A disintegrin & metalloproteinase with thrombospondin type 1 motif 7; ADAMTS-7; ADAM-TS 7; ADAM-TS7; COMPase (ADAMTS7)
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Function
- metalloprotease
- may play a role in the degradation of COMP
- interacts with COMP
- may be cleaved by a furin endopeptidase
- precursor is sequentially processed
Cofactor: binds 1 Zn+2 per subunit (putative)
- Optimum pH is between 7.5 & 9.5
Structure
- N-glycosylated
- O-glycosylated proteoglycan
- contains chondroitin sulfate
- spacer domain & the TSP type-1 domains are important for a tight interaction with the extracellular matrix
- the conserved Cys 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
- secreted, extracellular space, extracellular matrix (putative)
- also found associated with the external cell surface (putative)
Alternative splicing
named isoforms=2
Expression
- expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney & pancreas
- detected in meniscus, bone, tendon, cartilage, synovium, fat & ligaments
- up-regulated in articular cartilage & synovium from patients with osteoarthritis