A disintegrin & metalloproteinase with thrombospondin type 1 motif 12; ADAMTS-12; ADAM-TS 12; ADAM-TS12; (ADAMTS12)
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Function
- interaction with the extracellular matrix
- precursor is cleaved by a furin endopeptidase
- subjected to an intracellular maturation process yielding a 120 kD N-terminal fragment containing the metalloproteinase, disintegrin, one TSP type-1 domain & the Cys-rich domains & a 83 kD C-terminal fragment containing the spacer 2 & four TSP type-1 domains
Cofactor: binds 1 Zn+2 per subunit (putative)
Structure
- spacer domain & TSP type-1 domains are important for a tight interaction with the extracellular matrix
- conserved cysteine present in the cysteine-switch motif binds the catalytic Zn+2, thus inhibiting the enzyme
- dissociation of Cys from Zn+2 upon the activation- peptide release activates the enzyme
- contains 1 disintegrin domain
- contains 1 peptidase M12B domain
- contains 1 PLAC domain
- contains 8 TSP type-1 domains
Compartment
Alternative splicing
named isoforms=2
Expression
expressed exclusively in fetal lung
Pathology
- expressed in gastric carcinomas & in cancer cells of diverse origin