ATP6V0A2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0016471 vacuolar proton-transporting V-type ATPase complex	IBA GO_REF:0000033	ACCEPT	Summary: ATP6V0A2 encodes the a2 isoform of the V0 membrane sector of the V-ATPase. Complex membership is a core cellular-component annotation supported by UniProt curation and human V-ATPase structural literature. Reason: The annotation correctly places ATP6V0A2 in the vacuolar proton-transporting V-type ATPase complex. The protein is a V0 a-subunit of a multisubunit proton pump, and the V0 sector is the membrane proton-translocation module of the complex. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase PMID:33065002 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.
GO:0046961 proton-transporting ATPase activity, rotational mechanism	IBA GO_REF:0000033	ACCEPT	Summary: ATP6V0A2 contributes to the rotational V-ATPase proton-pumping activity as a V0 membrane-sector subunit, but does not independently hydrolyze ATP outside the assembled complex. Reason: The contributes_to qualifier is appropriate for a subunit of the V-ATPase complex. The complex couples ATP hydrolysis in V1 to proton transfer through V0, and ATP6V0A2 is a V0 a-subunit. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase PMID:33065002 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.
GO:0005886 plasma membrane	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Plasma-membrane localization is plausible for V-ATPase a-subunits in some cell contexts, but ATP6V0A2 is better established in endosomal, Golgi, and lysosomal/vesicular membranes. Reason: UniProt includes cell-membrane localization and the GOA contains HPA plasma-membrane evidence, so the annotation is not rejected. It should not be treated as the main proteostasis-relevant location for ATP6V0A2, whose strongest mechanistic evidence is in intracellular acidic compartments. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Cell membrane; Multi-pass membrane protein. PMID:16415858 The a2-isoform is targeted to early endosomes
GO:0007035 vacuolar acidification	IBA GO_REF:0000033	ACCEPT	Summary: Vacuolar acidification is a correct broad biological-process annotation for ATP6V0A2 as a V-ATPase V0 subunit involved in acidification of acidic intracellular compartments. Reason: The term captures the core acidification role of the V-ATPase. For the PN batch, lysosomal lumen acidification is added separately as a more specific supported annotation, but the existing broad annotation remains biologically sound. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments PMID:32001091 V-ATPases are the primary source of organellar acidification in all eukaryotes PMID:33065002 organellar V-ATPases are essential in establishing and maintaining the pH
GO:0051117 ATPase binding	IBA GO_REF:0000033	MARK AS OVER ANNOTATED	Summary: ATPase binding is much less informative than the complex-membership and contributes_to V-ATPase activity annotations already present for ATP6V0A2. Reason: ATP6V0A2 functions as an integral V0-sector subunit. Treating ATPase binding as a gene-level molecular function risks reducing complex assembly/participation to a vague binding annotation; the more informative annotations are V-ATPase complex/V0-domain membership and contribution to proton-pumping ATPase activity. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase PMID:33065002 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.
GO:0000220 vacuolar proton-transporting V-type ATPase, V0 domain	IEA GO_REF:0000002	ACCEPT	Summary: The vacuolar V-ATPase V0-domain annotation matches ATP6V0A2 family/domain evidence and its role as an integral membrane V0 a-subunit. Reason: ATP6V0A2 is a member of the V-ATPase 116 kDa subunit family and is curated as a V0-complex subunit. The broader V0-domain annotation is correct; the PN-derived lysosomal V0-domain annotation is added separately where lysosomal localization is supported. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Belongs to the V-ATPase 116 kDa subunit family.
