Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
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VMA22 IBA annotations derive from family-transfer context and are strongest for Vma12-Vma22 complex membership; unfolded protein binding is too broad.
"GOA WITH/FROM includes PANTHER evidence for GO:1990871 Vma12-Vma22 assembly complex and GO:0051082 unfolded protein binding."
UniProtKB entry for VMA22_YEAST
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Vma22 is required for V-ATPase activity and has two UniProt alternative initiation isoforms.
"FUNCTION: Required for V-ATPase activity. ALTERNATIVE PRODUCTS: Event = Alternative initiation; Named isoforms = 2."
Genes required for vacuolar acidity in Saccharomyces cerevisiae
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy
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The localization library used visual assignments without co-localization markers; the cached main text does not identify VMA22's individual score.
"Since no co-localization markers were used we only assigned localizations that could be easily discriminated by eye: ER, nuclear periphery, cytosol, cell periphery, vacuole lumen, vacuole membrane, mitochondria, nucleus, bud/bud neck and punctate"
Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complex
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Vma22 is ER-associated and required for V-ATPase assembly but is not a subunit of the mature V-ATPase.
"Vma22p is a 21-kDa hydrophilic protein that is not a subunit of the V-ATPase but rather is associated with ER membranes."
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Loss of VMA22 blocks V-ATPase complex assembly and activity.
"vma22 delta cells contain no V-ATPase activity due to a failure to assemble the enzyme complex."
vph6 mutants of Saccharomyces cerevisiae require calcineurin for growth and are defective in vacuolar H(+)-ATPase assembly
Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex
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Vma12 and Vma22 form a stable ER-associated complex that transiently interacts with Vph1 during V-ATPase assembly.
"Vma12p and Vma22p form a stable membrane associated complex. Cross-linking analysis also revealed a direct physical interaction between the Vma12p/Vma22p assembly complex and Vph1p."
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Vma22 is a dedicated assembly factor, not a general molecular chaperone.
"Unlike general molecular chaperones such as Kar2p/BiP (Gething and Sambrook, 1992), Vma12p, Vma21p, and Vma22p represent a class of ER resident proteins dedicated to the assembly of a specific enzyme complex, the V-ATPase."
Falcon deep research report for VMA22
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Falcon supports Vma22 as an ER-associated V-ATPase V0-region assembly factor and not a general unfolded-protein binding protein.
"**VMA22 (P38784/YHR060W)** encodes **Vma22p**, an **ER-associated peripheral assembly factor** required for **V-ATPase V0-region biogenesis**."