VMA1 (V-type proton ATPase catalytic subunit A)

FEATURES

ORGANISM

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

FAMILY

DESCRIPTION

Also known as VATA_YEAST, VMA1, CLS8, TFP1. Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit., 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. V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.

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EXTERNAL LINKS

VMA1

V-type proton ATPase catalytic subunit A

MOLECULAR SYNOPSIS STRUCTURAL LIGANDABILITY

VMA1

Molecular Synopsis