Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Mutations in the X-linked ATP6AP2 cause a glycosylation disorder with autophagic defects.
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Human disease variants, mouse liver defects, fly phenotypes and human-cell partner interactions jointly support ATP6AP2 involvement in V-ATPase biogenesis; these are distinct experimental contexts.
"Our results suggest that ATP6AP2 has a crucial role in V-ATPase assembly, both in invertebrates and vertebrates."
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ATP6AP2 interacts with V0 assembly factors including ATP6AP1 and VMA21.
"Together, these results suggest that ATP6AP2 forms a complex with other V-ATPase assembly factors"
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Fly ATP6AP2L98S mutant fat-body clones show reduced acidotropic staining, providing model-specific evidence of impaired organelle acidification.
"ATP6AP2L98S mutant clones showed a reduction in Lysotracker-positive organelles compared with the WT surrounding tissue, indicating reduced acidity"
ATP6AP2 variant impairs CNS development and neuronal survival to cause fulminant neurodegeneration.
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ATP6AP2 deficiency impairs lysosomal acidification, protein degradation, and V-ATPase membrane assembly in neuronal disease models.
"severe deficiency in lysosomal acidification and
protein degradation leading to neuronal cell death"
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The authors conclude ATP6AP2 mediates V-ATPase-dependent signaling and protein degradation in the developing CNS.
"ATP6AP2 is a key mediator of
V-ATPase-dependent signaling and protein degradation in the developing human
central nervous system."
Interaction between PHB2 and Enterovirus A71 VP1 Induces Autophagy and Affects EV-A71 Infection.
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ATP6AP2 knockdown increases lysosomal pH and inhibits autolysosomal degradation in a viral autophagy model.
"To evaluate the effect of ATP6AP2 knockdown on lysosomal pH, we employed an acidophilic fluorescent probe to measure the lysosomal pH, which increased significantly"
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The paper cites an assembly role for ATP6AP2 as background; its direct ATP6AP2 experiments measure depletion-associated lysosomal pH and viral/autophagy outcomes.
"ATP6AP2 is an important auxiliary component of the V-ATPase complex and coordinates correct V-ATPase assembly"
Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.
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Human V-ATPases are ATP-driven proton pumps responsible for organelle and vesicle acidification.
"Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-driven
proton pumps comprised of a cytoplasmic V1 complex for ATP hydrolysis and a
membrane-embedded Vo complex for proton transfer."
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 complex.
"PRR functions in a renin-independent manner as an adaptor
between Wnt receptors and the vacuolar H+-adenosine triphosphatase (V-ATPase)
complex."
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The study reports PRR/V-ATPase-dependent Wnt signaling during Xenopus neural patterning; the phenotype is distinct from human-cell Wnt reporter assays.
"PRR and V-ATPase were required to mediate Wnt signaling
during antero-posterior patterning of Xenopus early central nervous system"
TMEM9 promotes intestinal tumorigenesis through vacuolar-ATPase-activated Wnt/β-catenin signalling.
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TMEM9/V-ATPase assembly and vesicular acidification provide additional support for the Wnt-acidification connection.
"TMEM9 binds to and facilitates assembly of
vacuolar-ATPase (v-ATPase), a vacuolar proton pump, resulting in enhanced
vesicular acidification and trafficking."
Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin.
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ATP6AP2 is a renin/prorenin receptor that binds renin/prorenin, increases angiotensinogen conversion, and activates ERK1/2.
"Transfected cells stably expressing the receptor showed renin- and
prorenin-specific binding."
A unique exonic splice enhancer mutation in a family with X-linked mental retardation and epilepsy points to a novel role of the renin receptor.
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A splice-affecting ATP6AP2 variant supports a role in brain development while preserving renin binding/catalytic enhancement.
"indicate a novel specific role for the renin receptor in cognitive functions and
brain development."
Renin increases mesangial cell transforming growth factor-beta1 and matrix proteins through receptor-mediated, angiotensin II-independent mechanisms.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
A reference map of the human binary protein interactome.
Multimodal cell maps as a foundation for structural and functional genomics.
Structure and Roles of V-type ATPases.
Renin:Prorenin Receptor hydrolyzes Angiotensinogen to AGT(25-34) (Angiotensin-(1-10))
Prorenin:Prorenin Receptor hydrolyzes Angiotensinogen to AGT(25-35) (Angiotensin-(1-10))
Exocytosis of tertiary granule membrane proteins
Exocytosis of ficolin-rich granule membrane proteins
UniProt record for human ATP6AP2
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UniProt summarizes ATP6AP2 as a multifunctional renin/prorenin receptor and V-ATPase accessory protein involved in endolysosomal acidification.
"Multifunctional protein which functions as a renin, prorenin
CC cellular receptor and is involved in the assembly of the lysosomal
CC proton-transporting V-type ATPase (V-ATPase) and the acidification of
CC the endo-lysosomal system"
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UniProt records ATP6AP2 as an accessory component of the multisubunit V-ATPase pump.
"Accessory component of
CC the multisubunit proton-transporting vacuolar (V)-ATPase protein pump"