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A disintegrin & metalloproteinase with thrombospondin type 1 motif 2; ADAMTS-2; ADAM-TS 2; ADAM-TS2; procollagen I/II amino propeptide-processing enzyme; procollagen I N-proteinase; PC I-NP; procollagen N-endopeptidase; pNPI (ADAMTS2, PCINP, PCPNI)
Function:
- cleaves the propeptides of collagen type 1 & collagen type 2 prior to fibril assembly
- does not act on collagen type 3
- may also play a role in development independent of its role in collagen biosynthesis
- may be component of a multimeric complex
- binds specifically to collagen type 14 (putative)
- precursor is cleaved by a furin endopeptidase
- cleaves the N-propeptide of collagen-1 alpha-1 at Pro-|-Gln & of collagen-2 alpha-1 & collagen-1 alpha-2 at Ala-|-Gln
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
- contains 1 disintegrin domain
- contains 1 peptidase M12B domain
- contains 1 PLAC domain
- contains 4 TSP type-1 domains
Compartment:
- secreted, extracellular space, extracellular matrix (putative)
Alternative splicing: named isoforms=2; LpNPI, SpNPI
Expression:
- expressed at high level in skin, bone, tendon & aorta & at low levels in thymus & brain
Pathology:
- defects in ADAMTS2 are the cause of Ehlers-Danlos syndrome type 7C
Note: has been referred to as ADAMTS3
General
A disintegrin & metalloproteinase with thrombospondin type 1 motif (ADAMTS)
glycoprotein
Properties
SIZE: entity length = 1211 aa
MW = 135 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-29}
alanine-rich region {40-43}
MOTIF: alanine residue (SEVERAL)
N-glycosylation site {N112}
glutamate-rich region {185-188}
MOTIF: glutamate residue (SEVERAL)
N-glycosylation site {N251}
Peptidase M12B {266-470}
MOTIF: cysteine residue {C386}
MODIFICATION: cysteine residue {C465}
Zn+2-binding site
SITE: 408-408
glutamate residue {E409}
Zn+2-binding site
SITE: 412-412
Zn+2-binding site
SITE: 418-418
cysteine residue {C425}
MODIFICATION: cysteine residue {C451}
cysteine residue {C451}
MODIFICATION: cysteine residue {C425}
cysteine residue {C465}
MODIFICATION: cysteine residue {C386}
disintegrin domain {480-560}
TSP1 module {561-616}
MOTIF: cysteine residue {C573}
MODIFICATION: cysteine residue {C610}
cysteine residue {C577}
MODIFICATION: cysteine residue {C615}
cysteine residue {C588}
MODIFICATION: cysteine residue {C600}
cysteine residue {C600}
MODIFICATION: cysteine residue {C588}
cysteine residue {C610}
MODIFICATION: cysteine residue {C573}
cysteine residue {C615}
MODIFICATION: cysteine residue {C577}
cysteine-rich region {618-722}
MOTIF: Cell attachment site {691-693}
Spacer {723-851}
TSP1 module {854-912}
TSP1 module {914-971}
MOTIF: N-glycosylation site {N949}
TSP1 module {975-1029}
MOTIF: cysteine residue {C987}
MODIFICATION: cysteine residue {C1023}
cysteine residue {C991}
MODIFICATION: cysteine residue {C1028}
N-glycosylation site {N993}
cysteine residue {C1002}
MODIFICATION: cysteine residue {C1012}
cysteine residue {C1012}
MODIFICATION: cysteine residue {C1002}
cysteine residue {C1023}
MODIFICATION: cysteine residue {C987}
cysteine residue {C1028}
MODIFICATION: cysteine residue {C991}
N-glycosylation site {N1031}
PLAC {1059-1097}
N-glycosylation site {N1098}
N-glycosylation site {N1145}
N-glycosylation site {N1150}
Database Correlations
OMIM correlations
UniProt O95450
PFAM correlations
Entrez Gene 9509
Kegg hsa:9509
ENZYME 3.4.24.14
References
UniProt :accession O95450