CPR7 encodes a cytosolic CyP40-family Hsp90 co-chaperone with a cyclophilin peptidyl-prolyl isomerase domain and TPR-mediated Hsp90-binding domain; its core in vivo role is organizing Hsp90-dependent proteostasis and client maturation, with PPIase activity as a supported biochemical function.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003755 peptidyl-prolyl cis-trans isomerase activity | IBA GO_REF:0000033 | ACCEPT | Summary: peptidyl-prolyl cis-trans isomerase activity reviewed for CPR7: ACCEPT. Reason: Retain as a supported cyclophilin biochemical activity, with the caveat that it is not sufficient to explain all CPR7 in vivo roles. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 has **cyclosporin A (CsA)-inhibitable PPIase activity in vitro**, consistent with cyclophilins |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: cytoplasm reviewed for CPR7: ACCEPT. Reason: Retain as broad localization consistent with Cpr7 acting in the cytosolic Hsp90 chaperone system. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 is a cytosolic **CyP40-type cyclophilin/immunophilin** |
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: protein folding reviewed for CPR7: ACCEPT. Reason: Retain as the biological process supported by Cpr7 PPIase and Hsp90 co-chaperone functions. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 is an **Hsp90 co-chaperone** that regulates aspects of the Hsp90 folding cycle and client maturation via its **TPR-mediated binding** to Hsp90 |
| GO:0016018 cyclosporin A binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: cyclosporin A binding reviewed for CPR7: KEEP_AS_NON_CORE. Reason: Keep as an in vitro ligand-binding property of the cyclophilin domain, but it is not a core physiological function. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 has **cyclosporin A (CsA)-inhibitable PPIase activity in vitro**, consistent with cyclophilins |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: cytosol reviewed for CPR7: ACCEPT. Reason: Retain as the more precise localization for the cytosolic Hsp90 co-chaperone role. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 is a cytosolic **CyP40-type cyclophilin/immunophilin** |
| GO:0003755 peptidyl-prolyl cis-trans isomerase activity | IEA GO_REF:0000120 | ACCEPT | Summary: peptidyl-prolyl cis-trans isomerase activity reviewed for CPR7: ACCEPT. Reason: Retain as a supported cyclophilin biochemical activity, with the caveat that it is not sufficient to explain all CPR7 in vivo roles. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 has **cyclosporin A (CsA)-inhibitable PPIase activity in vitro**, consistent with cyclophilins |
| GO:0006457 protein folding | IEA GO_REF:0000002 | ACCEPT | Summary: protein folding reviewed for CPR7: ACCEPT. Reason: Retain as the biological process supported by Cpr7 PPIase and Hsp90 co-chaperone functions. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 is an **Hsp90 co-chaperone** that regulates aspects of the Hsp90 folding cycle and client maturation via its **TPR-mediated binding** to Hsp90 |
| GO:0016853 isomerase activity | IEA GO_REF:0000043 | MODIFY | Summary: isomerase activity reviewed for CPR7: MODIFY. Reason: General isomerase activity is less specific than the supported cyclophilin peptidyl-prolyl cis-trans isomerase activity. Proposed replacements: peptidyl-prolyl cis-trans isomerase activity Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md General isomerase activity is less specific than the supported cyclophilin peptidyl-prolyl cis-trans isomerase activity |
| GO:0042026 protein refolding | IEA GO_REF:0000117 | ACCEPT | Summary: protein refolding reviewed for CPR7: ACCEPT. Reason: Retain because Cpr7 has direct in vitro chaperone activity and participates in Hsp90/Hsp104-associated proteostasis and refolding networks. Supporting Evidence: PMID:10942767 In contrast, the chaperone activity of Cpr6 is much lower than that of Cpr7. |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000117 | MODIFY | Summary: unfolded protein binding reviewed for CPR7: MODIFY. Reason: Unfolded protein binding is too broad; Cpr7 is better represented as a chaperone/co-chaperone component of the Hsp90 folding machinery. Proposed replacements: protein folding chaperone Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 is best annotated as an Hsp90 co-chaperone with immunophilin architecture |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | MODIFY | Summary: protein binding reviewed for CPR7: MODIFY. Reason: Replace generic protein binding with protein-folding chaperone binding because this evidence is specifically about Cpr7 participation in Hsp90/co-chaperone machinery, not an undifferentiated interaction survey. Proposed replacements: protein-folding chaperone binding Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Hsp90 binding is mediated by the **carboxy-terminal TPR region**, which recognizes the conserved Hsp90 C-terminal **EEVD/MEEVD** acceptor motif |
