ATP11 encodes a mitochondrial matrix assembly factor for the F1 sector of mitochondrial F1FO ATP synthase. Atp11 is not a stoichiometric ATP synthase subunit; it is a dedicated assembly chaperone/stabilizing factor for the unassembled F1 beta subunit Atp2, preventing nonproductive aggregation and promoting formation of the alpha3-beta3 catalytic F1 head. In vitro, Atp11 also displays general holdase activity, suppressing aggregation of a non-client surrogate substrate (reduced insulin) in addition to its natural F1 beta client.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: IBA mitochondrial localization is consistent with direct ATP11 localization. Reason: Atp11 functions in mitochondria, specifically the matrix. Supporting Evidence: PMID:1532796 vitro import assays of ATP11 precursor and immunochemical evidence indicate that...the protein is located in mitochondria. file:interpro/panther/PTHR13126/PTHR13126-metadata.yaml accession: PTHR13126...name: CHAPERONE ATP11 |
| GO:0140777 protein-containing complex stabilizing activity | IBA GO_REF:0000033 | ACCEPT | Summary: This is the most specific molecular-function term for Atp11. Reason: Atp11 stabilizes the unassembled F1 beta subunit during ATP synthase assembly. Supporting Evidence: PMID:10681564 evidence that Atp11p binds selectively to the beta-subunit of F(1). PMID:12829692 Atp11p yields a subfragment of the protein (called Atp11pTRNC) that retains...molecular chaperone function...the natural substrate (F1 beta). file:yeast/ATP11/ATP11-deep-research-falcon.md that binds the...F1 Ξ² subunit (Atp2)...to prevent its nonproductive self-association |
| GO:0033615 mitochondrial proton-transporting ATP synthase complex assembly | IBA GO_REF:0000033 | ACCEPT | Summary: The IBA process term matches classic ATP11 mutant and biochemical evidence. Reason: ATP synthase F1 assembly is the central process affected by ATP11. Supporting Evidence: PMID:2142305 explanation for the mutant phenotype is a block in the assembly of the F1...oligomer. PMID:36596815 it cooperates with the assembly...factors Atp11 and Atp12 to form the F1 domain of the ATP synthase. |
| GO:0005739 mitochondrion | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic mitochondrion annotation is correct. Reason: Atp11 is a mitochondrial matrix assembly factor. Supporting Evidence: PMID:1532796 The hybrid protein is detected in mitochondria with antibodies |
| GO:0065003 protein-containing complex assembly | IEA GO_REF:0000002 | MODIFY | Summary: The term is correct but too broad. Reason: Replace with the specific mitochondrial ATP synthase assembly term. Proposed replacements: mitochondrial proton-transporting ATP synthase complex assembly Supporting Evidence: PMID:2142305 important function at a...late stage in the synthesis of F1 |
| GO:0005515 protein binding | IPI PMID:27107014 An inter-species protein-protein interaction network across ... | REMOVE | Summary: This comes from a yeast-human inter-species interaction map and is not a physiological ATP11 function. Reason: The annotation does not identify the endogenous yeast Atp2/F1 beta client and uses an uninformative term. Supporting Evidence: PMID:27107014 systematically probed the yeast and human proteomes for interactions between...proteins from these two species |
| GO:0005759 mitochondrial matrix | IDA PMID:1532796 Characterization of ATP11 and detection of the encoded prote... | ACCEPT | Summary: Direct evidence supports mitochondrial matrix localization. Reason: The F1 ATP synthase assembly role occurs in the matrix; PMID:1532796 detects Atp11 in mitochondria and reports co-purification with F1 alpha and beta subunits, which makes the matrix inference explicit. Supporting Evidence: PMID:1532796 Biotinated ATP11 protein can be partially...purified by affinity chromatography PMID:1532796 biotinated ATP11 protein also contains the alpha and beta subunits of F1-ATPase |
