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A disintegrin & metalloproteinase with thrombospondin type 1 motif 1; ADAMTS-1; ADAM-TS 1; ADAM-TS1; METH-1 (ADAMTS1, KIAA1346, METH1)
Function:
- cleaves aggrecan, a cartilage proteoglycan, & may play role in its turnover (putative)
- cleaves aggrecan at the 1938-Glu-|-Leu-1939 site, within the chondroitin sulfate attachment domain
- has angiogenic inhibitor activity
- active metalloprotease
- may be associated with various inflammatory processes
- may play role in follicular rupture
- precursor is cleaved by a furin endopeptidase
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 Cys present in the cysteine-switch motif binds the catalytic Zn+2, thus inhibiting the enzyme
- dissociation of Cys from Zn+2 upon activation- peptide release activates the enzyme
- contains 1 disintegrin domain
- contains 1 peptidase M12B domain
- contains 3 TSP type-1 domains
Compartment:
- secreted, extracellular space, extracellular matrix (putative)
Pathology:
- may play role in development of cancer cachexia
General
A disintegrin & metalloproteinase with thrombospondin type 1 motif (ADAMTS)
glycoprotein
Properties
SIZE: MW = 105 kD
entity length = 967 aa
COMPARTMENT: extracellular compartment
MOTIF: cysteine switch
SITE: C198
FOR-BINDING-OF: Zn+2
MOTIF: cysteine residue
active site
SITE: E402
disintegrin domain {476-559}
MOTIF: N-glycosylation site {N547}
TSP1 module {560-616}
cysteine-rich region {617-724}
MOTIF: N-glycosylation site {N720}
N-glycosylation site {N764}
TSP1 module {850-908}
TSP1 module {909-967}
Database Correlations
OMIM 605174
UniProt Q9UHI8
PFAM correlations
Entrez Gene 9510
Kegg hsa:9510
References
UniProt :accession Q9UHI8