The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The gene symbol “crt10” is ambiguous, and literature is very limited for this specific protein. The identifiers that safely define the research target are UniProt O42996, ORF SPBC27B12.05 (alias pi073), from Schizosaccharomyces pombe strain 972/ATCC 24843. Exact searches using these identifiers and S. pombe crt10 found no primary study directly characterizing the protein. Therefore, findings about similarly named genes in other organisms were not transferred to this target.
O42996 is best described as an uncharacterized, probably nonenzymatic WD-repeat/β-propeller protein. Its supplied InterPro annotations—WD40-repeat signatures plus “Coatomer_complex_subunit” and “Crt10”—make a protein-interaction or scaffolding role, possibly related to an intracellular coatomer-like complex, plausible. They do not, however, establish COPI or COPII membership, a particular cargo, a biochemical reaction, localization, phenotype, or signaling pathway.
| Question | Best-supported conclusion | Evidence type | Confidence |
|---|---|---|---|
| Identity | Target is the Schizosaccharomyces pombe strain 972 protein O42996, encoded by ORF SPBC27B12.05 (alias pi073) and described as an uncharacterized WD repeat-containing protein. The label crt10/Crt10 is ambiguous and should not be used without the accession and organism. | Supplied UniProt record; identifier-specific literature searches found no direct paper | High for accession/ORF identity; low for crt10 as an established gene name |
| Molecular function | No experimentally established molecular function was found. The safest hypothesis is a nonenzymatic protein-interaction or scaffolding role characteristic of WD40 β-propellers—not a demonstrated activity of O42996. | Supplied domain annotation plus family-level inference | Low–moderate |
| Domains/structure | Supplied InterPro annotations include Coatomer_complex_subunit (IPR050844), Crt10 (IPR014839), WD40/YVTN-repeat-like and WD40-domain superfamilies (IPR015943, IPR036322), and a WD40-repeat conserved site (IPR019775). These support a WD40-like β-propeller fold but do not prove membership in a particular coat complex. Protocoatomer proteins commonly use β-propeller architecture (schlacht2015unexpectedancientparalogs pages 2-3). | Computational sequence/domain classification; family-level structural literature | High for WD40-like architecture; low–moderate for coatomer assignment |
| Biological process/pathway | Intracellular membrane trafficking is a plausible hypothesis because of the coatomer signature. COPI mediates Golgi-to-ER and intra-Golgi traffic, whereas COPII mediates ER-to-Golgi export (schlacht2015unexpectedancientparalogs pages 1-2, enkler2021cex1isa pages 1-2). No evidence identifies O42996 as a COPI or COPII component, so neither pathway should be assigned as established. | Family-level mechanistic analogy only | Low |
| Localization | Unknown for O42996. A coatomer-related hypothesis would predict association with cytosolic faces of ER/Golgi-derived membranes or vesicles, but this has not been demonstrated. Related COPI-associated proteins can occupy membrane fractions and Golgi/TGN puncta (enkler2021cex1isa pages 4-6). | Family-level localization analogy; no target-specific experiment | Low |
| Catalytic activity/substrate | No catalytic reaction, enzyme class, transporter substrate, or cargo specificity is established. WD40 proteins generally provide interaction surfaces; in known COPI machinery, a Sec27 WD40 propeller recognizes a dilysine cargo motif, but this cannot be transferred to O42996 (lam2009theroleof pages 16-21, enkler2021cex1isa pages 4-6). | Absence of target-specific evidence; mechanistic family comparison | High that no activity/substrate is presently established |
| Gene-specific experimental literature | Exact searches for O42996, SPBC27B12.05, pi073, and S. pombe crt10 found no primary study directly characterizing function, localization, interactions, phenotype, structure, or pathway. Literature on similarly named genes or other organisms must not be used for this target. | Identifier-specific literature search | High within the searched literature |
| Recent 2024 high-throughput context | A 2024 meiotic study quantified 4,673 proteins (~91% of the predicted proteome) and 7,172 phosphosites, with 2,680 proteins and 4,005 sites changing significantly, but its retrieved text did not name or interpret crt10/O42996 (sivakova2024quantitativeproteomicsand pages 1-2, sivakova2024quantitativeproteomicsand pages 12-14, sivakova2024quantitativeproteomicsand pages 5-6). A December 2024 RNA-dependence screen detected 2,563 S. pombe proteins and classified 472 (18.4%) as RNA-dependent, yet supplied no target-specific conclusion (waber2024acensusof pages 1-2). | Recent high-throughput proteomics; no demonstrated target-level interpretation | High for dataset statistics; none for O42996 function |
Table: This table separates verified identity and domain annotations from family-level hypotheses and unresolved functions. It also shows why recent high-throughput studies do not yet establish a molecular role or localization for O42996.
