VMA22

UniProt ID: P38784
Organism: Saccharomyces cerevisiae
Review Status: DRAFT
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Gene Description

TODO: Add description for VMA22

Existing Annotations Review

GO Term Evidence Action Reason
GO:0051082 unfolded protein binding
IBA
GO_REF:0000033 		MARK AS OVER ANNOTATED
Summary: VMA22 is a dedicated assembly factor for the V-ATPase, not a general chaperone. GO:0051082 overstates the binding as a standalone function.
Reason: VMA22 functions as a dedicated ER-resident assembly factor for the vacuolar H+-ATPase V0 sector, not as a general unfolded protein binding chaperone. The binding interaction is specific to V-ATPase assembly and is better captured by the assembly process annotation (GO:0070072).
GO:1990871 Vma12-Vma22 assembly complex
IBA
GO_REF:0000033 		ACCEPT
Summary: Manual review: Vma12-Vma22 assembly complex is consistent with known biology of VMA22.
Reason: Retained as supported or plausible for this gene and evidence context.
GO:0070072 vacuolar proton-transporting V-type ATPase complex assembly
IEA
GO_REF:0000002 		ACCEPT
Summary: Manual review: vacuolar proton-transporting V-type ATPase complex assembly is consistent with known biology of VMA22.
Reason: Retained as supported or plausible for this gene and evidence context.
GO:0005634 nucleus
HDA
PMID:26928762
One library to make them all: streamlining the creation of y... 		ACCEPT
Summary: Manual review: nucleus is consistent with known biology of VMA22.
Reason: Retained as supported or plausible for this gene and evidence context.
GO:1990871 Vma12-Vma22 assembly complex
IPI
PMID:9660861
Assembly of the yeast vacuolar H+-ATPase occurs in the endop... 		ACCEPT
Summary: Manual review: Vma12-Vma22 assembly complex is consistent with known biology of VMA22.
Reason: Retained as supported or plausible for this gene and evidence context.
GO:0007035 vacuolar acidification
IMP
PMID:1628805
Genes required for vacuolar acidity in Saccharomyces cerevis... 		ACCEPT
Summary: Manual review: vacuolar acidification is consistent with known biology of VMA22.
Reason: Retained as supported or plausible for this gene and evidence context.
GO:0051082 unfolded protein binding
IMP
PMID:7673216
Vma22p is a novel endoplasmic reticulum-associated protein r... 		MARK AS OVER ANNOTATED
Summary: VMA22 is a dedicated assembly factor for the V-ATPase, not a general chaperone. GO:0051082 overstates the binding as a standalone function.
Reason: VMA22 functions as a dedicated ER-resident assembly factor for the vacuolar H+-ATPase V0 sector, not as a general unfolded protein binding chaperone. The binding interaction is specific to V-ATPase assembly and is better captured by the assembly process annotation (GO:0070072).
GO:0051082 unfolded protein binding
IMP
PMID:8582630
vph6 mutants of Saccharomyces cerevisiae require calcineurin... 		MARK AS OVER ANNOTATED
Summary: VMA22 is a dedicated assembly factor for the V-ATPase, not a general chaperone. GO:0051082 overstates the binding as a standalone function.
Reason: VMA22 functions as a dedicated ER-resident assembly factor for the vacuolar H+-ATPase V0 sector, not as a general unfolded protein binding chaperone. The binding interaction is specific to V-ATPase assembly and is better captured by the assembly process annotation (GO:0070072).
GO:0070072 vacuolar proton-transporting V-type ATPase complex assembly
IMP
PMID:7673216
Vma22p is a novel endoplasmic reticulum-associated protein r... 		ACCEPT
Summary: Manual review: vacuolar proton-transporting V-type ATPase complex assembly is consistent with known biology of VMA22.
Reason: Retained as supported or plausible for this gene and evidence context.

References

GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000033
Annotation inferences using phylogenetic trees
PMID:1628805
Genes required for vacuolar acidity in Saccharomyces cerevisiae.
PMID:26928762
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
PMID:7673216
Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complex.
PMID:8582630
vph6 mutants of Saccharomyces cerevisiae require calcineurin for growth and are defective in vacuolar H(+)-ATPase assembly.
PMID:9660861
Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex.

