pik3 (vps34; SPAC458.05; UniProt P50520) encodes the only phosphatidylinositol 3-kinase of fission yeast, a class III enzyme that phosphorylates phosphatidylinositol at the D-3 position to make PI3P and does not make PI(3,4)P2 or PIP3. Like its orthologs, it works in two complexes with Vps15 and Atg6. Complex I, with Atg14 and the fission-yeast-specific Atg8-binding Atg38, makes PI3P at the phagophore assembly site for autophagy. Complex II, with Vps38, acts on endosomes for vacuolar protein sorting. pik3 deletion cells lose PI3P, have enlarged vacuoles and are sensitive to heat and salt. During sporulation, PI3P recruits the sorting nexins Vps5/Vps17 to orient forespore membrane growth, and pik3 deletion spores are inviable.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000045 autophagosome assembly | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; Vps34 in PtdIns3K complex I makes PI3P at the phagophore, needed for autophagosome formation. Supported by S. pombe complex I work. Reason: Pik3 is the catalytic subunit of fission yeast PtdIns3K complex I (with Vps15, Atg6, Atg14, and Atg38), which generates PI3P at the phagophore assembly site and establishes a positive feedback loop with Atg8 to drive autophagosome formation (PMID:31941401). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K (Vps34/PIK3C3) clade node; autophagosome assembly via complex I is conserved and experimentally demonstrated in S. pombe. MGI:MGI:2445019 SUPPORTS TRANSFER Mouse Pik3c3 autophagosome assembly evidence transfers cleanly across the Vps34 clade. RGD:620899 SUPPORTS TRANSFER Rat Pik3c3 autophagosome assembly evidence transfers cleanly across the Vps34 clade. UniProtKB:Q8NEB9 SUPPORTS TRANSFER Human PIK3C3 autophagosome assembly evidence transfers cleanly across the Vps34 clade. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. PMID:31941401 We revealed that the Atg38-Atg8 interaction establishes a positive feedback loop between Atg8 and the PtdIns3K complex I to facilitate autophagosome formation. |
| GO:0000407 phagophore assembly site | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; complex I is recruited to the PAS. Reason: In S. pombe, PtdIns3K complex I containing Pik3/Vps34 is recruited to the phagophore assembly site and interacts with Atg8 via Atg38 to promote autophagosome formation (PMID:31941401). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K clade node; phagophore assembly site recruitment of PtdIns3K complex I is conserved across yeasts. SGD:S000004230 SUPPORTS TRANSFER S. cerevisiae Vps34 PAS localization transfers cleanly to S. pombe Pik3 in complex I. Supporting Evidence: PMID:31941401 We revealed that the Atg38-Atg8 interaction establishes a positive feedback loop between Atg8 and the PtdIns3K complex I to facilitate autophagosome formation. |
| GO:0000425 pexophagy | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT inference from S. cerevisiae Vps34 in pexophagy; selective autophagy depends on complex I, but pexophagy is not studied in S. pombe. Reason: PtdIns3K complex I is required for core autophagosome biogenesis across selective and bulk autophagy pathways, so a contribution to pexophagy is evolutionarily plausible from S. cerevisiae Vps34, but pexophagy has not been directly assayed in S. pombe; kept as non-core, matching the worm vps-34 review. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K clade node; selective autophagy pathways require Vps34-generated PI3P, retained as a non-core downstream context. SGD:S000004230 SUPPORTS TRANSFER S. cerevisiae Vps34 pexophagy evidence supports a plausible non-core selective-autophagy role. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0005515 protein binding | IPI PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | REMOVE | Summary: IPI with a PtdIns3K complex subunit. Generic protein binding carries no functional information; the interaction itself is not in doubt and is captured in the complex membership and description. Reason: Uninformative generic protein-binding term. Supporting Evidence: PMID:31941401 Furthermore, Vps34, Vps15, Atg6, and Atg14, but not Vps38, a complex II-specific subunit, were co-purified with SPBC660. |
