title: Primary structure of human complement component C2. Homology to two unrelated protein families.
abstract: The primary structure of the second component of human complement (C2) was determined by cDNA cloning and sequence analysis. C2 has 39% identity with the functionally analogous protein Factor B. The C-terminal half of C2a is homologous to the catalytic domains of other serine proteinases. C2b contains three direct repeats of approx. 60 amino acid residues. They are homologous to repeats in Factor B, C4b-binding protein and Factor H, suggesting a functional significance of the repeat in C4b and C3b binding. The repeats are also found in the non-complement proteins beta 2-glycoprotein I and interleukin-2 receptor, and this repeat family may be widespread.
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002352:Carrier Proteins; D003175:Complement C2; D003180:Complement C3b Inactivator Proteins; D011415:Complement Factor B; D017242:Complement Factor H; D003169:Complement Inactivator Proteins; D004247:DNA; D006023:Glycoproteins; D006801:Humans; D012333:RNA, Messenger; D053482:beta 2-Glycoprotein I
chemical_list: C493495:CFH protein, human; D002352:Carrier Proteins; D003175:Complement C2; D003180:Complement C3b Inactivator Proteins; D003169:Complement Inactivator Proteins; D006023:Glycoproteins; D012333:RNA, Messenger; D053482:beta 2-Glycoprotein I; D017242:Complement Factor H; D004247:DNA; D011415:Complement Factor B