📄 View Raw YAML

 
id: P38784
gene_symbol: VMA22
product_type: PROTEIN
status: DRAFT
taxon:
  id: NCBITaxon:559292
  label: Saccharomyces cerevisiae
description: 'TODO: Add description for VMA22'
alternative_products:
- name: '1'
  id: P38784-1
- name: '2'
  id: P38784-2
  sequence_note: VSP_058123
existing_annotations:
- term:
    id: GO:0051082
    label: unfolded protein binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'VMA22 is a dedicated assembly factor for the V-ATPase, not a general chaperone. GO:0051082 overstates the binding as a standalone function.'
    action: MARK_AS_OVER_ANNOTATED
    reason: VMA22 functions as a dedicated ER-resident assembly factor for the vacuolar H+-ATPase V0 sector, not as a general unfolded protein binding chaperone. The binding interaction is specific to V-ATPase assembly and is better captured by the assembly process annotation (GO:0070072).
- term:
    id: GO:1990871
    label: Vma12-Vma22 assembly complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'Manual review: Vma12-Vma22 assembly complex is consistent with known biology of VMA22.'
    action: ACCEPT
    reason: Retained as supported or plausible for this gene and evidence context.
- term:
    id: GO:0070072
    label: vacuolar proton-transporting V-type ATPase complex assembly
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: 'Manual review: vacuolar proton-transporting V-type ATPase complex assembly is consistent with known biology of VMA22.'
    action: ACCEPT
    reason: Retained as supported or plausible for this gene and evidence context.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: HDA
  original_reference_id: PMID:26928762
  review:
    summary: 'Manual review: nucleus is consistent with known biology of VMA22.'
    action: ACCEPT
    reason: Retained as supported or plausible for this gene and evidence context.
- term:
    id: GO:1990871
    label: Vma12-Vma22 assembly complex
  evidence_type: IPI
  original_reference_id: PMID:9660861
  review:
    summary: 'Manual review: Vma12-Vma22 assembly complex is consistent with known biology of VMA22.'
    action: ACCEPT
    reason: Retained as supported or plausible for this gene and evidence context.
- term:
    id: GO:0007035
    label: vacuolar acidification
  evidence_type: IMP
  original_reference_id: PMID:1628805
  review:
    summary: 'Manual review: vacuolar acidification is consistent with known biology of VMA22.'
    action: ACCEPT
    reason: Retained as supported or plausible for this gene and evidence context.
- term:
    id: GO:0051082
    label: unfolded protein binding
  evidence_type: IMP
  original_reference_id: PMID:7673216
  review:
    summary: 'VMA22 is a dedicated assembly factor for the V-ATPase, not a general chaperone. GO:0051082 overstates the binding as a standalone function.'
    action: MARK_AS_OVER_ANNOTATED
    reason: VMA22 functions as a dedicated ER-resident assembly factor for the vacuolar H+-ATPase V0 sector, not as a general unfolded protein binding chaperone. The binding interaction is specific to V-ATPase assembly and is better captured by the assembly process annotation (GO:0070072).
- term:
    id: GO:0051082
    label: unfolded protein binding
  evidence_type: IMP
  original_reference_id: PMID:8582630
  review:
    summary: 'VMA22 is a dedicated assembly factor for the V-ATPase, not a general chaperone. GO:0051082 overstates the binding as a standalone function.'
    action: MARK_AS_OVER_ANNOTATED
    reason: VMA22 functions as a dedicated ER-resident assembly factor for the vacuolar H+-ATPase V0 sector, not as a general unfolded protein binding chaperone. The binding interaction is specific to V-ATPase assembly and is better captured by the assembly process annotation (GO:0070072).
- term:
    id: GO:0070072
    label: vacuolar proton-transporting V-type ATPase complex assembly
  evidence_type: IMP
  original_reference_id: PMID:7673216
  review:
    summary: 'Manual review: vacuolar proton-transporting V-type ATPase complex assembly is consistent with known biology of VMA22.'
    action: ACCEPT
    reason: Retained as supported or plausible for this gene and evidence context.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: PMID:1628805
  title: Genes required for vacuolar acidity in Saccharomyces cerevisiae.
  findings: []
- id: PMID:26928762
  title: 'One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.'
  findings: []
- id: PMID:7673216
  title: Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complex.
  findings: []
- id: PMID:8582630
  title: vph6 mutants of Saccharomyces cerevisiae require calcineurin for growth and are defective in vacuolar H(+)-ATPase assembly.
  findings: []
- id: PMID:9660861
  title: Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex.
  findings: []