| GO:0005515 protein binding | IPI PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | REMOVE | Summary: IPI with a PtdIns3K complex subunit. Generic protein binding carries no functional information; the interaction itself is not in doubt and is captured in the complex membership and description. Reason: Uninformative generic protein-binding term. Supporting Evidence: PMID:31941401 Furthermore, Vps34, Vps15, Atg6, and Atg14, but not Vps38, a complex II-specific subunit, were co-purified with SPBC660. |
| GO:0005515 protein binding | IPI PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | REMOVE | Summary: IPI with a PtdIns3K complex subunit. Generic protein binding carries no functional information; the interaction itself is not in doubt and is captured in the complex membership and description. Reason: Uninformative generic protein-binding term. Supporting Evidence: PMID:31941401 Furthermore, Vps34, Vps15, Atg6, and Atg14, but not Vps38, a complex II-specific subunit, were co-purified with SPBC660. |
| GO:0005737 cytoplasm | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: Cytoplasmic signal in the ORFeome screen. Reason: Direct high-throughput YFP localization in S. pombe places Pik3 in the cytoplasm (PMID:16823372), consistent with a peripheral lipid kinase recruited from the cytosol to endosomal and autophagic membranes. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference of location; agrees with the localisation screen. Reason: Corroborated by the direct S. pombe ORFeome YFP localization in the cytoplasm (PMID:16823372). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005673 SUPPORTS TRANSFER PI3K family node; cytoplasmic localization is conserved and directly corroborated in S. pombe (PMID:16823372). SGD:S000004230 SUPPORTS TRANSFER S. cerevisiae Vps34 cytoplasmic localization supports transfer to S. pombe Pik3. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005768 endosome | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; complex II acts at endosomes for vacuolar protein sorting. Reason: Pik3 is the catalytic subunit of PtdIns3K complex II (with Vps15, Atg6, and Vps38), which acts at endosomes in vacuolar protein sorting (PMID:31941401). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K clade node; endosomal localization and activity of PtdIns3K complex II are conserved in S. pombe. SGD:S000004230 SUPPORTS TRANSFER S. cerevisiae Vps34 endosomal localization transfers cleanly to S. pombe Pik3. UniProtKB:Q8NEB9 SUPPORTS TRANSFER Human PIK3C3 endosomal localization supports eukaryotic conservation. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0005777 peroxisome | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: PAINT inference from S. cerevisiae Vps34 peroxisome association during pexophagy; not shown in S. pombe. Reason: The peroxisome IBA rests solely on S. cerevisiae Vps34 in a pexophagy context. In S. pombe, Pik3 is localized to the cytoplasm/cytosol (PMID:16823372) and acts in PtdIns3K complex I at the phagophore assembly site and complex II in vacuolar protein sorting (PMID:31941401); neither peroxisomal localization nor pexophagy has been demonstrated in fission yeast. Under the root-organelle policy (projects/ORGANELLES.md, rule 3), an unsupported synthesis row on a root organelle term is marked MARK_AS_OVER_ANNOTATED, matching the worm vps-34 review on PTN000005955. Propagation Review Root cause: PROPAGATION BAD Failure modes: CONTEXT OR TISSUE MISMATCH Sources checked: PANTHER:PTN000005955 SUPPORTS SOURCE BUT NOT TARGET Class III PI3K clade node; peroxisomal association reflects a specialized S. cerevisiae pexophagy context not demonstrated for S. pombe Pik3. SGD:S000004230 SUPPORTS SOURCE BUT NOT TARGET S. cerevisiae Vps34 peroxisome annotation is tied to budding-yeast pexophagy and does not establish peroxisomal residence for S. pombe Pik3. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0005829 cytosol | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: ORFeome YFP screen placed pik3 in the cytosol, consistent with a soluble metabolic enzyme. Reason: Direct high-throughput YFP localization in S. pombe places Pik3 in the cytosol (PMID:16823372), where the soluble pool of the lipid kinase resides prior to membrane recruitment. