Abstract:
:Factor VII is a precursor to a serine protease that is present in mammalian plasma. In its activated form, it participates in blood coagulation by activating factor X and/or factor IX in the presence of tissue factor and calcium. Clones coding for factor VII were obtained from two cDNA libraries prepared from poly(A) RNA from human liver and Hep G2 cells. The amino acid sequence deduced from the cDNAs indicates that factor VII is synthesized with a prepro-leader sequence of 60 or 38 amino acids. The mature protein that circulates in plasma is a single-chain polypeptide composed of 406 amino acids. The amino acid sequence analysis of the protein and the amino acid sequence deduced from the cDNAs indicate that factor VII is converted to factor VIIa by the cleavage of a single internal bond between arginine and isoleucine. This results in the formation of a light chain (152 amino acids) and a heavy chain (254 amino acids) that are held together by a disulfide bond. The light chain contains a gamma-carboxyglutamic acid (Gla) domain and two potential epidermal growth factor domains, while the heavy chain contains the serine protease portion of the molecule. Factor VII shows a high degree of amino acid sequence homology with the other vitamin K-dependent plasma proteins.
journal_name
Proc Natl Acad Sci U S Aauthors
Hagen FS,Gray CL,O'Hara P,Grant FJ,Saari GC,Woodbury RG,Hart CE,Insley M,Kisiel W,Kurachi Kdoi
10.1073/pnas.83.8.2412subject
Has Abstract,Author List Incompletepub_date
1986-04-01 00:00:00pages
2412-6issue
8eissn
0027-8424issn
1091-6490journal_volume
83pub_type
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