Abstract
With the aim of elucidating the evolutionary processes of the kringle and protease domains in serine proteases which are involved with the system of blood coagulation and fibrinolysis, we constructed phylogenetic trees for the kringle and protease domains, separately, by use of amino acid sequence data. The phylogenetic trees constructed clearly showed that the topologies were different between the kringle and protease domains. Because both domains are coded by single peptides of serine proteases, this strongly suggests that the kringle and protease domains must have undergone different evolutionary processes. Thus, these observations imply that serine proteases evolve in a way such that each domain is a unit of evolution, exemplifying a typical mode of domain evolution. A possible relationship between the domain evolution and the exon shuffling theory is also discussed from the viewpoint of gene evolution.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Apolipoproteins / chemistry
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Apolipoproteins / genetics
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Apoprotein(a)
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Biological Evolution*
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Factor XII / chemistry
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Factor XII / genetics
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Hepatocyte Growth Factor / chemistry
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Hepatocyte Growth Factor / genetics*
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Humans
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Kringles*
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Lipoprotein(a)*
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Molecular Sequence Data
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Plasminogen / chemistry
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Plasminogen / genetics
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Prothrombin / chemistry
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Prothrombin / genetics
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Sequence Alignment
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Sequence Homology, Amino Acid
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Serine Endopeptidases / chemistry
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Serine Endopeptidases / genetics*
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Tissue Plasminogen Activator / chemistry
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Tissue Plasminogen Activator / genetics
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Urokinase-Type Plasminogen Activator / chemistry
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Urokinase-Type Plasminogen Activator / genetics
Substances
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Apolipoproteins
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Lipoprotein(a)
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Hepatocyte Growth Factor
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Prothrombin
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Factor XII
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Plasminogen
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Apoprotein(a)
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Serine Endopeptidases
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Tissue Plasminogen Activator
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Urokinase-Type Plasminogen Activator