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