CCT5 encodes the epsilon subunit of the cytosolic group II chaperonin TRiC/CCT. Cct5 is an obligate subunit of the ATP-driven double-ring folding machine, contributes one ATPase/substrate-contact module to the chamber, and is best curated as part of the complex that folds actin, tubulin, and other cytosolic clients. The subunit-specific literature emphasizes ATP-cycle asymmetry and chamber architecture rather than a separate standalone activity.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: CCT5 participates in protein folding as an obligate subunit of TRiC/CCT, the cytosolic chaperonin that folds actin, tubulin, and other clients. Reason: Protein folding is the correct biological-process context for the chaperonin complex, supported by direct yeast CCT actin-folding assays and PANTHER/InterPro family evidence. Supporting Evidence: file:yeast/CCT5/CCT5-deep-research-falcon.md CCT5 is best defined as a **structural and catalytic component** |
| GO:0005832 chaperonin-containing T-complex | IBA GO_REF:0000033 | ACCEPT | Summary: CCT5 is a named subunit of the chaperonin-containing T-complex. Reason: Complex membership is central to the gene product function and is supported by yeast CCT complex literature and family evidence. |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MODIFY | Summary: unfolded protein binding reflects substrate engagement by TRiC/CCT, but it is less informative than the ATP-dependent folding chaperone function of the complex. Reason: Replace generic substrate-binding language with the specific chaperonin activity supported by yeast CCT actin-folding assays and domain evidence. Proposed replacements: ATP-dependent protein folding chaperone |
| GO:0000166 nucleotide binding | IEA GO_REF:0000043 | MARK AS OVER ANNOTATED | Summary: nucleotide binding is a true but overly broad family/keyword annotation for CCT5; ATP binding, ATP hydrolysis, and ATP-dependent chaperone annotations capture the specific chemistry. Reason: Generic nucleotide binding does not add useful functional information beyond the more specific ATP-related chaperonin annotations already present. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: CCT5 contains a conserved chaperonin ATP-binding site, but ATP binding alone is a domain property rather than the core biological function. Reason: Keep as a valid supporting molecular property of the CCT ATPase cycle, while treating ATP hydrolysis and complex-level protein folding as the core function. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: CCT5 functions as part of the cytosolic TRiC/CCT chaperonin. Reason: Cytoplasm is the established location of the CCT/TRiC folding machine. |
| GO:0005832 chaperonin-containing T-complex | IEA GO_REF:0000117 | ACCEPT | Summary: CCT5 is a named subunit of the chaperonin-containing T-complex. Reason: Complex membership is central to the gene product function and is supported by yeast CCT complex literature and family evidence. |
| GO:0006457 protein folding | IEA GO_REF:0000120 | ACCEPT | Summary: CCT5 participates in protein folding as an obligate subunit of TRiC/CCT, the cytosolic chaperonin that folds actin, tubulin, and other clients. Reason: Protein folding is the correct biological-process context for the chaperonin complex, supported by direct yeast CCT actin-folding assays and PANTHER/InterPro family evidence. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000002 | ACCEPT | Summary: CCT5 is a TCP-1/CCT chaperonin subunit with conserved ATPase machinery that powers TRiC/CCT conformational cycling. Reason: ATP hydrolysis is a defensible subunit-level molecular function for CCT family members and is directly tied to the chaperonin folding cycle. |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000120 | MODIFY | Summary: unfolded protein binding reflects substrate engagement by TRiC/CCT, but it is less informative than the ATP-dependent folding chaperone function of the complex. Reason: Replace generic substrate-binding language with the specific chaperonin activity supported by yeast CCT actin-folding assays and domain evidence. Proposed replacements: ATP-dependent protein folding chaperone |
| GO:0140662 ATP-dependent protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: CCT5 is an obligate subunit of the ATP-dependent TRiC/CCT folding machine. Reason: The term is appropriate as a complex-level chaperonin function; in the synthesized core function it is modeled as a contributed-to molecular function rather than a standalone activity of an isolated subunit. Supporting Evidence: PMID:16762366 The eukaryotic cytosolic chaperonin CCT is an essential ATP-dependent protein folding machine whose action is required for folding the cytoskeletal proteins actin and tubulin |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: protein binding is too generic for a CCT subunit and does not describe the chaperonin mechanism or substrate class. Reason: Physical-interaction datasets are useful evidence context, but generic protein binding should not stand as a functional annotation when the specific TRiC/CCT chaperonin role is known. Supporting Evidence: PMID:19536198 It should be emphasized that the interactions presented are indirect TAP-tag based interactions and not direct binary interactions. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | MARK AS OVER ANNOTATED | Summary: protein binding is too generic for a CCT subunit and does not describe the chaperonin mechanism or substrate class. Reason: Physical-interaction datasets are useful evidence context, but generic protein binding should not stand as a functional annotation when the specific TRiC/CCT chaperonin role is known. |
| GO:0006457 protein folding | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | ACCEPT | Summary: CCT5 participates in protein folding as an obligate subunit of TRiC/CCT, the cytosolic chaperonin that folds actin, tubulin, and other clients. Reason: Protein folding is the correct biological-process context for the chaperonin complex, supported by direct yeast CCT actin-folding assays and PANTHER/InterPro family evidence. Supporting Evidence: PMID:16762366 The eukaryotic cytosolic chaperonin CCT is an essential ATP-dependent protein folding machine whose action is required for folding the cytoskeletal proteins actin and tubulin |
| GO:0005832 chaperonin-containing T-complex | IPI PMID:15704212 Physiological effects of unassembled chaperonin Cct subunits... | ACCEPT | Summary: CCT5 is a named subunit of the chaperonin-containing T-complex. Reason: Complex membership is central to the gene product function and is supported by yeast CCT complex literature and family evidence. Supporting Evidence: PMID:16762366 The eukaryotic cytosolic chaperonin CCT is an essential ATP-dependent protein folding machine whose action is required for folding the cytoskeletal proteins actin and tubulin |
| GO:0005832 chaperonin-containing T-complex | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | ACCEPT | Summary: CCT5 is a named subunit of the chaperonin-containing T-complex. Reason: Complex membership is central to the gene product function and is supported by yeast CCT complex literature and family evidence. 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 |
| GO:0051082 unfolded protein binding | IDA PMID:16762366 Quantitative actin folding reactions using yeast CCT purifie... | MODIFY | Summary: unfolded protein binding reflects substrate engagement by TRiC/CCT, but it is less informative than the ATP-dependent folding chaperone function of the complex. Reason: Replace generic substrate-binding language with the specific chaperonin activity supported by yeast CCT actin-folding assays and domain evidence. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: PMID:16762366 The eukaryotic cytosolic chaperonin CCT is an essential ATP-dependent protein folding machine whose action is required for folding the cytoskeletal proteins actin and tubulin |
Loading supporting content…
Download this section (compressed HTML)Q: How does the high-ATP-affinity Cct5 subunit shape client progression through the yeast TRiC/CCT ATPase cycle?
Experiment: Compare ATPase-cycle reporters, client folding assays, and viability for targeted CCT5 ATP-pocket alleles in yeast, separating assembled-complex abundance from kinetic effects.
Hypothesis: Cct5 ATP binding/hydrolysis helps set the timing of TRiC/CCT chamber closure for actin and tubulin clients.
Type: site-directed mutagenesis with chaperonin folding and ATPase assays
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)