The requested identity is internally consistent:
The critical nomenclature caveat is that Crt10 appears more securely supported here as a computational family/domain label than as a literature-established functional gene name in fission yeast. No retrieved article named O42996, SPBC27B12.05, or pi073. Consequently, O42996/SPBC27B12.05—not “crt10” alone—should be used in future searches and experiments.
WD40 repeats generally assemble into β-propeller structures that provide broad surfaces for protein–protein interactions and multiprotein-complex assembly. Multiple independent WD40-related InterPro calls in O42996 make this architectural interpretation substantially stronger than any particular pathway assignment.
This architecture is compatible with coat-associated scaffolding: evolutionarily related protocoatomer systems use β-propeller/α-solenoid architectures in membrane-deforming and trafficking complexes. COPII core components are ancient, and five subunits—Sar1, Sec23, Sec24, Sec13, and Sec31—are sufficient for vesicle budding in vitro. Nevertheless, that family-level observation does not identify O42996 as any one of these components or even prove it belongs to COPII (schlacht2015unexpectedancientparalogs pages 2-3).
There is no evidence that O42996 is an enzyme or transporter. No catalytic residues, EC reaction, substrate, product, transporter class, or transported molecule has been established. The most defensible working model is instead a noncatalytic interaction protein or adaptor/scaffold.
Known coatomer proteins illustrate what such a role could entail. In COPI, WD40 propellers of the β′-COP/Sec27 subunit bind cytosolic dilysine retrieval motifs on membrane cargo. This demonstrates that a WD40 coat protein can function as a cargo-recognition surface, but it does not show that O42996 recognizes dilysine motifs or any other cargo (lam2009theroleof pages 16-21, enkler2021cex1isa pages 4-6).
The “Coatomer_complex_subunit” signature makes intracellular membrane trafficking a reasonable hypothesis, but assignment to a specific route would currently be overinterpretation.
No retrieved evidence places O42996 in either complex. It therefore should not yet receive a definitive COPI, COPII, ER–Golgi transport, or vesicle-cargo-selection annotation. Likewise, no signaling cascade, metabolic pathway, cell-cycle module, or stress pathway is directly supported.
The localization of O42996 is unknown. If its coatomer-family prediction is correct, one might expect a cytosolic protein that is recruited transiently to the cytoplasmic face of ER-, Golgi-, or vesicle-associated membranes. This remains a testable hypothesis, not an annotation.
The distinction is important because related coat-associated proteins can show specific membrane localization. For example, budding-yeast Cex1 interacts with several COPI subunits and occurs in membrane-associated fractions and α-COP-positive/TGN puncta; deletion perturbs retrieval of one ER membrane protein. These observations validate membrane fractionation, colocalization, and cargo-retrieval assays as approaches, but Cex1 is a different protein and its localization cannot be assigned to O42996 (enkler2021cex1isa pages 4-6, enkler2021cex1isa pages 2-3).
No retrieved publication directly reports O42996/SPBC27B12.05 localization, deletion phenotype, physical interactions, structure, cargo specificity, catalytic activity, or pathway membership. Thus, there is presently no precise experiment that establishes its primary function.
A peer-reviewed October 2024 meiotic proteomics study used TMTpro 18-plex labeling and phosphopeptide enrichment to quantify 4,673 proteins—about 91% of the predicted S. pombe proteome—and 7,172 phosphosites. Across mitosis and meiotic stages, 2,680 proteins (57.4%) and 4,005 phosphosites (55.8%) changed significantly. The retrieved article text did not name or interpret crt10/O42996, so these impressive coverage statistics do not establish its function (sivakova2024quantitativeproteomicsand pages 1-2, sivakova2024quantitativeproteomicsand pages 12-14, sivakova2024quantitativeproteomicsand pages 5-6). Publication: Sivakova et al., Scientific Reports, October 2024, DOI 10.1038/s41598-024-74523-0.