| GO:0005515 protein binding | IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for CPR7: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is generic here because the source is a broad complex/interactome survey rather than a focused Hsp90-co-chaperone experiment; do not convert this one to a specific Hsp90-binding term. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 genetically and physically associates with the Hsp90 system |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for CPR7: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is generic here because the source is a broad chaperone-interaction atlas rather than a focused Cpr7-Hsp90 mechanistic study; do not convert this one to a specific Hsp90-binding term. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 influences the maturation of heterologous clients and drug sensitivity |
| GO:0005515 protein binding | IPI PMID:23396352 Integration of the accelerator Aha1 in the Hsp90 co-chaperon... | MODIFY | Summary: protein binding reviewed for CPR7: MODIFY. Reason: Replace generic protein binding with protein-folding chaperone binding because this evidence concerns the Hsp90 co-chaperone cycle rather than a nonspecific interactome hit. Proposed replacements: protein-folding chaperone binding Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 supports maturation of multiple clients and participates in selective Hsp90 co-chaperone modules |
| GO:0005515 protein binding | IPI PMID:8873448 Identification of two CyP-40-like cyclophilins in Saccharomy... | MARK AS OVER ANNOTATED | Summary: protein binding reviewed for CPR7: MARK_AS_OVER_ANNOTATED. Reason: Protein binding is generic here because this older interaction evidence is not specific enough to distinguish the Hsp90-binding function from broad protein association. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md CPR7 is one of two yeast **cyclophilin-40 (CyP40) homologs** analyzed in the context of the **Hsp90 chaperone machine** |
| GO:0005515 protein binding | IPI PMID:9819421 CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces ... | MODIFY | Summary: protein binding reviewed for CPR7: MODIFY. Reason: Replace generic protein binding with protein-folding chaperone binding because the cited biology is the CPR7/Cns1/Hsp90 co-chaperone system. Proposed replacements: protein-folding chaperone binding Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cns1 was isolated as a **high-copy suppressor** of the cpr7 deletion slow-growth phenotype and is found in complexes with **Hsp90 and Cpr7** |
| GO:0005515 protein binding | IPI PMID:9819422 Cns1 is an essential protein associated with the hsp90 chape... | MODIFY | Summary: protein binding reviewed for CPR7: MODIFY. Reason: Replace generic protein binding with protein-folding chaperone binding because the evidence concerns Cpr7 interaction with Hsp90 machinery. Proposed replacements: protein-folding chaperone binding Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Hsp90 binding is mediated by the **carboxy-terminal TPR region**, which recognizes the conserved Hsp90 C-terminal **EEVD/MEEVD** acceptor motif |
| GO:0005829 cytosol | IPI PMID:10942767 Cpr6 and Cpr7, two closely related Hsp90-associated immunoph... | ACCEPT | Summary: cytosol reviewed for CPR7: ACCEPT. Reason: Retain as the more precise localization for the cytosolic Hsp90 co-chaperone role. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 is a cytosolic **CyP40-type cyclophilin/immunophilin** |
| GO:0003755 peptidyl-prolyl cis-trans isomerase activity | IDA PMID:10942767 Cpr6 and Cpr7, two closely related Hsp90-associated immunoph... | ACCEPT | Summary: peptidyl-prolyl cis-trans isomerase activity reviewed for CPR7: ACCEPT. Reason: Retain as a supported cyclophilin biochemical activity, with the caveat that it is not sufficient to explain all CPR7 in vivo roles. Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 has **cyclosporin A (CsA)-inhibitable PPIase activity in vitro**, consistent with cyclophilins |
| GO:0042026 protein refolding | IDA PMID:10942767 Cpr6 and Cpr7, two closely related Hsp90-associated immunoph... | ACCEPT | Summary: protein refolding reviewed for CPR7: ACCEPT. Reason: Retain because Cpr7 has direct in vitro chaperone activity and participates in Hsp90/Hsp104-associated proteostasis and refolding networks. Supporting Evidence: PMID:10942767 In contrast, the chaperone activity of Cpr6 is much lower than that of Cpr7. |
| GO:0051082 unfolded protein binding | IDA PMID:10942767 Cpr6 and Cpr7, two closely related Hsp90-associated immunoph... | MODIFY | Summary: unfolded protein binding reviewed for CPR7: MODIFY. Reason: Unfolded protein binding is too broad; Cpr7 is better represented as a chaperone/co-chaperone component of the Hsp90 folding machinery. Proposed replacements: protein folding chaperone Supporting Evidence: file:yeast/CPR7/CPR7-deep-research-falcon.md Cpr7 is best annotated as an Hsp90 co-chaperone with immunophilin architecture |
Loading supporting content…
Download this section (compressed HTML)Q: Which endogenous yeast Hsp90 clients require Cpr7 catalytic PPIase activity rather than TPR-mediated co-chaperone scaffolding?
Q: How does Cpr7 coordinate with Cns1, Sti1, Cpr6, and Hsp104 across different metabolic or stress states?
Experiment: Compare endogenous CPR7 wild type, PPIase-dead, PPIase-domain surface, and TPR-disrupting mutants for Hsp90 binding, client maturation, eEF2 solubility, stress sensitivity, and protein-refolding phenotypes.
Hypothesis: Most CPR7-dependent proteostasis phenotypes require TPR-mediated Hsp90 co-chaperone function, while a narrower client subset depends on PPIase-domain surfaces.
Type: domain separation-of-function analysis
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)