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Evolution of prothrombin: Isolation and characterization of the cDNAs encoding chicken and hagfish prothrombin

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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.

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Author notes

  1. David K. Banfield

    Present address: MRC Laboratory of Molecular Biology, CB2 2QH, Cambridge, U.K.

  2. David M. Irwin

    Present address: Department of Clinical Biochemistry, University of Toronto, 100 College Street, M5G 1L5, Toronto, Ontario, Canada

Authors and Affiliations

  1. Department of Biochemistry, University of British Columbia, 2146 Health Sciences Mall, V6T 1Z3, Vancouver, Canada

    David K. Banfield, David M. Irwin & Ross T.A. MacGillivray

  2. Department of Physiology, Wayne State University School of Medicine, 48201, Detroit, Michigan, USA

    Daniel A. Walz

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  1. David K. Banfield
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  2. David M. Irwin
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  4. Ross T.A. MacGillivray
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Additional information

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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Banfield, D.K., Irwin, D.M., Walz, D.A. et al. Evolution of prothrombin: Isolation and characterization of the cDNAs encoding chicken and hagfish prothrombin. J Mol Evol 38, 177–187 (1994). https://doi.org/10.1007/BF00166164

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  • DOI: https://doi.org/10.1007/BF00166164

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