EC Number   |
Posttranslational Modification |
Reference  |
|---|
   3.4.21.41 | proteolytic modification |
activation of C1r involves cleavage of a single peptide bond which converts the proenzyme into active enzyme. Activation of the serine-proteinase domain of C1r is controlled by a Ca2+-dependent intramolecular mechanism involving the Ca2+-binding alpha-region. This control is released in C1 by a signal originating in C1q and transmitted through the C1q/C1r interface |
81388 |
| 3.4.21.41 | proteolytic modification |
- |
81389 |
| 3.4.21.41 | proteolytic modification |
binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar |
81390 |
| 3.4.21.41 | side-chain modification |
the zymogen C1r is a glycoprotein |
81391, 81395 |
| 3.4.21.41 | side-chain modification |
the A-chain contains 7.4% carbohydrate and the B-chain contains 12.4% carbohydrate |
81393 |
| 3.4.21.41 | proteolytic modification |
activation of the proenzyme C1r can be mimicked under certain conditions by digestion of C1r with trypsin or plasmin |
81395 |
| 3.4.21.41 | proteolytic modification |
the proenzyme is C1r |
81395 |
| 3.4.21.41 | side-chain modification |
C1rbar contains about 40 carbohydrate residues per molecule |
81395 |
| 3.4.21.41 | proteolytic modification |
the proenzyme C1r is not autoactivatable but undergoes proteolysis by exogenous C1rbar |
81397 |
| 3.4.21.41 | side-chain modification |
in the case of the recombinant proteins the incompletely processed N-linked carbohydrate chains lack at least the terminal sialic acid residues |
81400 |
