Structure of murine complement component C3. II. Nucleotide sequence of cloned complementary DNA coding for the alpha chain.
From the inserts of two recombinant plasmids isolated from a murine liver cDNA library, the nucleotide sequence coding for the C3 alpha chain was obtained and the corresponding amino acid sequence was derived. The alpha chain portion of the mRNA is 2979 nucleotides long, specifying a polypeptide of 993 amino acids. The molecular weight of the alpha chain, in the absence of carbohydrate, was calculated from the sequence data to be 112,933. Two possible carbohydrate attachment sites were predicted at residues 269 (Asn) and 947 (Asn). In addition, the positions for two putative factor I cleavage sites were predicted from a comparison with the cleavage sites in the human C3 alpha chain. The C3 alpha chain contains 24 cysteine residues, 10 of these clustered in the C-terminal 175 amino acids of the alpha chain. Together with the accompanying report (Lundwall, A, Wetsel, R.A., Domdey, H., Tack, B.F., and Fey, G.H. (1984) J. Biol. Chem. 259, 13851-13856), this study completes the nucleotide and amino acid structure of the murine precursor prepro-C3 molecule.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon / Q000032:analysis; D003176:Complement C3 / Q000235:genetics*; D004247:DNA / Q000032:analysis*; D004262:DNA Restriction Enzymes / Q000378:metabolism; D008099:Liver / Q000032:analysis; D051379:Mice; D008970:Molecular Weight
D003062:Codon; D003176:Complement C3; D004247:DNA; D004262:DNA Restriction Enzymes