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Journal of Molecular Evolution

, Volume 46, Issue 3, pp 327–333 | Cite as

Origin of the NEFA and Nuc Signal Sequences

  • Anton  Karabinos
  • Debashish  Bhattacharya
  • Hartmut D.  Kratzin
  • Norbert  Hilschmann

Abstract.

The human protein NEFA binds calcium, contains a leucine zipper repeat that does not form a homodimer, and is proposed (along with the homologous Nuc protein) to have a common evolutionary history with an EF-hand ancestor. We have isolated and characterized the N-terminal domain of NEFA that contains a signal sequence inferred from both endoproteinase Asp-N (Asp-N) and tryptic digests. Analysis of this N-terminal sequence shows significant similarity to the conserved multiple domains of the mitochondrial carrier family (MCF) proteins. The leader sequence of Nuc is, however, most similar to the signal sequences of membrane and/or secreted proteins (e.g., mouse insulin-like growth factor receptor). We suggest that the divergent NEFA and Nuc N-terminal sequences may have independent origins and that the common high hydrophobicity governs their targeting to the ER. These results provide insights into signal sequence evolution and the multiple origins of protein targeting.

Key words: EF-hand — Gene duplication — Molecular evolution — Nuc — Secretory proteins 

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Copyright information

© Springer-Verlag New York Inc. 1998

Authors and Affiliations

  • Anton  Karabinos
    • 1
  • Debashish  Bhattacharya
    • 2
  • Hartmut D.  Kratzin
    • 1
  • Norbert  Hilschmann
    • 1
  1. 1.Department of Immunochemistry, Max Planck Institute for Experimental Medicine, Hermann-Rein-Straße 3, 37075 Göttingen, GermanyDE
  2. 2.Department of Biological Sciences, University of Iowa, 138 Biology Building, Iowa City, IA 52242-1324, USAUS

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