Evolution of prothrombin: Isolation and characterization of the cDNAs encoding chicken and hagfish prothrombin |
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| Authors: | David K. Banfield David M. Irwin Daniel A. Walz Ross T.A. MacGillivray |
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| Affiliation: | (1) Department of Biochemistry, University of British Columbia, 2146 Health Sciences Mall, V6T 1Z3 Vancouver, Canada;(2) Department of Physiology, Wayne State University School of Medicine, 48201 Detroit, Michigan, USA;(3) Present address: MRC Laboratory of Molecular Biology, CB2 2QH Cambridge, U.K.;(4) Present address: Department of Clinical Biochemistry, University of Toronto, 100 College Street, M5G 1L5 Toronto, Ontario, Canada |
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| Abstract: | ![]()
The cDNA sequences of chicken and hagfish prothrombin have been determined. The sequences predict that prothrombin from both species is synthesized as a prepro-protein consisting of a putative Gla domain, two kringle domains, and a two-chain protease domain. Chicken and hagfish prothrombin share 51.6% amino acid sequence identity (313/627 residues). Both chicken and hagfish prothrombin are structurally very similar to human, bovine, rat, and mouse prothrombin and all six species share 41% amino acid sequence identity. Amino acid sequence alignments of human, bovine, rat, mouse, chicken, and hagfish prothrombin suggest that the thrombin B-chain and the propeptide-Gla domain are the regions most constrained for the common function(s) of vertebrate prothrombins.The nucleotide sequences reported in this paper have been submitted to the EMBL/Genbank database under the following secession numbers: M 81391 for Gallus gallus, M 81393 for Eptatretus stouti.Correspondence to: R.T.A. MacGillivray |
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| Keywords: | Prothrombin cDNA Hagfish |
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