Molecular Cloning of a cDNA Encoding Canine Factor IX

• Published in: Blood 1989-07, Vol.74 (1), p.207-212
• Main Authors: Evans, James P., Watzke, Herbert H., Ware, Jerry L., Stafford, Darrel W., High, Katherine A.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Cloning, Molecular; DNA - genetics; Dogs - genetics; Factor IX - genetics; Fundamental and applied biological sciences. Psychology; Genes. Genome; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Restriction Mapping
• ISSN: 0006-4971; 1528-0020
• DOI: 10.1182/blood.V74.1.207.207

Factor IX (F.IX) is a vitamin K-dependent plasma protein, a deficiency of which results in hemophilia B. A canine model of hemophilia B exists; attempts to use this model for gene transfer experiments or characterization of the hemophilic defect require elucidation of normal canine F.IX structure. We report the isolation and characterization of the coding region for canine F.IX cDNA. Canine F.IX possesses 86% identity at the amino-acid level with human F.IX. The leader peptide, Gia domain, EGF domains, and the carboxyterminal portion of the heavy chains show extensive sequence conservation between the canine and human. All Glu residues undergoing γ-carboxylation in humans are conserved in canines. The complete coding sequence for canine F.IX has been determined, and the derived translation product has been analyzed. A similar approach should allow identification of the causative mutation in canine hemophilia B. Furthermore, this clone may prove a valuable resource ip gene transfer experiments for this disease.