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J. Biol. Chem., Vol. 263, Issue 28, 14152-14159, 10, 1988
AK Verma, AG Filoteo, DR Stanford, ED Wieben, JT Penniston, EE Strehler, R Fischer, R Heim, G Vogel and S Mathews
cDNAs coding for a plasma membrane Ca2+ pump were isolated from a human
teratoma library and sequenced. The translated sequence contained 1,220
amino acids with a calculated molecular weight of 134,683. All regions of
functional importance known from other ion-transporting ATPases could be
identified. The translated sequence also contained, near the carboxyl
terminus, the calmodulin-binding domain and two domains which are very rich
in glutamic acid and aspartic acid. These two domains resemble calmodulin
somewhat and one of them may play a role in the binding of Ca2+. The enzyme
also contains domains rich in serine and threonine, one of which has a
sequence matching those of good cAMP- dependent protein kinase substrates.
The carboxyl-terminal region is important for regulation by calmodulin,
proteolysis, and phosphorylation. Near the amino terminus are two domains
which are very rich in lysine and glutamic acid, as well as two domains
resembling EF hands, one of which also has some resemblance to calmodulin.
Comparison of the cloned sequence with peptide sequences from the
erythrocyte Ca2+ pump showed that the two proteins have a very high
proportion of identical residues but are not 100% identical, indicating
that they represent different isozymes.
Complete primary structure of a human plasma membrane Ca2+ pump
Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905.
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