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The complete cDNA sequence of bovine coagulation factor V
E R Guinto1, C T Esmon, K G Mann
1Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104.
The Journal of Biological Chemistry
|February 15, 1992
Summary
Researchers determined the primary structure of bovine factor V, revealing two variants and significant sequence identity with human factor Va, particularly in heavy and light chains. Differences in the B domain suggest evolutionary divergence between bovine and human factor V and factor VIII. Keywords: bovine factor V, primary structure, cDNA, human factor Va, evolution.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- The primary structure of bovine factor V (coagulation factor V) is crucial for understanding its structure-function relationships.
- Previous studies lacked detailed primary structure information for bovine factor V, limiting comprehensive analysis.
Purpose of the Study:
- To determine the complete primary amino acid sequence of bovine factor V.
- To compare the bovine factor V sequence with its human counterpart and factor VIII to infer evolutionary insights.
Main Methods:
- Synthesis of three complementary DNA (cDNA) libraries using liver messenger RNA (mRNA) from bovine sources.
- Sequencing of seven overlapping cDNA clones to assemble the full-length bovine factor V sequence.
- Bioinformatic analysis comparing deduced amino acid sequences with human factor Va and factor VIII.
Main Results:
- Identification of two distinct bovine factor V variants differing in coding sequence length.
- The deduced protein sequence comprises 2211 or 2206 amino acids, including a signal peptide.
- High sequence identity (84-86%) was observed between bovine and human factor Va heavy and light chains, respectively.
- Lower identity (59%) in the B domain (connecting region) with unique repeat structures in bovine factor V compared to human factor V.
- Identification of an 18-amino acid sequence homologous to human factor VIII's B domain within the bovine factor V sequence.
Conclusions:
- The determined primary structure of bovine factor V provides a foundation for detailed structure-function studies.
- Significant sequence conservation in heavy and light chains suggests functional importance, while B domain variations highlight evolutionary divergence.
- The identified homologous sequence in the B domain may indicate shared evolutionary origins or functional convergence between factor V and factor VIII.