3.4.21.41: complement subcomponent C1r
This is an abbreviated version!
For detailed information about complement subcomponent C1r, go to the full flat file.
Reaction
Selective cleavage of Lys(or Arg)-/-Ile bond in complement subcomponent C1s to form C_overbar_1s_ (EC 3.4.21.42) =
Synonyms
activated complement C1r, C1r, C1r protease, C1r serine protease, C1r-LP, C1rbar-esterase, complement C1r subcomponent-like protein, complement C1r, activated, complement protease C1r, complement subcomponent 1r, CUB, multiprotein complex C1, proteases C1r, serine protease C1r, Xld, xolloid
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.41 - complement subcomponent C1r
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glycoprotein
proteolytic modification
side-chain modification
proteolytic modification
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binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar
proteolytic modification
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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
proteolytic modification
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autolytic proteolysis involves cleavage of the Arg279-Gly280 bond in the sequence Asp-Ser-Arg-Gly-Trp-Lys
proteolytic modification
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activation of the proenzyme C1r can be mimicked under certain conditions by digestion of C1r with trypsin or plasmin
proteolytic modification
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the proenzyme C1r is not autoactivatable but undergoes proteolysis by exogenous C1rbar
proteolytic modification
autoactivation of C1r as part of the C1 complex, modeling, overview
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the A-chain contains 7.4% carbohydrate and the B-chain contains 12.4% carbohydrate
side-chain modification
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C1rbar contains about 40 carbohydrate residues per molecule
side-chain modification
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postranslational modification of C1r by beta-hydroxylation of specific Asp and Asn residues, 10% of the recombinant C1r is hydroxylated
side-chain modification
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in the case of the recombinant proteins the incompletely processed N-linked carbohydrate chains lack at least the terminal sialic acid residues