Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis.
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ATP6V1C2 was cloned as a novel tissue-specific isoform of the human V-ATPase C subunit; reported as kidney- and placenta-enriched.
"Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits"
Integral and associated lysosomal membrane proteins.
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ATP6V1C2 was detected among V-ATPase polypeptides in purified placental lysosomal membrane fractions.
"In membranes purified from placental lysosomes, we identified 58 proteins, known to reside at least partially in the lysosomal membrane. These included 17 polypeptides comprising or associated with the vacuolar adenosine triphosphatase."
Large-scale proteomics and phosphoproteomics of urinary exosomes.
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ATP6V1C2 detected in a bulk urinary-exosome proteome (1132 proteins); likely reflects endolysosomal/MVB membrane content rather than a primary exosomal function.
"we used LC-MS/MS to profile the proteome of human urinary exosomes. Overall, the analysis identified 1132 proteins unambiguously"
Requirement of prorenin receptor and vacuolar H+-ATPase-mediated acidification for Wnt signaling.
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PRR (ATP6AP2) acts as an adaptor between Wnt receptors and the V-ATPase; PRR and V-ATPase acidification are required for Wnt signaling. The role is a general V-ATPase requirement, not C2-specific.
"PRR functions in a renin-independent manner as an adaptor between Wnt receptors and the vacuolar H+-adenosine triphosphatase (V-ATPase) complex. Moreover, PRR and V-ATPase were required to mediate Wnt signaling"
Expression, purification and characterization of isoforms of peripheral stalk subunits of human V-ATPase.
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Human V-ATPase peripheral stalk subunit isoforms, including C2, were expressed and purified in a cell-free system; no C2 self-association is demonstrated.
"we expressed and purified the isoforms of human V-ATPase peripheral stalk subunits using Escherichia coli cell-free protein synthesis system: E1, E2, G1, G2, G3, C1, C2, H and N-terminal soluble part of a1 and a2 isoforms"
Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts.
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The lipofuscin study does not examine ATP6V1C2; the macroautophagy link is indirect via V-ATPase-dependent lysosomal acidification.
"both the autophagosomes and the lysosomal system are not mandatory for the formation of lipofuscin"
Intraphagosomal pH is lowered to 5 by V-ATPase
Acidification of Tf:TfR1 containing endosome
RRAGC,D exchanges GTP for GDP
RRAGA,B exchanges GDP for GTP
v-ATPase:Ragulator:RRAGA,B:GTP:RRAGC,D:GDP:SLC38A9:Arginine dissociates yielding v-ATPase:Ragulator:RRAGA,B:GTP:RRAGC,D:GDP and SLC38A9:Arginine
v-ATPase:Ragulator:RagA,B:GDP:RagC,D:GDP binds SLC38A9:Arginine
v-ATPase:Ragulator:RRAGA,B:GTP:RRAGC,D:GDP binds mTORC1
UniProtKB entry for ATP6V1C2 (Q8NEY4)
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Subunit C is necessary for assembly of the catalytic V1 sector and likely has a specific function in V-ATPase catalytic activity.
"Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity"
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ATP6V1C2 expression is kidney- and placenta-enriched.
"Kidney and placenta."