentially processed (By similarity).
Detected in liver, ovary, kidney, testicle, lung and embryo.
A disintegrin and metalloproteinase with thrombospondin motifs 7, ADAM-TS 7, ADAM-TS7, ADAMTS-7, COMPase, Adamts7
Proteins
Oncology
We found 1 product in 1 category