ADAMTS12

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.

The C-terminal four TSP1-like repeats are necessary and sufficient for binding COMP.

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.

Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties.

The precursor is cleaved by a furin endopeptidase.

Subjected to an intracellular maturation process yielding a 120 kDa N-terminal fragment containing the metalloproteinase, disintegrin, one TSP type-1 and the Cys-rich domains and a 83 kDa C-terminal fragment containing the spacer 2 and four TSP type-1 domains.

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).

Expressed in skeletal muscle and fat.

• Secreted
• Extracellular space
• Extracellular matrix

UNQ1918/PRO4389, ADAMTS12, A disintegrin and metalloproteinase with thrombospondin motifs 12, ADAM-TS 12, ADAM-TS12, ADAMTS-12

• entrezGene:81792
• omim:606184
• swissprot:P58397

Proteins

Oncology

177676Da