| GO:0033615 mitochondrial proton-transporting ATP synthase complex assembly | IMP PMID:36596815 The mitochondrial Hsp70 controls the assembly of the F(1)F(O... | ACCEPT | Summary: Recent work places Atp11 with Atp12 and mtHsp70 in F1 assembly. Reason: This is the specific ATP synthase assembly process affected by Atp11. Supporting Evidence: PMID:36596815 it cooperates with the assembly...factors Atp11 and Atp12 to form the F1 domain of the ATP synthase. |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | ACCEPT | Summary: High-throughput mitochondrial proteomics is consistent with ATP11 biology. Reason: Mitochondrial localization is core to Atp11 function. Supporting Evidence: PMID:24769239 isolated mitochondria extracted from yeast grown on fermentative...and respiratory...media |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: High-throughput mitochondrial proteome data are consistent with direct localization. Reason: The broad mitochondrion term is correct. Supporting Evidence: PMID:16823961 A total of 851 different proteins (PROMITO dataset) were...identified by use of multidimensional LC-MS/MS |
| GO:0051082 unfolded protein binding | IDA PMID:10681564 The assembly factor Atp11p binds to the beta-subunit of the ... | KEEP AS NON CORE | Summary: Atp11 binds the unassembled, non-native F1 beta subunit, which is genuine unfolded protein binding but is secondary to its client-specific assembly-chaperone role. Reason: Binding to the nucleotide-binding domain of unassembled F1 beta is a well-grounded IDA that should be demoted rather than discarded; the companion holdase assay in PMID:12829692 shows the activity extends to a non-client surrogate substrate, so it is not fully captured by GO:0140777. This matches the gene-specific determination recorded in projects/UNFOLDED_PROTEIN_BINDING.md, which lists ATP11 as NON_CORE for unfolded protein binding. GO:0140777 remains the core molecular function. Supporting Evidence: PMID:10681564 Atp11p bound to a region of the nucleotide-binding...domain of the beta-subunit |
| GO:0033615 mitochondrial proton-transporting ATP synthase complex assembly | IPI PMID:10681564 The assembly factor Atp11p binds to the beta-subunit of the ... | ACCEPT | Summary: The Atp11-F1 beta interaction directly supports ATP synthase F1 assembly. Reason: This is the correct process-level interpretation of the Atp11-Atp2 interaction. Supporting Evidence: PMID:10681564 alpha-subunits may exchange for bound Atp11p...during the process of F(1) assembly. |
| GO:0005739 mitochondrion | IDA PMID:1532796 Characterization of ATP11 and detection of the encoded prote... | ACCEPT | Summary: Direct evidence places Atp11 in mitochondria. Reason: Mitochondrial localization is required for ATP synthase F1 assembly. Supporting Evidence: PMID:1532796 vitro import assays of ATP11 precursor and immunochemical evidence indicate that...the protein is located in mitochondria. |
| GO:0007005 mitochondrion organization | IMP PMID:2142305 Identification of two nuclear genes (ATP11, ATP12) required ... | MODIFY | Summary: This broad phenotype should be replaced by the specific F1 ATP synthase assembly defect. Reason: ATP11 mutants block F1 assembly, not general mitochondrial organization as a primary function. Proposed replacements: mitochondrial proton-transporting ATP synthase complex assembly Supporting Evidence: PMID:2142305 important function at a...late stage in the synthesis of F1 |
| GO:0033615 mitochondrial proton-transporting ATP synthase complex assembly | IMP PMID:2142305 Identification of two nuclear genes (ATP11, ATP12) required ... | ACCEPT | Summary: Classic genetic evidence directly supports ATP synthase assembly. Reason: ATP11 was identified as required for assembly of yeast F1-ATPase. Supporting Evidence: PMID:2142305 explanation for the mutant phenotype is a block in the assembly of the F1...oligomer. |
| GO:0051082 unfolded protein binding | IDA PMID:12829692 A purified subfragment of yeast Atp11p retains full molecula... | KEEP AS NON CORE | Summary: Atp11 suppresses aggregation of reduced insulin, a non-client surrogate substrate, which is genuine unfolded protein binding beyond client-specific F1 stabilization. Reason: This IDA rests on the canonical holdase assay with a surrogate substrate (reduced insulin) as well as the natural F1 beta client, so it is not captured by GO:0140777 and should be demoted rather than replaced. This matches the gene-specific determination recorded in projects/UNFOLDED_PROTEIN_BINDING.md, which lists ATP11 as NON_CORE for unfolded protein binding. The core function remains client-specific stabilization of the F1 assembly intermediate. Supporting Evidence: PMID:12829692 Atp11p yields a subfragment of the protein (called Atp11pTRNC) that retains...molecular chaperone function...the natural substrate (F1 beta). |
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