A December 2024 preprint adapted R-DeeP/RNase-dependent sedimentation profiling to fission yeast. It detected 2,563 proteins, of which 472 (18.4%) shifted after RNase treatment. Such shifts indicate RNA-dependent sedimentation or complex association, not necessarily direct RNA binding; the retrieved evidence again supplied no O42996-specific conclusion (waber2024acensusof pages 1-2, waber2024acensusof pages 2-5). Publication: Wäber et al., bioRxiv, December 2024, DOI 10.1101/2024.12.06.627129.
There is no known real-world application specifically involving O42996. However, current S. pombe tools make direct characterization practical. The peer-reviewed POMBOX system supports protein expression, epitope tagging, deletion, mutation insertion, interaction studies, and multigene assembly. It includes 40 new DNA parts, 14 characterized promoters, 12 tested terminators, and constructs spanning 4–24 kb; it can assemble pathways of up to 12 transcriptional units and was used to generate as many as 24 fluorescent-protein strains in seven days (hebra2024pomboxafission pages 1-2, hebra2024pomboxafission pages 3-5, hebra2024pomboxafission pages 2-3). Publication: Hebra et al., ACS Synthetic Biology 13:558–567, published online November 22, 2023/in the 2024 volume, DOI 10.1021/acssynbio.3c00529.
The highest-value experiments would be:
The strongest current conclusion is architectural rather than mechanistic: O42996 is likely a WD40 β-propeller interaction protein. The coatomer-related annotation raises a credible trafficking hypothesis, because coat complexes contain β-propeller interaction and cargo-recognition modules and operate at ER/Golgi membranes. Yet WD40 domains occur in many unrelated complexes, and coatomer/protocoatomer architecture spans trafficking coats, nuclear pores, and other assemblies (schlacht2015unexpectedancientparalogs pages 2-3).
Accordingly, the following remain unresolved:
The recommended annotation is therefore: “Uncharacterized WD40-repeat protein; predicted protein-interaction/scaffolding factor, possibly associated with a coatomer-like complex.” A more specific description would exceed the available evidence.
References
(schlacht2015unexpectedancientparalogs pages 2-3): Alexander Schlacht and Joel B. Dacks. Unexpected ancient paralogs and an evolutionary model for the copii coat complex. Genome Biology and Evolution, 7:1098-1109, Mar 2015. URL: https://doi.org/10.1093/gbe/evv045, doi:10.1093/gbe/evv045. This article has 59 citations and is from a domain leading peer-reviewed journal.
(schlacht2015unexpectedancientparalogs pages 1-2): Alexander Schlacht and Joel B. Dacks. Unexpected ancient paralogs and an evolutionary model for the copii coat complex. Genome Biology and Evolution, 7:1098-1109, Mar 2015. URL: https://doi.org/10.1093/gbe/evv045, doi:10.1093/gbe/evv045. This article has 59 citations and is from a domain leading peer-reviewed journal.
(enkler2021cex1isa pages 1-2): Ludovic Enkler, Bruno Rinaldi, Johan Owen de Craene, Philippe Hammann, Osamu Nureki, Bruno Senger, Sylvie Friant, and Hubert D. Becker. Cex1 is a component of the copi intracellular trafficking machinery. Biology Open, Mar 2021. URL: https://doi.org/10.1242/bio.058528, doi:10.1242/bio.058528. This article has 2 citations and is from a peer-reviewed journal.
(enkler2021cex1isa pages 4-6): Ludovic Enkler, Bruno Rinaldi, Johan Owen de Craene, Philippe Hammann, Osamu Nureki, Bruno Senger, Sylvie Friant, and Hubert D. Becker. Cex1 is a component of the copi intracellular trafficking machinery. Biology Open, Mar 2021. URL: https://doi.org/10.1242/bio.058528, doi:10.1242/bio.058528. This article has 2 citations and is from a peer-reviewed journal.
(lam2009theroleof pages 16-21): Karen Kar Yan Lam. The role of palmitoylation in endoplasmic reticulum transport and quality control of the yeast polytopic protein chs3. ArXiv, Jan 2009. URL: https://doi.org/10.14288/1.0067083, doi:10.14288/1.0067083. This article has 4 citations.
