Sequence of a Menkes-type Cu-transporting ATPase from rat C6 glioma cells: comparison of the rat protein with other mammalian Cu-transporting ATPases

Rat Atp7a occupied a single open reading frame (274502) 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 additi...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 1998-04, Vol.181 (1-2), p.49-61
Main Authors: Qian, Y, Tiffany-Castiglioni, E, Harris, E D
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - genetics
Amino Acid Sequence
Amino Acid Substitution
Amino acids
Animals
Base Sequence
Binding Sites
Carrier Proteins - chemistry
Carrier Proteins - genetics
Cation Transport Proteins
Copper-transporting ATPases
DNA, Complementary - genetics
Glioma - enzymology
Heavy metals
Menkes Kinky Hair Syndrome - enzymology
Menkes Kinky Hair Syndrome - genetics
Metals, Heavy - metabolism
Molecular Sequence Data
Protein Structure, Secondary
Rats
Recombinant Fusion Proteins
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Tumor Cells, Cultured
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Summary:Rat Atp7a occupied a single open reading frame (274502) 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 theATPase transport function whereas variations to theATPase domain would be more critical.
ISSN:0300-8177
1573-4919
DOI:10.1023/A:1006896612272