Cloning of a new cation ATPase from Plasmodium falciparum: conservation of critical amino acids involved in calcium binding in mammalian organellar Ca(2+)-ATPases

Gene. 1995 May 26;158(1):133-7. doi: 10.1016/0378-1119(95)00158-3.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics*
  • Adenosine Triphosphatases / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Calcium / metabolism*
  • Calcium-Transporting ATPases / metabolism*
  • Cations
  • Chromosome Mapping
  • Cloning, Molecular
  • Conserved Sequence*
  • DNA, Recombinant
  • Humans
  • Mammals
  • Molecular Sequence Data
  • Plasmodium falciparum / enzymology
  • Plasmodium falciparum / genetics*
  • Protein Binding
  • Sequence Homology, Amino Acid

Substances

  • Cations
  • DNA, Recombinant
  • Adenosine Triphosphatases
  • Calcium-Transporting ATPases
  • Calcium

Associated data

  • GENBANK/U16995