Molecular and Cellular Biochemistry

, Volume 181, Issue 1, pp 49–61

Sequence of a Menkes-type Cu-transporting ATPase from Rat C6 Glioma Cells: Comparison of the rat protein with other mammalian Cu-transporting ATPases

  • Yongchang Qian
  • Evelyn Tiffany-Castiglioni
  • Edward D. Harris
Article

DOI: 10.1023/A:1006896612272

Cite this article as:
Qian, Y., Tiffany-Castiglioni, E. & Harris, E.D. Mol Cell Biochem (1998) 181: 49. doi:10.1023/A:1006896612272

Abstract

Rat Atp7a occupied a single open reading frame (27-4502) which coded for a protein of 1492 residues. Rat Atp7a was 98% and 95% identical to published sequences for the mouse and Chinese hamster, respectively, and 94% homologous to human ATP7A. Compared to ATP7A, the rat transcript coded for an additional alanine (A446) in the heavy metal binding (Hmb) domain and showed a 34 bp gap in the 3′ UTR. Based on published sequence data, hydropathic profiles for rat, mouse, Chinese hamster, and human Cu-ATPases were practically identical with the exception of 8 additional amino acid residues between the 4th and 5th Hmb sites in the human. As deduced from amino acid sequence data, Hmb was predicted to have regions with helical and beta structures. All four species had five of the six metal binding sites centered within hydrophobic regions. The comparative analyses suggested that the Hmb region of the molecule could experience numerous amino acid substitutions with no apparent disruption to the ATPase transport function whereas variations to the ATPase domain would be more critical.

Menkes gene Menkes transcript Cu-ATPase heavy metal binding domain rat brain ATPase copper homeostasis C6 rat glioma 

Copyright information

© Kluwer Academic Publishers 1998

Authors and Affiliations

  • Yongchang Qian
    • 1
  • Evelyn Tiffany-Castiglioni
    • 2
  • Edward D. Harris
    • 1
  1. 1.Department of Biochemistry and BiophysicsTexas and UniversityCollege StationUSA
  2. 2.Department of Veterinary Anatomy and Public HealthTexas A&M UniversityCollege StationUSA

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