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J. Biol. Chem., Vol. 263, Issue 18, 8646-8657, 06, 1988
GE Shull and J Greeb
Complementary DNAs for two isoforms of the plasma membrane Ca2+-ATPase from
rat brain have been isolated. The cDNAs were identified using an
oligonucleotide probe derived from a conserved amino acid sequence of the
ATP binding site of the aspartylphosphate family of transport ATPases. The
complete nucleotide sequences have been determined, and the primary
structures for both isoforms have been deduced. The Mr of isoform 1, which
has 1,176 amino acids, is 129,500 and that of isoform 2, which has 1,198
amino acids, is 132,605. A region of isoform 1 exhibits perfect amino acid
identity with a fragment consisting of 17 amino acids from the
phosphorylation domain of the human erythrocyte calmodulin-sensitive
Ca2+-ATPase (James, P., Zvaritch, E.I., Shakhparonov, M.I., Penniston,
J.T., and Carafoli, E. (1987) Biochem. Biophys. Res. Commun. 149, 7-12). A
comparison of transport ATPases from diverse species has allowed the
identification of a sequence that may form part of a second ATP binding
site. Amino acid similarity and hydropathy profile comparisons suggest that
the transmembrane organization of the plasma membrane Ca2+-ATPase is the
same as that of the Na+,K+-ATPase and sarcoplasmic reticulum Ca2+-ATPase;
the data indicate that each of these enzymes has an even number of
transmembrane domains and that their C termini are located on the
cytoplasmic side of the membrane. An arginine-rich sequence that is highly
characteristic of the "A" domain of a calmodulin binding site is located
near the C termini of both isoforms. This putative A domain is identical in
isoforms 1 and 2 but their "B" domains, and the remaining C-terminal
sequences, are very different. However, 3'-untranslated sequences of the
isoform 1 transcript have the potential to encode a calmodulin binding B
domain and a C terminus that is very similar to that of isoform 2. This
suggests the possibility that additional diversity may occur via
alternative processing of the primary transcript.
Molecular cloning of two isoforms of the plasma membrane Ca2+- transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+,K+- and other cation transport ATPases
Department of Microbiology and Molecular Genetics, University of Cincinnati College of Medicine, Ohio 45267-0524.
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