GO:0005886 plasma membrane	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: Plasma-membrane localization is supported by UniProt/HPA-derived evidence but is secondary to the intracellular organelle acidification role. Reason: The location is plausible and appears in curated resources, but the literature most directly supporting ATP6V0A2 function emphasizes early endosomes, Golgi function, and endolysosomal acidification rather than a primary plasma-membrane role. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Cell membrane; Multi-pass membrane protein. PMID:16415858 The a2-isoform is targeted to early endosomes
GO:0010008 endosome membrane	IEA GO_REF:0000044	ACCEPT	Summary: ATP6V0A2 is well supported at the endosome membrane, especially early endosomes, where a2-containing V-ATPase contributes to pH sensing and endocytic trafficking. Reason: The UniProt-derived IEA annotation is consistent with direct literature showing the a2 isoform is targeted to early endosomes and participates in intra-endosomal acidification-dependent ARNO recruitment and endocytic trafficking. Supporting Evidence: PMID:16415858 The a2-isoform is targeted to early endosomes PMID:16415858 interacts with ARNO in an intra-endosomal acidification-dependent manner file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Essential component of the endosomal pH-sensing machinery
GO:0033179 proton-transporting V-type ATPase, V0 domain	IEA GO_REF:0000120	ACCEPT	Summary: The V0-domain annotation is a core cellular-component annotation for ATP6V0A2. Reason: ATP6V0A2 is the a2 isoform of the V-ATPase 116 kDa a-subunit and belongs to the V0 membrane proton-transfer sector. This term is already aligned with the PN V0 component projection, although PN also supports a lysosomal-specific child term. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase PMID:33065002 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.
GO:0046961 proton-transporting ATPase activity, rotational mechanism	IEA GO_REF:0000002	MODIFY	Summary: The V-ATPase rotational proton-pump activity is correct for the assembled ATP6V0A2-containing complex. ATP6V0A2 should be interpreted as contributing to this activity as a V0 subunit rather than acting as an independent ATPase. Reason: The term is biologically appropriate for ATP6V0A2-containing V-ATPase complexes, but the GOA qualifier should be changed from enables to contributes_to. The contributes_to IBA qualifier is the clearest representation of a single V0 subunit's contribution to the assembled proton pump. Proposed replacements: proton-transporting ATPase activity, rotational mechanism Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase PMID:33065002 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.
GO:1902600 proton transmembrane transport	IEA GO_REF:0000002	ACCEPT	Summary: ATP6V0A2 participates in proton transmembrane transport as part of the V-ATPase proton-translocation machinery. Reason: The V0 sector transfers protons across organelle membranes as part of the V-ATPase. ATP6V0A2 is a V0 a-subunit in this machinery, so the process annotation is appropriate. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments PMID:33065002 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.
GO:0005515 protein binding	IPI PMID:16415858 V-ATPase interacts with ARNO and Arf6 in early endosomes and...	REMOVE	Summary: PMID:16415858 supports a specific ARNO interaction with the a2 isoform, but GO:0005515 protein binding is too generic to retain as useful functional annotation. Reason: The interaction evidence is real, but generic protein binding is uninformative and is explicitly discouraged in this review workflow. The functional meaning of the interaction is better captured in the review text as endosomal pH-sensing/trafficking, not as GO:0005515. Supporting Evidence: PMID:16415858 interacts with ARNO in an intra-endosomal acidification-dependent manner PMID:16415858 Inhibition of endosomal acidification abrogates protein trafficking between
GO:0001669 acrosomal vesicle	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Acrosomal-vesicle localization is plausible by orthology for V-ATPase a-subunits but is not part of the core ATP6V0A2 proteostasis role reviewed here. Reason: The annotation comes from Ensembl orthology transfer rather than direct ATP6V0A2 literature in this review. It is retained as a possible specialized reproductive-cell location, but the main supported locations are endosome, Golgi, lysosomal, and other acidic-vesicle membranes. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO:0015078 proton transmembrane transporter activity	IEA GO_REF:0000107	ACCEPT	Summary: ATP6V0A2 contributes to proton transmembrane transporter activity as a V0 membrane-sector component of the assembled V-ATPase. Reason: The contributes_to qualifier is appropriate for ATP6V0A2 because proton translocation is performed by the assembled V-ATPase/V0 machinery rather than by the isolated subunit. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase PMID:33065002 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.
GO:0033176 proton-transporting V-type ATPase complex	IEA GO_REF:0000107	ACCEPT	Summary: The broader proton-transporting V-type ATPase complex annotation is correct for ATP6V0A2. Reason: ATP6V0A2 is an integral V0-sector subunit of the V-ATPase. The annotation is less specific than the V0-domain annotations but remains valid complex membership. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase PMID:33065002 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.
