3.4.21.42	C1s(MASP-2 CCP1/2)	chimeric C1s protease containing the MASP-2 complement control protein domain, cleavage efficiency of C4 similar to MASP-2 protease	665686	
3.4.21.42	C1s(MASP-2 SP)	chimeric C1s protease containing the MASP-2 serine protease domain, cleavage efficiency similar to wild-type C1s	665686	
3.4.21.42	C294R	the mutation is associated with periodontal Ehlers-Danlos syndrome	752432	
3.4.21.42	D275S/P276I/K405V	similar to wild-type C1s	665686	
3.4.21.42	D343N	complement component C4 cleavage activity below 50% compared to wild-type, complement component C2 cleavage activity similar to wild-type	669727	
3.4.21.42	G630E	missense mutation, like normal C1s, the mutant has the ability to form a complex with rC1r. The activity of the mutant is significantly lower than that of wild-type, being only 60% of the activity of the wild-type rC1s. The mutant has a higher susceptibility to proteolysis than the wild-type, and prolonged proteolysis generates a truncated L chain with little or no protease activity	699344	
3.4.21.42	K628A	the mutant shows lower activity than wild-type enzyme against peptide substrates, cleavage of C4 is reduced by 5fold compared to the wild-type enzyme	731865	
3.4.21.42	K628Q	the mutant shows greater activity than wild-type enzyme against peptide substrates and peptide substrates containing physiological substrate sequences, unaltered activity with 2-aminobenzoyl-GLQRALEI-Lys(dinitrophenol)-NH2 substrate compared to the wild-type enzyme, but cleavage of C4 complement is reduced by 5fold compared to the wild-type enzyme	731865	
3.4.21.42	additional information	only the fragment bearing the serine protease (SP) and the complement control protein (CCP) module 2 of MASP-2 were expressed and crystallized	659718	
3.4.21.42	P341I	complement component C4 cleavage activity below 50% compared to wild-type, complement component C2 cleavage activity similar to wild-type	669727