EC Number |
Posttranslational Modification |
Reference |
---|
3.4.24.87 | glycoprotein |
- |
719163, 719761 |
3.4.24.87 | glycoprotein |
ADAMTS13 is a multidomain glycoprotein |
711563 |
3.4.24.87 | glycoprotein |
binding site for alpha-mannosyl residue, 10 potential N-glycosylation sites, Asn-Xaa-Thr/Ser |
652191 |
3.4.24.87 | glycoprotein |
enzym contains 10 potential N-glycosylation sites |
652481 |
3.4.24.87 | glycoprotein |
N-glycosylation |
653678 |
3.4.24.87 | glycoprotein |
N-glycosylation is necessary for efficient secretion of ADAMTS13, while conversion of the N-glycans from oligomannose to complex type in the Golgi complex enhances the proteolytic activity of the protease toward von Willebrand factor multimers. After its secretion, ADAMTS13 does not require N-glycans for its von Willebrand factor cleaving activity |
691464 |
3.4.24.87 | glycoprotein |
the ADAMTS13 ancillary domains, ADAMTS13-DTCS, contain four potential N-glycosylation sites |
710732 |
3.4.24.87 | proteolytic modification |
made as a zymogen, requires proteolytic activation, possibly intracellularly by furin, cleavage of residues 1-74 |
652191 |
3.4.24.87 | proteolytic modification |
propeptide is very short and poorly conserved, dispensable for protein folding, is cleaved off by furin after export from the endoplasmic reticulum, the pro-enzyme form is fully active |
652481 |
3.4.24.87 | proteolytic modification |
the pro-peptide is removed during self-activation, which is not required for full enzyme activity |
711809 |