GO:0048471 perinuclear region of cytoplasm	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Perinuclear-region localization is compatible with Golgi/endosomal distribution but is not the most informative cellular-component annotation for ATP6V0A2. Reason: The annotation is retained as a broad localization transferred by Ensembl, but more precise experimentally supported locations include endosome membrane, Golgi membrane, and lysosomal membrane. Supporting Evidence: PMID:16415858 The a2-isoform is targeted to early endosomes file:human/ATP6V0A2/ATP6V0A2-uniprot.txt May play a role in maintaining the Golgi functions
GO:0005886 plasma membrane	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: HPA reports ATP6V0A2 at the plasma membrane, but this is a secondary location relative to intracellular acidic compartments. Reason: The IDA evidence supports retaining the localization, but the core functional literature for ATP6V0A2 centers on endosomal/Golgi/lysosomal acidification and V-ATPase complex function. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO:0000139 Golgi membrane	NAS PMID:32001091 Structure and Roles of V-type ATPases.	ACCEPT	Summary: Golgi membrane localization is consistent with ATP6V0A2 disease biology and Golgi acidification/glycosylation functions. Reason: ATP6V0A2 is implicated in maintaining Golgi pH-dependent functions, including glycosylation maturation. ComplexPortal and review evidence support Golgi-membrane assignment for the ATP6V0A2-containing V-ATPase variant. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH PMID:32001091 V-ATPases are the primary source of organellar acidification in all eukaryotes
GO:0033176 proton-transporting V-type ATPase complex	NAS PMID:33065002 Structures of a Complete Human V-ATPase Reveal Mechanisms of...	ACCEPT	Summary: Human V-ATPase structural literature supports ATP6V0A2 as part of a proton-transporting V-type ATPase complex. Reason: The annotation captures the assembled complex in which ATP6V0A2 acts. Human V-ATPase structures define a V1 ATP-hydrolysis complex and a Vo proton-transfer complex. Supporting Evidence: PMID:33065002 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. file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase
GO:0061795 Golgi lumen acidification	NAS PMID:32001091 Structure and Roles of V-type ATPases.	ACCEPT	Summary: Golgi lumen acidification is a supported ATP6V0A2-associated process and explains the glycosylation defects seen when ATP6V0A2 is disrupted. Reason: UniProt and review evidence support ATP6V0A2 involvement in Golgi pH control and glycosylation maturation. This is a meaningful organelle-specific acidification annotation, not merely a broad proteostasis projection. Supporting Evidence: file:human/ATP6V0A2/ATP6V0A2-uniprot.txt May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH PMID:32001091 V-ATPases are the primary source of organellar acidification in all eukaryotes
GO:1902600 proton transmembrane transport	NAS PMID:33065002 Structures of a Complete Human V-ATPase Reveal Mechanisms of...	ACCEPT	Summary: Proton transmembrane transport is the fundamental transport process mediated by the assembled V-ATPase containing ATP6V0A2. Reason: The human V-ATPase is an ATP-driven proton pump with a Vo membrane complex for proton transfer, and ATP6V0A2 is one of the Vo a-subunits. Supporting Evidence: PMID:33065002 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. file:human/ATP6V0A2/ATP6V0A2-uniprot.txt V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments
GO:0006879 intracellular iron ion homeostasis	IMP PMID:28296633 The vacuolar-ATPase complex and assembly factors, TMEM199 an...	KEEP AS NON CORE	Summary: ATP6V0A2 disruption was identified in a V-ATPase/HIF screen, and the study supports a non-core role for V-ATPase function in intracellular iron availability and HIF prolyl hydroxylation. Reason: The evidence is direct enough to retain the annotation, but intracellular iron homeostasis is downstream of the core V-ATPase acidification role rather than the primary evolved function of ATP6V0A2. Supporting Evidence: PMID:28296633 ATP6AP1, ATP6V1A, ATP6V1G1, ATP6V0A2 and ATP6V0D1 PMID:28296633 disrupting the V-ATPase results in intracellular iron depletion
GO:0036295 cellular response to increased oxygen levels	IMP PMID:28296633 The vacuolar-ATPase complex and assembly factors, TMEM199 an...	MARK AS OVER ANNOTATED	Summary: The PMID:28296633 evidence supports V-ATPase effects on HIF stability under aerobic conditions through iron/PHD activity, but the GO term frames this too broadly as a response to increased oxygen levels. Reason: ATP6V0A2 depletion affects HIF1A regulation indirectly through V-ATPase-dependent iron homeostasis. The paper explicitly argues against a lysosomal-degradation mechanism and focuses on PHD activity; the broad oxygen-response term should not be treated as a core ATP6V0A2 function. Supporting Evidence: PMID:28296633 ATP6AP1, ATP6V1A, ATP6V1G1, ATP6V0A2 and ATP6V0D1 PMID:28296633 disrupting the V-ATPase results in intracellular iron depletion PMID:28296633 Rather than preventing the lysosomal degradation of HIF1α, the V-ATPase inhibition stabilised HIF1α by decreasing PHD enzymatic activity.
