CLONING OF A NEW CATION ATPASE FROM PLASMODIUM-FALCIPARUM - CONSERVATION OF CRITICAL AMINO-ACIDS INVOLVED IN CALCIUM-BINDING IN MAMMALIAN ORGANELLAR CA2+-ATPASES
- Author(s)
- Trottein, F; Thompson, J; Cowman, AF;
- Details
- Publication Year 1995-05-26,Volume 158,Issue #1,Page 133-137
- Journal Title
- GENE
- Publication Type
- Journal Article
- 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 Ca2+-ATPases.
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- SARCOPLASMIC-RETICULUM; CA-2+ PUMP; CA-2+-ATPASE; GENE; CHLOROQUINE; PROTEIN; ACIDIFICATION; ERYTHROCYTES; SEQUENCE; SUBUNIT
- Publisher's Version
- https://doi.org/10.1016/0378-1119(95)00158-3
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 1995-05-26 12:00:00