Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway.
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The abstract identifies a2 targeting to early endosomes. This supports the endosomal location, while the separately documented ARNO association does not establish autonomous GEF activity.
"The a2-isoform is targeted to early endosomes"
Integral and associated lysosomal membrane proteins.
Cloning of a cDNA for a T cell produced molecule with a putative immune regulatory role.
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Hybrid-selected translated material suppressed a mixed-lymphocyte reaction. The result is real at the described assay scope, while transfer from historical mouse J6B7 to intact human ATP6V0A2 remains unresolved.
"significant suppression of a mixed lymphocyte
reaction (MLR)"
Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts.
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The abstract distinguishes lipofuscin formation from its macroautophagic uptake. This does not resolve whether a2 itself regulates macroautophagy in the experiment.
"macroautophagy is responsible
for the uptake of lipofuscin into the lysosomes."
The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1α prolyl hydroxylation by regulating cellular iron levels.
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The human HeLa CRISPR validation includes ATP6V0A2 and measures HIF reporter and endogenous HIF stabilization under aerobic culture. This does not establish an oxygen step-up response or an a2-specific iron-rescue assay.
"or ATP6V0A2. GFP levels were assessed by flow cytometry"
Structure and Roles of V-type ATPases.
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This review describes organelle acidification by assembled V-ATPases as family context. Its abstract does not establish an a2-specific primary experiment.
"V-ATPases are the primary source of organellar
acidification"
Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.
Intraphagosomal pH is lowered to 5 by V-ATPase
Acidification of Tf:TfR1 containing endosome
UniProtKB ATP6V0A2 record Q9Y487
Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2.
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Patient ATP6V0A2 mutations accompany abnormal serum-protein glycosylation and impaired Golgi trafficking in affected fibroblasts; the abstract is not a direct pH measurement.
"cause an impairment of Golgi trafficking"
The Human Mutation K237_V238del in a Putative Lipid Binding Motif within the V-ATPase a2 Isoform Suggests a Molecular Mechanism Underlying Cutis Laxa.
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The PI4P-binding study uses the purified human a2 N-terminal fragment, amino acids 1–400. Its binding and Golgi-retention results do not by themselves establish full-length pump activation.
"human a2 (amino acid 1–400)"
Golgi pH elevation due to loss of V-ATPase subunit V0a2 function correlates with tissue-specific glycosylation changes and globozoospermia.
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Human a2-V5 constructs localize with a trans-Golgi marker in HeLa cells. This is separate from the calibrated Golgi-pH measurements performed in mutant mouse fibroblasts.
"V0a2-RQ with trans-Golgi network marker TGN46"
A proton pump ATPase with testis-specific E1-subunit isoform required for acrosome acidification.
Direct recruitment of H+-ATPase from lysosomes for phagosomal acidification.