GO:0016241 regulation of macroautophagy	NAS PMID:22982048 Lipofuscin is formed independently of macroautophagy and lys...	MARK AS OVER ANNOTATED	Summary: The macroautophagy annotation is too broad for ATP6V0A2. V-ATPase acidification supports lysosomal degradation/autophagic flux, but PMID:22982048 does not establish ATP6V0A2 as a specific regulator of macroautophagy. Reason: The supporting paper discusses lipofuscin, autophagy, and lysosomal activity rather than ATP6V0A2-specific regulation of macroautophagy. For the PN batch, ATP6V0A2 should be represented by lysosomal acidification/V-ATPase component terms, not by a generic macroautophagy regulation term. Supporting Evidence: PMID:22982048 both the autophagosomes and the lysosomal system are not mandatory
GO:0005765 lysosomal membrane	HDA PMID:17897319 Integral and associated lysosomal membrane proteins.	ACCEPT	Summary: Lysosomal membrane localization is supported by lysosomal membrane proteomics and is important for the PN lysosomal V-ATPase projection. Reason: ATP6V0A2 is part of the V-ATPase system, and lysosomal membrane proteomics detected vacuolar ATPase-associated polypeptides in purified lysosomal membranes. This supports retaining the lysosomal membrane annotation and adding lysosomal V0-domain specificity. Supporting Evidence: PMID:17897319 17 polypeptides comprising or associated with the vacuolar adenosine file:human/ATP6V0A2/ATP6V0A2-deep-research-manual.md Both projected terms are accepted conservatively in the review because they are supported by ATP6V0A2 V0-subunit identity, lysosomal membrane evidence, and the broader human V-ATPase endosome/lysosome acidification literature. file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase
GO:0030670 phagocytic vesicle membrane	TAS Reactome:R-HSA-1222516	KEEP AS NON CORE	Summary: Phagocytic vesicle membrane localization is supported by Reactome V-ATPase phagosome acidification context but is a context-specific location rather than ATP6V0A2 core identity. Reason: The V-ATPase acidifies phagosomes, but ATP6V0A2-specific evidence is indirect through Reactome complex membership. Retain as a specialized acidic-vesicle context, not as a main gene function. Supporting Evidence: Reactome:R-HSA-1222516 movement of three protons into the phagosome
GO:0010008 endosome membrane	TAS Reactome:R-HSA-5252133	ACCEPT	Summary: Reactome places ATP6V0A2-containing V-ATPase context at endosome membranes during ATP6AP1/V-ATPase binding and acidification-related events. Reason: Endosome membrane localization is well supported by both primary literature and Reactome event context; ATP6V0A2 is targeted to early endosomes and participates in pH-dependent trafficking. Supporting Evidence: Reactome:R-HSA-5252133 Vacuolar-type H+-ATPases (V-ATPases) are proton pumps that acidify intracellular cargos PMID:16415858 The a2-isoform is targeted to early endosomes
GO:0010008 endosome membrane	TAS Reactome:R-HSA-74723	ACCEPT	Summary: Endosome membrane localization is supported by the Reactome endosome acidification event and direct early-endosome literature for the a2 isoform. Reason: The annotation matches ATP6V0A2 involvement in endosomal acidification and pH-dependent endocytic trafficking. Supporting Evidence: Reactome:R-HSA-74723 The effect of the proton pump is to allow entry of [H+] ions into the lumen of the endosome. PMID:16415858 The a2-isoform is targeted to early endosomes PMID:16415858 Inhibition of endosomal acidification abrogates protein trafficking between
