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A disintegrin & metalloproteinase with thrombospondin type 1 motif 7; ADAMTS-7; ADAM-TS 7; ADAM-TS7; COMPase (ADAMTS7)
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)
Kinetic parameters:
- 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
General
A disintegrin & metalloproteinase with thrombospondin type 1 motif (ADAMTS)
glycoprotein
Properties
SIZE: entity length = 1686 aa
MW = 184 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-27}
N-glycosylation site {N94}
Cysteine switch {202-209}
MOTIF: Zn+2-binding site
SITE: 204-204
Peptidase M12B {242-452}
MOTIF: cysteine residue {C366}
MODIFICATION: cysteine residue {C447}
Zn+2-binding site
SITE: 388-388
glutamate residue {E389}
Zn+2-binding site
SITE: 392-392
Zn+2-binding site
SITE: 398-398
cysteine residue {C405}
MODIFICATION: cysteine residue {C431}
cysteine residue {C431}
MODIFICATION: cysteine residue {C405}
cysteine residue {C447}
MODIFICATION: cysteine residue {C366}
disintegrin domain {462-537}
TSP1 module {538-593}
MOTIF: cysteine residue {C550}
MODIFICATION: cysteine residue {C587}
cysteine residue {C554}
MODIFICATION: cysteine residue {C592}
cysteine residue {C565}
MODIFICATION: cysteine residue {C577}
cysteine residue {C577}
MODIFICATION: cysteine residue {C565}
cysteine residue {C587}
MODIFICATION: cysteine residue {C550}
cysteine residue {C592}
MODIFICATION: cysteine residue {C554}
cysteine-rich region {595-697}
MOTIF: N-glycosylation site {N693}
Spacer {698-809}
MOTIF: N-glycosylation site {N778}
TSP1 module {821-880}
TSP1 module {881-940}
TSP1 module {942-995}
TSP1 module {1411-1459}
TSP1 module {1462-1522}
TSP1 module {1523-1567}
TSP1 module {1569-1629}
PLAC {1632-1672}
Database Correlations
OMIM 605009
UniProt Q9UKP4
PFAM correlations
Entrez Gene 11173
References
UniProt :accession Q9UKP4