Genomic organization of the serine protease light chain of mouse complement factor I gene.
A portion of the mouse complement factor I (mCFI) gene encoding for the mCFI light chain was cloned from a mouse 129/SVJ1 bacterial artificial chromosome library. It contains five exons and four introns. The intron sizes are remarkably different from the human homolog. Several polymorphisms were found in exon 13. One polymorphism was in the coding region, which causes a threonine in the Balb/c mCFI to be replaced by an isoleucine in the 129/SVJ1 mCFI. The other two polymorphisms are located in the 3' untranslated region. The organization of the serine protease domain in mCFI is similar to that of trypsin but very different from that of the other complement serine proteases.
Jiang
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N
Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA.
Molina
H
H
D019943:Amino Acid Substitution; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D017244:Complement Factor I / Q000235:genetics*; D005091:Exons; D015723:Gene Library; D016678:Genome; D006801:Humans; D007438:Introns; D007532:Isoleucine; D046911:Macromolecular Substances; D051379:Mice; D008807:Mice, Inbred BALB C; D008815:Mice, Inbred Strains / Q000235:genetics*; D008969:Molecular Sequence Data; D011110:Polymorphism, Genetic; D012697:Serine Endopeptidases / Q000235:genetics*; D013912:Threonine
D046911:Macromolecular Substances; D007532:Isoleucine; D013912:Threonine; D012697:Serine Endopeptidases; D017244:Complement Factor I