EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.45 | glycoprotein |
factor I is a multidomain acute phase glycoprotein, that is N-glycosylated at six positions (25-27%, w/w) with heavily sialylated biantennary glycans. Three-dimensional overview of the glycosylation sites. Deglycosylation by endoglycosidases, profile overview |
732047 |
| 3.4.21.45 | glycoprotein |
N-glycosylation sites are Asn-73, 421, 493 and 535, and a O-glycosylation sites is Thr-36. Has little species-specificity like human factor I, according to the relatively high homology of the AA sequences in the serine protease region, in comparison with those of membrane complement regulatory proteins |
701342 |
| 3.4.21.45 | glycoprotein |
sequence contains three potential N-glycosylation sites |
717618 |
| 3.4.21.45 | glycoprotein |
the first GlcNAc residue of each of the six N-linked glycosylation sites is ordered and visible in the electron density, crystallization data |
718324 |
| 3.4.21.45 | proteolytic modification |
CFI mRNA is translated in both a heavy and light chain which is further cleaved at a tetrapeptide processing site |
717618 |
| 3.4.21.45 | side-chain modification |
carbohydrate content is at least 10.7% w/w, not including neuraminic acid, with 7.2% hexose and 3.2% glucosamine |
95489 |
| 3.4.21.45 | side-chain modification |
glycoprotein |
95484, 95488, 95494 |
| 3.4.21.45 | side-chain modification |
glycosylation of more than 20% of the total mass |
95493 |
| 3.4.21.45 | side-chain modification |
most of the six potential N-glycosylation acceptance sites are utilized in the mouse protein |
95494 |
