Genomic and cDNA cloning of the human C1 inhibitor. Intron-exon junctions and comparison with other serpins.
Amino acid sequencing of trypsin fragments of C1 inhibitor gave regions of low codon degeneracy that were used for oligonucleotide probes. Human liver cDNA libraries gave clones containing most of the protein sequence, showing that the inhibitory domain belongs to the 'serpin' class of protein inhibitors. Fragments of these cDNA clones were used to probe human genomic cosmid libraries. The genomic sequence was found to be about 17 X 10(3) base pairs, with a coding sequence of approximately 1800 base pairs containing introns at amino acid positions--6, 162, 207, 275, 321, 395, and one in the 5' non-coding region. There is very little similarity of intron position amongst the serpin genes. All but one of the intron positions in the C1 inhibitor structural gene correspond to surface residues if C1 inhibitor is considered to have a structure similar to the cleaved form of alpha 1-antiproteinase. The serine and threonine residues in the N-terminal 100 amino acids of the sequence thought to carry complex carbohydrates are found in a single exon.
Carter
P E
PE
Department of Biochemistry, University of Aberdeen, Scotland.
Dunbar
B
B
Fothergill
J E
JE
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003174:Complement C1 Inactivator Proteins / Q000235:genetics* / Q000302:isolation & purification; D004247:DNA / Q000302:isolation & purification*; D005091:Exons; D005796:Genes; D006801:Humans; D007438:Introns; D008969:Molecular Sequence Data; D009841:Oligonucleotides; D010446:Peptide Fragments / Q000302:isolation & purification; D012697:Serine Endopeptidases / Q000235:genetics*; D014357:Trypsin
D003174:Complement C1 Inactivator Proteins; D009841:Oligonucleotides; D010446:Peptide Fragments; D004247:DNA; D012697:Serine Endopeptidases; D014357:Trypsin