Molecular cloning of human C1 inhibitor: sequence homologies with alpha 1-antitrypsin and other members of the serpins superfamily.
Genetic and acquired diseases in man show that the proteolytic activity of the complement component C1 is crucially regulated by C1 inhibitor (C1-INH), a plasma protein whose suspected relatedness to other serine proteinase inhibitors (serpins) contrasts with its atypically large size and high degree of glycosylation. Indeed we have found that the C1-INH polypeptide precursor synthesized in a cell-free system is a 64-kDa protein, hence it exceeds the length of the precursor forms of typical serpins. Seeking more conclusive sequence information and a probe for the structural locus, we isolated C1-INH cDNA clones from a library representing size-enriched human liver mRNA. Nucleotide sequence analysis of a clone covering the carboxyterminal half of C1-INH conclusively documents the relatedness of this protein with the serpins, and reveals 27% amino acid identity with alpha 1-antitrypsin.
D003001:Cloning, Molecular; D003174:Complement C1 Inactivator Proteins / Q000235:genetics*; D004247:DNA / Q000235:genetics; D006801:Humans; D008099:Liver / Q000502:physiology; D011480:Protease Inhibitors / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D012694:Serine; D000515:alpha 1-Antitrypsin / Q000235:genetics
D003174:Complement C1 Inactivator Proteins; D011480:Protease Inhibitors; D000515:alpha 1-Antitrypsin; D012694:Serine; D004247:DNA