3.4.21.41	glycoprotein	-	683195	
3.4.21.41	glycoprotein	carbohydrate content of C1r fragments	652176	
3.4.21.41	proteolytic modification	-	81389	
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	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	autoactivation of C1r as part of the C1 complex	683195	
3.4.21.41	proteolytic modification	autoactivation of C1r as part of the C1 complex, modeling, overview	683889	
3.4.21.41	proteolytic modification	autolytic proteolysis involves cleavage of the Arg279-Gly280 bond in the sequence Asp-Ser-Arg-Gly-Trp-Lys	81403	
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	proteolytic modification	the proenzyme C1r is not autoactivatable but undergoes proteolysis by exogenous C1rbar	81397