VMA2 — Neurospora crassa

Summary

NCU08515, designated VMA2 in Neurospora crassa and located on chromosome 2, encodes the B subunit of the vacuolar ATPase (V-ATPase) V1 domain, a component of the proton-transporting ATP synthase complex that exhibits ATP hydrolase activity and binds ADP and ATP. The gene is associated with vacuolar acidification, proton transmembrane transport, ATP metabolism, proton motive force-driven mitochondrial ATP synthesis, and autophagy. It localises to the V1 domain, mitochondrial inner membrane, plasmalemma, and cytoplasm. Phenotypic associations link VMA2 to abnormal replicative lifespan, prion inheritance and formation, cell cycle progression, budding pattern, endocytosis, vacuolar transport, micronucleophagy, pheromone sensitivity, hyperosmotic stress resistance, innate thermotolerance, alkaline pH resistance, colony colour, Golgi morphology, nuclear size, and nutrient uptake. Studies of related genes in other species connect the V-ATPase family to zinc, calcium, and acid sensitivity, as well as oxidative stress response.

Annotations

Chromosome
2
Related genes
VMA2, DBF2, SCS7, VMA10, GSH1, UTP10, ARC35, RBG2
GO terms
Proton Motive Force-driven Mitochondrial ATP Synthesis, ATP Binding, Cytoplasm, plasmalemma, F1-F0 complex, Proton-transporting ATP Synthase Activity, Rotational Mechanism, mitochondria, ATP hydrolase activity
Publications
19214209, 34849884, 9491072, 22244335, 33513092, 32737079, 8307336, 22526809
Traits
RESISTANCE TO CHEMICALS: DECREASED, COMPETITIVE FITNESS: DECREASED, STRESS RESISTANCE: DECREASED, INVIABLE, RESISTANCE TO CHEMICALS: INCREASED, CELL CYCLE PROGRESSION: ABNORMAL, ENTRY INTO G0 (STATIONARY PHASE): INCREASED, RESISTANCE TO CHEMICALS: NORMAL