EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.4.39 | glycoprotein |
- |
678439, 680925, 682694, 695455, 697080, 697490, 698987, 700238, 700364, 700525, 713629, 716315 |
| 3.1.4.39 | glycoprotein |
ATX is synthesized as pre-pro-enzyme and secreted upon removal of the N-terminal signal peptide and further trimming by a furine-type protease |
696397 |
| 3.1.4.39 | glycoprotein |
N-glycosylation of NPP2 is essential for the expression of its catalytic activity. Lysophospholipase-D activity and the nucleotide phosphodiesterase activity of rat are abolished by deglycosylation. Examination of the structure of the essential glycan side chain of Asn524. Catalytic activity of NPP2 is critically dependent on the presence of a Man8/9GlcNAc2 moiety on Asn-524, a site that is phylogenetically conserved, not only in NPP2 but also in six of seven NPP isozymes. Suggestion that this glycan chain has a structural function and is involved in the interaction between the catalytic and nuclease-like domains of NPP2 |
680750 |
| 3.1.4.39 | proteolytic modification |
ATX is synthesized as a preproenzyme and proteolytically processed, the mature protein is secreted |
713665 |
| 3.1.4.39 | proteolytic modification |
cleaved at two N-terminal sites that match the consensus sequences for a signal sequence and furin |
665048 |
| 3.1.4.39 | proteolytic modification |
proteolytically processed protein is secreted, secreted and cell-associated NPP2 are differently glycosylated |
665800 |