GO:0010008 endosome membrane	TAS Reactome:R-HSA-917841	ACCEPT	Summary: Endosome membrane localization is supported by Reactome transferrin-receptor endosome acidification context and by direct literature on the a2 isoform in early endosomes. Reason: ATP6V0A2-containing V-ATPase participates in acidifying endosomal compartments, including transferrin-receptor recycling/endosome contexts in Reactome. Supporting Evidence: Reactome:R-HSA-917841 When pumping, ATP hydrolysis drives a 120 degree rotation of the rotor which leads to movement of three protons PMID:16415858 The a2-isoform is targeted to early endosomes
GO:0006955 immune response	TAS PMID:2247090 Cloning of a cDNA for a T cell produced molecule with a puta...	MARK AS OVER ANNOTATED	Summary: The old immune-response annotation is not a precise ATP6V0A2 functional annotation. The cited cloning paper reports a putative immune regulatory protein but does not establish the modern V-ATPase a2 mechanism as immune response. Reason: ATP6V0A2/V-ATPase activity can affect immune-cell and MHC degradation contexts indirectly, but GO:0006955 is too broad and weakly supported by PMID:2247090 for this gene. It should not be considered a core proteostasis annotation. Supporting Evidence: PMID:2247090 putative immune regulatory role file:human/ATP6V0A2/ATP6V0A2-uniprot.txt the in vivo relevance of this observation needs to be confirmed
GO:0007042 lysosomal lumen acidification	NAS PMID:33065002 Structures of a Complete Human V-ATPase Reveal Mechanisms of...	NEW	Summary: The PN projection proposes lysosomal lumen acidification as a more specific term than existing vacuolar acidification. This is accepted conservatively because ATP6V0A2 is a V0 V-ATPase subunit with lysosomal membrane evidence and broad human V-ATPase evidence for endosome/lysosome pH homeostasis. Reason: The PN source node is manually mapped to lysosomal lumen acidification and the gene is one of the V0 lysosomal V-ATPase pump components in the projection. Independent literature supports V-ATPase-dependent pH homeostasis of endosomes and lysosomes, and ATP6V0A2 has lysosomal membrane support. The annotation is added as a specific lysosomal acidification term, while broader autophagy/process claims are not promoted. Supporting Evidence: file:projects/PROTEOSTASIS/reports/pn_projection/pn_projected_annotations.tsv ATP6V0A2 Autophagy-Lysosome Pathway\|Lysosomal catabolism\|Regulation of lysosomal environment\|Lysosomal acidification\|V0 lysosomal v-ATPase proton pump component PMID:33065002 organellar V-ATPases are essential in establishing and maintaining the pH PMID:17897319 17 polypeptides comprising or associated with the vacuolar adenosine file:human/ATP6V0A2/ATP6V0A2-deep-research-manual.md Both projected terms are accepted conservatively in the review because they are supported by ATP6V0A2 V0-subunit identity, lysosomal membrane evidence, and the broader human V-ATPase endosome/lysosome acidification literature.
GO:0046610 lysosomal proton-transporting V-type ATPase, V0 domain	NAS PMID:33065002 Structures of a Complete Human V-ATPase Reveal Mechanisms of...	NEW	Summary: The PN projection proposes the lysosomal V0-domain component term. This is accepted because ATP6V0A2 is a V0 a-subunit, GOA already supports V0-domain membership, and lysosomal membrane evidence supports the lysosomal-specific component term. Reason: The existing GOA captures the broader V0 domain but lacks the lysosomal V0-domain component term. PN mapping and gene-level evidence together support the lysosomal-specific child term without requiring any broader autophagy-process assertion. Supporting Evidence: file:projects/PROTEOSTASIS/reports/pn_projection/pn_projected_annotations.tsv GO:0046610 lysosomal proton-transporting V-type ATPase, V0 domain file:human/ATP6V0A2/ATP6V0A2-uniprot.txt Subunit of the V0 complex of vacuolar(H+)-ATPase PMID:17897319 17 polypeptides comprising or associated with the vacuolar adenosine

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