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A disintegrin & metalloproteinase with thrombospondin type 1 motif 9; ADAMTS-9; ADAM-TS 9; ADAM-TS9 (ADAMTS9, KIAA1312)
Function:
- cleaves the large aggregating proteoglycans, aggrecan & versican
- cleaves aggrecan at the 1838-Glu-|-Ala-1839 site & versican at the 1428-Glu-|-Ala-1429 site
- precursor is cleaved by a furin endopeptidase
Cofactor: binds 1 Zn+2 per subunit (putative)
Structure:
- spacer domain & the TSP type-1 domains are important for a tight interaction with the extracellular matrix
- ancillary domains, including the TSRs domain, are required for specific extracellular localization & for its activity towards versican & aggrecan
- 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 activation- peptide release activates the enzyme
- contains 1 disintegrin domain
- contains 1 GON domain
- contains 1 peptidase M12B domain
- contains 15 TSP type-1 domains
Compartment:
- secreted, extracellular space, extracellular matrix (putative)
Alternative splicing: named isoforms=3
Expression:
- highly expressed in all fetal tissues
- expressed in a number of adult tissues with highest expression in heart, placenta & skeletal muscle
General
A disintegrin & metalloproteinase with thrombospondin type 1 motif (ADAMTS)
glycoprotein
Properties
SIZE: entity length = 1935 aa
MW = 216 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-18}
serine-rich region {88-96}
MOTIF: serine residue (SEVERAL)
N-glycosylation site {N112}
N-glycosylation site {N135}
Cysteine switch {221-228}
MOTIF: Zn+2-binding site
SITE: 223-223
N-glycosylation site {N271}
Peptidase M12B {293-499}
MOTIF: cysteine residue {C412}
MODIFICATION: cysteine residue {C494}
Zn+2-binding site
SITE: 434-434
glutamate residue {E435}
Zn+2-binding site
SITE: 438-438
Zn+2-binding site
SITE: 444-444
cysteine residue {C450}
MODIFICATION: cysteine residue {C478}
cysteine residue {C478}
MODIFICATION: cysteine residue {C450}
cysteine residue {C494}
MODIFICATION: cysteine residue {C412}
disintegrin domain {509-587}
TSP1 module {588-643}
MOTIF: cysteine residue {C600}
MODIFICATION: cysteine residue {C637}
cysteine residue {C604}
MODIFICATION: cysteine residue {C642}
cysteine residue {C615}
MODIFICATION: cysteine residue {C627}
cysteine residue {C627}
MODIFICATION: cysteine residue {C615}
cysteine residue {C637}
MODIFICATION: cysteine residue {C600}
cysteine residue {C642}
MODIFICATION: cysteine residue {C604}
cysteine-rich region {644-752}
MOTIF: N-glycosylation site {N749}
Spacer {753-877}
MOTIF: N-glycosylation site {N840}
TSP1 module {878-936}
MOTIF: cysteine residue {C890}
MODIFICATION: cysteine residue {C931}
cysteine residue {C894}
MODIFICATION: cysteine residue {C935}
cysteine residue {C904}
MODIFICATION: cysteine residue {C918}
cysteine residue {C918}
MODIFICATION: cysteine residue {C904}
cysteine residue {C931}
MODIFICATION: cysteine residue {C890}
cysteine residue {C935}
MODIFICATION: cysteine residue {C894}
TSP1 module {939-997}
TSP1 module {998-1049}
TSP1 module {1052-1109}
TSP1 module {1110-1166}
TSP1 module {1182-1240}
MOTIF: N-glycosylation site {N1213}
TSP1 module {1241-1296}
MOTIF: cysteine residue {C1250}
MODIFICATION: cysteine residue {C1290}
cysteine residue {C1254}
MODIFICATION: cysteine residue {C1295}
cysteine residue {C1265}
MODIFICATION: cysteine residue {C1278}
N-glycosylation site {N1267}
cysteine residue {C1278}
MODIFICATION: cysteine residue {C1265}
cysteine residue {C1290}
MODIFICATION: cysteine residue {C1250}
cysteine residue {C1295}
MODIFICATION: cysteine residue {C1254}
TSP1 module {1328-1379}
TSP1 module {1382-1440}
TSP1 module {1441-1494}
TSP1 module {1497-1555}
TSP1 module {1556-1611}
TSP1 module {1612-1676}
MOTIF: cysteine residue {C1624}
MODIFICATION: cysteine residue {C1670}
cysteine residue {C1628}
MODIFICATION: cysteine residue {C1675}
cysteine residue {C1639}
MODIFICATION: cysteine residue {C1659}
cysteine residue {C1659}
MODIFICATION: cysteine residue {C1639}
cysteine residue {C1670}
MODIFICATION: cysteine residue {C1624}
cysteine residue {C1675}
MODIFICATION: cysteine residue {C1628}
TSP1 module {1677-1734}
GON {1735-1935}
MOTIF: N-glycosylation site {N1788}
N-glycosylation site {N1806}
Database Correlations
OMIM 605421
UniProt Q9P2N4
PFAM correlations
Entrez Gene 56999
Kegg hsa:56999
References
UniProt :accession Q9P2N4