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A disintegrin & metalloproteinase with thrombospondin type 1 motif 20; ADAMTS-20; ADAM-TS 20; ADAM-TS20 (ADAMTS20)
Function:
- may play a role in tissue-remodeling process occurring in both normal & pathological conditions
- precursor is cleaved by a furin endopeptidase
Cofactor: binds 1 Zn+2 per subunit (putative)
Structure:
- 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=2
Expression:
- expressed at low levels in testis, prostate, ovary, heart, placenta, lung & pancreas
Pathology:
- overexpressed in several carcinomas:
a) brain neoplasms
b) colon carcinoma
c) breast carcinoma
General
A disintegrin & metalloproteinase with thrombospondin type 1 motif (ADAMTS)
glycoprotein
Properties
SIZE: entity length = 1910 aa
MW = 215 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-21}
N-glycosylation site {N92}
N-glycosylation site {N191}
Peptidase M12B {259-467}
MOTIF: cysteine residue {C381}
MODIFICATION: cysteine residue {C462}
Zn+2-binding site
SITE: 403-403
glutamate residue {E404}
Zn+2-binding site
SITE: 407-407
Zn+2-binding site
SITE: 413-413
cysteine residue {C419}
MODIFICATION: cysteine residue {C446}
N-glycosylation site {N445}
cysteine residue {C446}
MODIFICATION: cysteine residue {C419}
cysteine residue {C462}
MODIFICATION: cysteine residue {C381}
disintegrin domain {468-555}
TSP1 module {556-611}
MOTIF: cysteine residue {C568}
MODIFICATION: cysteine residue {C605}
cysteine residue {C572}
MODIFICATION: cysteine residue {C610}
cysteine residue {C583}
MODIFICATION: cysteine residue {C595}
cysteine residue {C595}
MODIFICATION: cysteine residue {C583}
cysteine residue {C605}
MODIFICATION: cysteine residue {C568}
cysteine residue {C610}
MODIFICATION: cysteine residue {C572}
cysteine-rich region {612-723}
MOTIF: N-glycosylation site {N702}
N-glycosylation site {N717}
Spacer {724-846}
MOTIF: N-glycosylation site {N728}
N-glycosylation site {N809}
TSP1 module {846-904}
MOTIF: N-glycosylation site {N870}
TSP1 module {905-961}
TSP1 module {966-1023}
TSP1 module {1024-1073}
MOTIF: N-glycosylation site {N1061}
TSP1 module {1076-1135}
TSP1 module {1152-1206}
TSP1 module {1207-1264}
TSP1 module {1304-1356}
TSP1 module {1358-1416}
TSP1 module {1417-1475}
MOTIF: N-glycosylation site {N1456}
TSP1 module {1476-1531}
TSP1 module {1535-1588}
MOTIF: N-glycosylation site {N1542}
N-glycosylation site {N1572}
TSP1 module {1589-1652}
TSP1 module {1654-1710}
GON {1711-1910}
MOTIF: N-glycosylation site {N1763}
N-glycosylation site {N1781}
N-glycosylation site {N1852}
Database Correlations
OMIM 611681
UniProt P59510
PFAM correlations
Entrez Gene 80070
Kegg hsa:80070
References
UniProt :accession P59510