(sivakova2024quantitativeproteomicsand pages 1-2): Barbara Sivakova, Anja Wagner, Miroslava Kretova, Jana Jakubikova, Juraj Gregan, Klaus Kratochwill, Peter Barath, and Lubos Cipak. Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast schizosaccharomyces pombe. Scientific Reports, Oct 2024. URL: https://doi.org/10.1038/s41598-024-74523-0, doi:10.1038/s41598-024-74523-0. This article has 11 citations and is from a peer-reviewed journal.
(sivakova2024quantitativeproteomicsand pages 12-14): Barbara Sivakova, Anja Wagner, Miroslava Kretova, Jana Jakubikova, Juraj Gregan, Klaus Kratochwill, Peter Barath, and Lubos Cipak. Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast schizosaccharomyces pombe. Scientific Reports, Oct 2024. URL: https://doi.org/10.1038/s41598-024-74523-0, doi:10.1038/s41598-024-74523-0. This article has 11 citations and is from a peer-reviewed journal.
(sivakova2024quantitativeproteomicsand pages 5-6): Barbara Sivakova, Anja Wagner, Miroslava Kretova, Jana Jakubikova, Juraj Gregan, Klaus Kratochwill, Peter Barath, and Lubos Cipak. Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast schizosaccharomyces pombe. Scientific Reports, Oct 2024. URL: https://doi.org/10.1038/s41598-024-74523-0, doi:10.1038/s41598-024-74523-0. This article has 11 citations and is from a peer-reviewed journal.
(waber2024acensusof pages 1-2): Nadine Bianca Wäber, Johanna Seidler, Fabienne Thelen, Thomas Timm, Günter Lochnit, Katja Sträßer, and Cornelia Kilchert. A census of rna-dependent proteins in yeast. bioRxiv, Dec 2024. URL: https://doi.org/10.1101/2024.12.06.627129, doi:10.1101/2024.12.06.627129. This article has 0 citations.
(enkler2021cex1isa pages 2-3): Ludovic Enkler, Bruno Rinaldi, Johan Owen de Craene, Philippe Hammann, Osamu Nureki, Bruno Senger, Sylvie Friant, and Hubert D. Becker. Cex1 is a component of the copi intracellular trafficking machinery. Biology Open, Mar 2021. URL: https://doi.org/10.1242/bio.058528, doi:10.1242/bio.058528. This article has 2 citations and is from a peer-reviewed journal.
(waber2024acensusof pages 2-5): Nadine Bianca Wäber, Johanna Seidler, Fabienne Thelen, Thomas Timm, Günter Lochnit, Katja Sträßer, and Cornelia Kilchert. A census of rna-dependent proteins in yeast. bioRxiv, Dec 2024. URL: https://doi.org/10.1101/2024.12.06.627129, doi:10.1101/2024.12.06.627129. This article has 0 citations.
(hebra2024pomboxafission pages 1-2): Téo Hebra, Helena Smrčková, Büsra Elkatmis, Martin Převorovský, and Tomáš Pluskal. Pombox: a fission yeast cloning toolkit for molecular and synthetic biology. ACS Synthetic Biology, 13:558-567, Nov 2024. URL: https://doi.org/10.1021/acssynbio.3c00529, doi:10.1021/acssynbio.3c00529. This article has 7 citations and is from a domain leading peer-reviewed journal.
(hebra2024pomboxafission pages 3-5): Téo Hebra, Helena Smrčková, Büsra Elkatmis, Martin Převorovský, and Tomáš Pluskal. Pombox: a fission yeast cloning toolkit for molecular and synthetic biology. ACS Synthetic Biology, 13:558-567, Nov 2024. URL: https://doi.org/10.1021/acssynbio.3c00529, doi:10.1021/acssynbio.3c00529. This article has 7 citations and is from a domain leading peer-reviewed journal.
(hebra2024pomboxafission pages 2-3): Téo Hebra, Helena Smrčková, Büsra Elkatmis, Martin Převorovský, and Tomáš Pluskal. Pombox: a fission yeast cloning toolkit for molecular and synthetic biology. ACS Synthetic Biology, 13:558-567, Nov 2024. URL: https://doi.org/10.1021/acssynbio.3c00529, doi:10.1021/acssynbio.3c00529. This article has 7 citations and is from a domain leading peer-reviewed journal.