| Category | Key findings (concise) | Evidence (study + year) | URL/DOI | Notes/quantitative data |
|---|---|---|---|---|
| Identity/domains | UniProt target O94656 matches **S. pombe** ORF **SPBC405.05**, named **atg16**; the protein is homologous to budding-yeast Atg16 and contains an **N-terminal Atg5-binding region** plus a **C-terminal coiled-coil domain**. (pqac-00000000, pqac-00000010, pqac-00000026) | Sun et al., 2013; Xu & Du, 2022 | https://doi.org/10.1371/journal.pgen.1003715; https://doi.org/10.3390/cells11071086 | Sequence/domain assignment is from the S. pombe primary paper; aligns with UniProt family call. |
| Molecular function | Atg16 is the scaffold subunit of the **Atg12–Atg5–Atg16** complex, which functions as the **E3-like factor for Atg8 conjugation to phosphatidylethanolamine (PE)** and helps determine where Atg8 lipidation occurs on autophagic membranes. (pqac-00000002, pqac-00000004, pqac-00000005, pqac-00000009) | Xu & Du, 2022; Noda, 2023 | https://doi.org/10.3390/cells11071086; https://doi.org/10.1080/27694127.2023.2277582 | Not an enzyme with its own catalytic active site; functions as an adaptor/scaffold within the E3-like complex. |
| Complex/partners | In **S. pombe**, Atg16 physically associates with **Atg5**; co-immunoprecipitation detected the Atg5–Atg16 interaction **both in wild type and atg12Δ cells**, indicating Atg5 binding does not strictly require Atg12. Atg18a also functionally/physically links to the complex for PAS targeting. (pqac-00000000, pqac-00000001, pqac-00000010, pqac-00000023) | Sun et al., 2013 | https://doi.org/10.1371/journal.pgen.1003715 | Co-IP inputs/IPs reported in the paper include **1% input / 20% IP** for one assay setup (pqac-00000020). |
| Localization | Atg16 localizes to the **PAS (phagophore assembly site / pre-autophagosomal structure)** during starvation and colocalizes with **CFP-Atg8**; proper PAS localization of the Atg12–Atg5–Atg16 complex requires **Atg18a**. (pqac-00000001, pqac-00000004, pqac-00000011) | Sun et al., 2013; Xu & Du, 2022 | https://doi.org/10.1371/journal.pgen.1003715; https://doi.org/10.3390/cells11071086 | Microscopy figures show **Atg16-YFP**, **Atg5-YFP**, and **Atg18a-YFP** colocalizing with CFP-Atg8; in **atg18aΔ**, Atg5/Atg16 puncta are lost (pqac-00000011). |
| Phenotypes/assays | **atg16Δ** is defective in **CFP-Atg8 processing**, supporting a requirement for bulk autophagy; **atg16Δ** cells also fail to form normal **Atg8 puncta** at the PAS in the cited imaging analysis. (pqac-00000000, pqac-00000010, pqac-00000011) | Sun et al., 2013 | https://doi.org/10.1371/journal.pgen.1003715 | Time course for the CFP-Atg8 assay included samples **before and 8 h after nitrogen starvation**; the snippet is qualitative and does not report a numeric processing fraction for atg16Δ (pqac-00000020). |
| S. pombe-specific notes | A notable **fission-yeast-specific feature** is that **Atg18a** is uniquely required to recruit the **Atg12–Atg5–Atg16** complex to the PAS; the three Atg18/WIPI paralogs are not redundant, and Atg18a differs functionally from Atg18b/c. (pqac-00000001, pqac-00000004, pqac-00000023) | Sun et al., 2013; Xu & Du, 2022 | https://doi.org/10.1371/journal.pgen.1003715; https://doi.org/10.3390/cells11071086 | In the cited phenotypes, **atg18aΔ abolishes Atg8 puncta**, whereas **atg18bΔ/atg18cΔ increase Atg8 puncta**, consistent with different pathway roles (pqac-00000001). |
| Recent (2023-2024) mechanistic context | Recent reviews/primary studies reinforce that Atg16/ATG16L1 has an **Atg5-binding N-terminus** and a **dimeric coiled-coil** that recruits the E3-like complex through **PROPPIN/WIPI proteins**; Atg16 dimerization is important for PROPPIN binding, and the coiled-coil has been described as about **13 nm** long in structural context. (pqac-00000005, pqac-00000006, pqac-00000007, pqac-00000008) | Noda, 2023; Bueno-Arribas et al., 2023 | https://doi.org/10.1080/27694127.2023.2277582; https://doi.org/10.1098/rsob.230192 | These recent papers are mostly broader mechanistic/structural context, not S. pombe-specific biochemistry for O94656 alone. |
| Applications/statistics | **S. pombe Atg16** was discovered/validated through a **genome-wide mating-phenotype barcode screen** and is now part of the tractable fission-yeast autophagy toolkit using **CFP/GFP-Atg8 processing** assays. The screen analyzed **2,915 deletion mutants**, generated **63,146 MD-score measurements** across **22 screens**, and called **206** hits at **FDR < 0.1** in all three standard screens; the study expanded the experimentally defined S. pombe autophagy factor set from **14 to 23** genes. (pqac-00000019, pqac-00000020, pqac-00000022, pqac-00000024, pqac-00000026) | Sun et al., 2013; Xu & Du, 2022 | https://doi.org/10.1371/journal.pgen.1003715; https://doi.org/10.3390/cells11071086 | Practical implementation details include **>99% spore purity**, barcode filters requiring **≥12 reads** and **≥1/40 upper-quartile** counts, and use of CFP/GFP-Atg8 processing as routine autophagy-flux assays (pqac-00000019, pqac-00000021). |


*Table: This table summarizes the core functional annotation of Schizosaccharomyces pombe Atg16 (UniProt O94656 / SPBC405.05), including identity, molecular role, interaction partners, localization, phenotypes, and recent mechanistic context. It is useful as a compact evidence map tying S. pombe-specific findings to broader 2023–2024 autophagy research.*