Phylogenetic analysis of P5 P-type ATPases, a eukaryotic lineage of secretory pathway pumps.
Eukaryotes encompass a remarkable variety of organisms and unresolved lineages. Different phylogenetic analyses have lead to conflicting conclusions as to the origin and associations between lineages and species. In this work, we investigated evolutionary relationship of a family of cation pumps exclusive for the secretory pathway of eukaryotes by combining the identification of lineage-specific genes with phylogenetic evolution of common genes. Sequences of P5 ATPases, which are regarded to be cation pumps in the endoplasmic reticulum (ER), were identified in all eukaryotic lineages but not in any prokaryotic genome. Based on a protein alignment we could group the P5 ATPases into two subfamilies, P5A and P5B that, based on the number of negative charges in conserved trans-membrane segment 4, are likely to have different ion specificities. P5A ATPases are present in all eukaryotic genomes sequenced so far, while P5B ATPases appear to be lost in three eukaryotic lineages; excavates, entamoebas and land plants. A lineage-specific gene expansion of up to four different P5B ATPases is seen in animals.
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000145:classification* / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D027682:Cation Transport Proteins / Q000737:chemistry / Q000145:classification* / Q000235:genetics; D004747:Entamoeba / Q000145:classification; D017353:Gene Deletion; D017343:Genes, Plant; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment
D027682:Cation Transport Proteins; D000251:Adenosine Triphosphatases