CCT7 encodes the eta subunit of the cytosolic chaperonin-containing T-complex/TRiC. Cct7 is one of eight distinct CCT subunits in each ring of the hetero-oligomeric double-ring chaperonin and contributes ATP binding/hydrolysis and subunit-specific surfaces to the complex-level ATP-dependent protein folding chaperone activity. The mature TRiC/CCT complex folds actin, tubulin, and other cytosolic clients. Therefore, CCT7 should be curated as a core component of the cytosolic CCT complex rather than as a stand-alone generic unfolded protein binding factor.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: IBA protein folding is consistent with CCT/TRiC chaperonin function. Reason: CCT7 contributes to the ATP-dependent protein folding activity of the CCT complex. Supporting Evidence: PMID:16762366 Yeast CCT catalyses the folding of yeast ACT1p and human beta-actin. file:yeast/CCT7/CCT7-deep-research-falcon.md CCT7 encodes a TRiC/CCT subunit whose primary function is ATP-dependent folding of cytosolic client proteins. |
| GO:0005832 chaperonin-containing T-complex | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference is correct; Cct7 is a CCT/TRiC subunit. Reason: Complex membership is central to CCT7 function. Supporting Evidence: PMID:15704212 Eukaryotic chaperonins, the Cct complexes, are assembled into two rings, each of...which is composed of a stoichiometric array of eight different subunits...Cct1p-Cct8p. |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MODIFY | Summary: The term is broadly related to chaperonin function but less precise than ATP-dependent protein folding chaperone. Reason: CCT7 functions through the assembled ATP-dependent chaperonin complex rather than generic unfolded protein binding. The replacement annotation should use the contributes_to qualifier, as CCT7 is a subunit that contributes to complex-level ATP-dependent folding activity rather than having the activity independently. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:16762366 binding pre-equilibrium...followed by a faster ATP-driven processing to...native actin |
| GO:0000166 nucleotide binding | IEA GO_REF:0000043 | MODIFY | Summary: Nucleotide binding is true but overly broad for the CCT ATPase fold. Reason: ATP binding is the more specific nucleotide-binding annotation already present. Proposed replacements: ATP binding Supporting Evidence: file:yeast/CCT7/CCT7-deep-research-falcon.md TRiC subunits contain equatorial ATP-binding domains and undergo ATP-driven conformational cycling. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: ATP binding is consistent with the conserved CCT chaperonin ATPase domain. Reason: ATP binding is required for the conformational cycle of CCT/TRiC. Supporting Evidence: file:yeast/CCT7/CCT7-deep-research-falcon.md ATP binding and hydrolysis drive TRiC open/closed conformational changes. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Cytoplasmic localization is correct for the CCT/TRiC chaperonin. Reason: CCT/TRiC is the eukaryotic cytosolic chaperonin. Supporting Evidence: PMID:16762366 This purified yeast CCT was used for a novel...quantitative actin-folding assay |
| GO:0005832 chaperonin-containing T-complex | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA electronic annotation is consistent with direct complex membership evidence. Reason: CCT7 is a core subunit of the chaperonin-containing T-complex. Supporting Evidence: PMID:15704212 Cct complexes, are assembled into two rings...Cct1p-Cct8p. |
| GO:0006457 protein folding | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic protein folding annotation is consistent with experimental CCT function. Reason: CCT7 contributes to complex-level protein folding. Supporting Evidence: PMID:16762366 Yeast CCT catalyses the...folding of yeast ACT1p and human beta-actin |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: ATP hydrolysis activity is consistent with the conserved CCT chaperonin cycle. Reason: ATP hydrolysis drives the CCT/TRiC conformational cycle for client folding. Supporting Evidence: PMID:16762366 binding pre-equilibrium...followed by a faster ATP-driven processing to...native actin |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000120 | MODIFY | Summary: Broad unfolded protein binding is less precise than ATP-dependent chaperone activity. Reason: GO:0140662 better represents the CCT/TRiC complex-level function. The replacement annotation should use the contributes_to qualifier, as CCT7 is a subunit that contributes to complex-level ATP-dependent folding activity rather than having the activity independently. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:16762366 binding pre-equilibrium...followed by a faster ATP-driven processing to...native actin |
| GO:0140662 ATP-dependent protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: This is the most informative MF term for the assembled CCT/TRiC machine. Reason: CCT7 contributes to ATP-dependent protein folding chaperone activity as a complex subunit. Supporting Evidence: PMID:16762366 The eukaryotic cytosolic chaperonin CCT is an essential ATP-dependent protein folding machine. |
| GO:0006457 protein folding | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | ACCEPT | Summary: Direct biochemical evidence with purified yeast CCT supports protein folding. Reason: The purified CCT complex catalyzes actin folding in vitro. Supporting Evidence: PMID:16762366 Yeast CCT catalyses the folding of yeast ACT1p and human beta-actin with nearly identical rate constants and yields. |
| GO:0005737 cytoplasm | HDA PMID:11914276 Subcellular localization of the yeast proteome. | ACCEPT | Summary: High-throughput cytoplasmic localization is consistent with CCT/TRiC biology. Reason: CCT is a cytosolic/cytoplasmic chaperonin complex. Supporting Evidence: file:yeast/CCT7/CCT7-deep-research-falcon.md Group II TRiC/CCT is classically described as cytosolic. |
| GO:0005832 chaperonin-containing T-complex | IPI PMID:15704212 Physiological effects of unassembled chaperonin Cct subunits... | ACCEPT | Summary: Interaction evidence supports Cct7 as part of the CCT complex. Reason: CCT7 function depends on the assembled hetero-oligomeric chaperonin. Supporting Evidence: PMID:15704212 Cct complexes, are assembled into two rings...Cct1p-Cct8p. |
| GO:0005832 chaperonin-containing T-complex | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | ACCEPT | Summary: Purified yeast CCT complex evidence supports complex membership. Reason: Cct7 is one subunit of the functional yeast CCT/TRiC folding machine. Supporting Evidence: PMID:16762366 An efficient purification...protocol for CCT from Saccharomyces cerevisiae has been developed. |
| GO:0051082 unfolded protein binding | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | MODIFY | Summary: The experiment supports substrate binding during CCT-mediated folding, but the generic term is less specific. Reason: Replace with ATP-dependent protein folding chaperone to capture the CCT complex mechanism. The replacement annotation should use the contributes_to qualifier, as CCT7 is a subunit that contributes to complex-level ATP-dependent folding activity rather than having the activity independently. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:16762366 controlled CCT-actin folding assay are...consistent with a model where CCT and Ac(I) are in a binding pre-equilibrium...ATP-driven processing to...native actin |
Loading supporting content…
Download this section (compressed HTML)Q: Should CCT subunit annotations to GO:0051082 be replaced by GO:0140662 with contributes_to semantics for individual subunits?
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)