VMA1
Function
Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:18055462, PubMed:2139027). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:18055462, PubMed:2139027).
PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates 'homing', a genetic event that converts a VMA1 allele lacking VDE into one that contains it.
Post-translational modifications
This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.
Sequence Similarities
Belongs to the ATPase alpha/beta chains family.
Cellular localization
- Endomembrane system
- Peripheral membrane protein
- Cytoplasmic side
- Vacuole membrane
- Peripheral membrane protein
- Cytoplasmic side
- Membranes of various intracellular acidic compartments.
Alternative names
CLS8, TFP1, YDL185W, D1286, VMA1, V-type proton ATPase catalytic subunit A, V-ATPase subunit A, Vacuolar proton pump subunit A