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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

Target type

Proteins

Molecular weight

118637Da

We found 1 product in 1 category

Primary Antibodies

Target

Application

Search our catalogue for 'VMA1' (1)

Products