|Name:||ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e|
|Aliases:||M9.2, Vma21p, VMA21|
|Old Name:||ATPase, H+ transporting, lysosomal (vacuolar proton pump) 9kD|
|PubMed (9556572):|| Ludwig J, Kerscher S, Brandt U, Pfeiffer K, Getlawi F, Apps DK, Schagger H. Identification and characterization of a novel 9.2-kDa membranesector-associated protein of vacuolar proton-ATPase from chromaffin granules.J Biol Chem. 1998 May 1;273(18):10939-47. PMID: 9556572 [PubMed - indexed for MEDLINE]|
Vacuolar proton-translocating ATPase (holoATPase and free membrane sector) was isolated from bovine chromaffin granules by blue native polyacrylamide gel electrophoresis. A 5-fold excess of membrane sector over holoenzyme was determined in isolated chromaffin granule membranes. M9.2, a novel extremely hydrophobic 9.2-kDa protein comprising 80 amino acids, was detected in the membrane sector. It shows sequence and structural similarity to Vma21p, a yeast protein required for assembly of vacuolar ATPase. A second membrane sector-associated protein (M8-9) was identified and characterized by amino-terminal protein sequencing.