Cloning of a new cation ATPase from Plasmodium falciparum: conservation of critical amino acids involved in calcium binding in mammalian organellar Ca(2+)-ATPases.
In order to study molecules that may be involved in pH gradient formation in Plasmodium, we have identified a novel cation-translocating ATPase (P-type ATPase) gene from P. falciparum (Pf). We report the full-length nucleotide and deduced amino acid (aa) sequences of this gene that we called PfATPase4. The PfATPase4 protein shares features with the different members of eukaryotic P-type ATPases, such as a similar transmembrane (TM) organization and aa identity in functionally important regions. Interestingly, the PfATPase4 protein possesses conserved aa involved in calcium binding in mammalian organellar Ca(2+)-ATPases.
Trottein
F
F
Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Victoria, Australia.
Thompson
J
J
Cowman
A F
AF
D000251:Adenosine Triphosphatases / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002412:Cations; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D017124:Conserved Sequence; D004274:DNA, Recombinant; D006801:Humans; D008322:Mammals; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000201:enzymology / Q000235:genetics*; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid
D002412:Cations; D004274:DNA, Recombinant; D000251:Adenosine Triphosphatases; D000252:Calcium-Transporting ATPases; D002118:Calcium