Summary: protein folding reviewed for CCT2: ACCEPT.

Reason: Retain as the core process carried out by the CCT/TRiC chaperonin containing Cct2.

Summary: chaperonin-containing T-complex reviewed for CCT2: ACCEPT.

Reason: Retain; Cct2 is a core subunit of the chaperonin-containing T-complex/CCT.

Summary: GO:0051082 is formally obsolete; Cct2 contributes to the CCT/TRiC complex's ATP-dependent protein-folding chaperone activity.

Reason: GO:0051082 "unfolded protein binding" is obsolete with GO:0044183 protein folding chaperone and GO:0140309 unfolded protein holdase activity as consider terms. The current PTHR11353 PAINT snapshot no longer carries GO:0051082 at this node. For Cct2, the evidence supports the more specific GO:0140662 ATP-dependent protein folding chaperone activity of the CCT/TRiC complex; because Cct2 is one subunit of that complex, any final GOA replacement with GO:0140662 should use the contributes_to qualifier.

Proposed replacements: ATP-dependent protein folding chaperone

Summary: nucleotide binding reviewed for CCT2: MODIFY.

Reason: Nucleotide binding is too general; Cct2 has a conserved ATP-binding/hydrolysis chaperonin domain.

Proposed replacements: ATP binding ATP hydrolysis activity

Summary: ATP binding reviewed for CCT2: ACCEPT.

Reason: Retain as a direct subunit molecular function supported by conserved CCT ATPase-domain biology.

Summary: cytoplasm reviewed for CCT2: ACCEPT.

Reason: Retain as a broad localization consistent with cytosolic CCT/TRiC function.

Summary: cytosol reviewed for CCT2: ACCEPT.

Reason: Retain as the more precise core localization for cytosolic CCT/TRiC.

Summary: chaperonin-containing T-complex reviewed for CCT2: ACCEPT.

Reason: Retain; Cct2 is a core subunit of the chaperonin-containing T-complex/CCT.

Summary: protein folding reviewed for CCT2: ACCEPT.

Reason: Retain as the core process carried out by the CCT/TRiC chaperonin containing Cct2.

Summary: ATP hydrolysis activity reviewed for CCT2: ACCEPT.

Reason: Retain as the ATPase activity coupled to the CCT/TRiC folding cycle.

Summary: GO:0051082 is formally obsolete; the CCT/TRiC complex-level replacement is ATP-dependent protein folding chaperone activity.

Reason: GO:0051082 "unfolded protein binding" is obsolete with GO:0044183 protein folding chaperone and GO:0140309 unfolded protein holdase activity as consider terms. The current automatic InterPro/UniProt rows no longer emit GO:0051082 for Cct2. The supported complex-level molecular function is GO:0140662 ATP-dependent protein folding chaperone activity of the CCT/TRiC complex; because Cct2 is one subunit of that complex, any final GOA replacement with GO:0140662 should use the contributes_to qualifier.

Proposed replacements: ATP-dependent protein folding chaperone

Summary: ATP-dependent protein folding chaperone is the best available molecular-function term for CCT/TRiC.

Reason: CCT/TRiC is an ATP-dependent protein-folding machine, and Cct2 contributes as one subunit of this complex.

Summary: protein binding reviewed for CCT2: REMOVE.

Reason: The interaction is compatible with Cct2's participation in the CCT/TRiC complex, but generic protein binding does not capture a specific molecular function. No more specific binding activity is supported by this high-throughput complex-mapping row.

Summary: protein binding reviewed for CCT2: REMOVE.

Reason: The chaperone-interaction atlas supports CCT/TRiC physical associations, but GO:0005515 is an uninformative molecular-function placeholder and the row does not establish a narrower binding term beyond Cct2's accepted chaperonin-complex and ATP-dependent folding activities.

Summary: protein binding reviewed for CCT2: REMOVE.

Reason: The 2023 interactome recovers CCT subunits and interactors by correlation even though the complex resists direct tagging, but this supports CCT/TRiC membership and client association rather than a useful standalone GO:0005515 molecular-function annotation.

Summary: protein folding reviewed for CCT2: ACCEPT.

Reason: Retain as the core process carried out by the CCT/TRiC chaperonin containing Cct2.

Summary: protein binding reviewed for CCT2: REMOVE.

Reason: Physical interaction with the co-chaperone PLP2 is biologically real, but generic protein binding is less informative than the accepted ATP-dependent protein-folding chaperone activity of the CCT/TRiC complex and the evidence does not define a specific replacement binding activity.

Summary: cytoplasm reviewed for CCT2: ACCEPT.

Reason: Retain as a broad localization consistent with cytosolic CCT/TRiC function.

Summary: chaperonin-containing T-complex reviewed for CCT2: ACCEPT.

Reason: Retain; Cct2 is a core subunit of the chaperonin-containing T-complex/CCT.

Summary: chaperonin-containing T-complex reviewed for CCT2: ACCEPT.

Reason: Retain; Cct2 is a core subunit of the chaperonin-containing T-complex/CCT.

Summary: GO:0051082 is formally obsolete; the CCT3-tagged yeast complex supports CCT/TRiC foldase function.

Reason: GO:0051082 "unfolded protein binding" is obsolete with GO:0044183 protein folding chaperone and GO:0140309 unfolded protein holdase activity as consider terms. The purified-CCT actin-folding evidence supports the GO:0140662 ATP-dependent protein folding chaperone activity of the CCT/TRiC complex more specifically than GO:0051082; because Cct2 is one subunit of that complex, any final GOA replacement with GO:0140662 should use the contributes_to qualifier.

Proposed replacements: ATP-dependent protein folding chaperone

Summary: The current InterPro row correctly captures Cct2 ATP binding through the conserved CCT/TRiC chaperonin ATPase domain.

Reason: Cct2 is a group II chaperonin subunit with an equatorial ATP-binding site; ATP binding is a direct subunit activity coupled to CCT/TRiC conformational cycling.

Summary: Dekker et al. structurally resolved yeast CCT as a hetero-oligomeric double-ring chaperonin, directly supporting Cct2 as part of the CCT/TRiC complex.

Reason: The yeast CCT crystal structure establishes the subunit organization of the chaperonin-containing T-complex; the ComplexPortal IPI row is therefore a direct experimental complex-membership annotation.