Crt10 is a WD-repeat protein of the Crt10 family found in the nucleus and cytoplasm of fission yeast. Its conserved role is inferred to be surveillance and disposal of nonfunctional large-subunit ribosomal RNA. In budding yeast, Crt10 directs an Rtt101-Mms1 cullin ubiquitin ligase toward defective ribosomes; the equivalent protein interactions and molecular activity of fission-yeast Crt10 remain incompletely characterized.
Summary: The ND molecular-function root correctly records that a specific molecular activity has not been established for fission-yeast Crt10.
Reason: The ND molecular-function root correctly records that a specific molecular activity has not been established for fission-yeast Crt10. Its Crt10/WD-repeat architecture supports an interaction protein, but does not identify a catalytic activity or a particular cullin partner.
HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...
ACCEPT
Summary: Nuclear and cytoplasmic localization is supported by the protein-localization study cited in the reviewed UniProt record (PMID:16823372); this is consistent with a nucleo-cytoplasmic RNA-surveillance protein.
Reason: Nuclear and cytoplasmic localization is supported by the protein-localization study cited in the reviewed UniProt record (PMID:16823372); this is consistent with a nucleo-cytoplasmic RNA-surveillance protein. Retain the compartment at the stated resolution.
Supporting Evidence:
file:SCHPO/crt10/crt10-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus CC {ECO:0000269|PubMed:16823372}.
Summary: Nuclear and cytoplasmic localization is supported by the protein-localization study cited in the reviewed UniProt record (PMID:16823372); this is consistent with a nucleo-cytoplasmic RNA-surveillance protein.
Reason: Nuclear and cytoplasmic localization is supported by the protein-localization study cited in the reviewed UniProt record (PMID:16823372); this is consistent with a nucleo-cytoplasmic RNA-surveillance protein. Retain the compartment at the stated resolution.
Supporting Evidence:
file:SCHPO/crt10/crt10-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus CC {ECO:0000269|PubMed:16823372}.
HDA PMID:22146723 Systematic localization study on novel proteins encoded by m...
UNDECIDED
Summary: The cited mitotic localization survey reports diverse cytoplasmic patterns among meiotically induced ORFs, but the accessible abstract does not identify the SPBC27B12.05 image or row.
Reason: The cited mitotic localization survey reports diverse cytoplasmic patterns among meiotically induced ORFs, but the accessible abstract does not identify the SPBC27B12.05 image or row. Cytoplasm is independently supported by PMID:16823372; retain this source-specific HDA assertion as unresolved until its target row is inspected.
Summary: Nuclear and cytoplasmic localization is supported by the protein-localization study cited in the reviewed UniProt record (PMID:16823372); this is consistent with a nucleo-cytoplasmic RNA-surveillance protein.
Reason: Nuclear and cytoplasmic localization is supported by the protein-localization study cited in the reviewed UniProt record (PMID:16823372); this is consistent with a nucleo-cytoplasmic RNA-surveillance protein. Retain the compartment at the stated resolution.
Supporting Evidence:
file:SCHPO/crt10/crt10-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus CC {ECO:0000269|PubMed:16823372}.
HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...
ACCEPT
Summary: Nuclear and cytoplasmic localization is supported by the protein-localization study cited in the reviewed UniProt record (PMID:16823372); this is consistent with a nucleo-cytoplasmic RNA-surveillance protein.
Reason: Nuclear and cytoplasmic localization is supported by the protein-localization study cited in the reviewed UniProt record (PMID:16823372); this is consistent with a nucleo-cytoplasmic RNA-surveillance protein. Retain the compartment at the stated resolution.
Supporting Evidence:
file:SCHPO/crt10/crt10-uniprot.txt
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus CC {ECO:0000269|PubMed:16823372}.
Summary: PomBase infers nonfunctional rRNA decay by curated orthology.
Reason: PomBase infers nonfunctional rRNA decay by curated orthology. The target has the diagnostic Crt10 family domain, and experiments in budding yeast show Crt10 is required for nonfunctional 25S rRNA decay. This supports the conserved pathway inference without assigning the target to a particular E3 complex.
We herein demonstrated that another accessory component, Crt10 was required for 25S NRD, but not for DNA repair, suggesting that this accessory component specifies the function of the E3 complex differently.
file:SCHPO/crt10/crt10-uniprot.txt
DR Pfam; PF08728; CRT10; 1.
Core Functions
Conserved Crt10-family factor inferred to participate in nonfunctional large-subunit rRNA decay. The exact molecular activity and cullin-binding partners in fission yeast are unresolved.
We herein demonstrated that another accessory component, Crt10 was required for 25S NRD, but not for DNA repair, suggesting that this accessory component specifies the function of the E3 complex differently.
Q: Does fission-yeast Crt10 bind Pcu4/Ddb1 or another cullin complex during nonfunctional rRNA decay, and does that association change after UV-B exposure?
External Prediction Reviews
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
Review rationale: Crt10 has a diagnostic CRT10 domain and a documented orthologous role in Rtt101-Mms1-dependent nonfunctional rRNA decay. This supports a relationship to cullin-mediated ubiquitination, but does not establish residence in the specific Cul4-RING E3 complex in fission yeast. The XML claim is a low-scoring phmmer transfer from Arabidopsis WDR5B Q9SY00 (model_score 0.11; phmmer_score 66.0); shared WD-repeat architecture does not demonstrate the relevant cullin partner or conserved subfamily function. Direct target-complex evidence or defensible orthology connecting this complex membership is missing. The claim is neither validated nor conclusively refuted.
Supporting Evidence:
PMID:25534857: "We herein demonstrated that another accessory component, Crt10 was required for 25S NRD, but not for DNA repair, suggesting that this accessory component specifies the function of the E3 complex differently."
Review rationale: The exact UV-B response prediction is not supported by the reviewed target annotations. Its source is a TMalign comparison to Arabidopsis DHU1 Q8GYY7 (model_score 0.11; chain-normalized scores 0.56569 and 0.36277), rather than a demonstrated conserved UV-B response mechanism. The experimentally characterized budding-yeast Crt10 directs nonfunctional 25S rRNA decay and is dispensable for the DNA-repair assay examined in that study, which does not exclude every possible UV-B response. Shared WD-repeat structure alone cannot validate this wavelength-specific phenotype in fission yeast. Target UV-B experiments or a conserved mechanistic link are missing, so UNC is appropriate.
Supporting Evidence:
PMID:25534857: "We herein demonstrated that another accessory component, Crt10 was required for 25S NRD, but not for DNA repair, suggesting that this accessory component specifies the function of the E3 complex differently."