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0006897 endocytosis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT inference of endocytosis; PI3P marks endosomes in the endocytic pathway, but a direct role is not shown in S. pombe. Reason: Pik3-generated PI3P on endosomes supports endosomal maturation and vacuolar protein sorting via PtdIns3K complex II (PMID:31941401), so an endocytic trafficking role is conserved across the Vps34 clade, but in S. pombe the directly characterized roles are vacuolar sorting, autophagy, and forespore membrane formation; kept as non-core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K clade node; endocytic trafficking via endosomal PI3P is conserved and retained as non-core in S. pombe. WB:WBGene00006932 SUPPORTS TRANSFER C. elegans vps-34 endocytic trafficking evidence supports the clade-level inference. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0016020 membrane | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference of membrane association. Reason: S. pombe Pik3/Vps34p and its PI 3-kinase activity fractionate almost exclusively with the crude membrane fraction (PMID:8719881), and the target itself (PomBase:SPAC458.05) is among the experimental seeds of PTN000005673. The annotated organelle terms (GO:0000407 phagophore assembly site and GO:0005768 endosome) are not is_a/part_of descendants of GO:0016020 in GO, and the membrane counterparts GO:0034045 (phagophore assembly site membrane, avoided per the SCHPO/atg2 and GO #29437 precedent because the PAS is a non-membrane-bound condensate) and GO:0010008 (endosome membrane) are not used to replace GO:0016020 because the direct S. pombe fractionation assay (PMID:8719881) did not resolve a specific organelle membrane and Pik3 also acts on the forespore membrane during sporulation (PMID:12557273). Accepted as matching the assay resolution and the IMP row, consistent with the worm vps-34 review. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005673 SUPPORTS TRANSFER PI3K family node; peripheral membrane association is directly supported by S. pombe crude-membrane fractionation (PMID:8719881). PomBase:SPAC458.05 SUPPORTS TRANSFER Target's own experimental membrane fractionation (PMID:8719881) grounds the clade annotation. Supporting Evidence: PMID:8719881 fractionates almost exclusively with the crude membrane fraction |
| GO:0016020 membrane | IMP PMID:8719881 Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-spe... | ACCEPT | Summary: Vps34p and PI 3-kinase activity fractionate with membranes. Reason: Direct biochemical fractionation shows S. pombe Vps34p and its PI 3-kinase activity fractionate almost exclusively with the crude membrane fraction (PMID:8719881), which does not resolve a specific sub-compartment membrane (such as GO:0010008 endosome membrane, while GO:0034045 phagophore assembly site membrane is avoided because the PAS is a non-membrane-bound condensate); accepted as matching the assay resolution. Supporting Evidence: PMID:8719881 fractionates almost exclusively with the crude membrane fraction |
| GO:0016236 macroautophagy | IMP PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | ACCEPT | Summary: PtdIns3K complex I, which contains Vps34, is needed for autophagosome formation in S. pombe. Reason: Pik3/Vps34 is the catalytic subunit of fission yeast PtdIns3K complex I, which facilitates autophagosome formation during macroautophagy through an Atg38-Atg8 positive feedback loop (PMID:31941401). Supporting Evidence: PMID:31941401 We revealed that the Atg38-Atg8 interaction establishes a positive feedback loop between Atg8 and the PtdIns3K complex I to facilitate autophagosome formation. |
| GO:0016236 macroautophagy | NAS PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | ACCEPT | Summary: Author statement; consistent. Reason: Consistent with the experimental demonstration in PMID:31941401 that PtdIns3K complex I containing Vps34 functions in macroautophagy. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0016301 kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: Generic InterPro-derived parent of the specific activity, which is already annotated. Reason: Correct but less specific than the experimentally demonstrated is_a descendant GO:0016303 (1-phosphatidylinositol-3-kinase activity, PMID:8719881), which the gene already carries. Proposed replacements: 1-phosphatidylinositol-3-kinase activity Supporting Evidence: PMID:8719881 Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; consistent with direct assays. Reason: Core catalytic activity of Pik3/Vps34p, directly demonstrated in S. pombe (PMID:8719881) and conserved across the class III PI3K clade (PTN000005955, where PomBase:SPAC458.05 is itself a seed). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K clade node; 1-phosphatidylinositol-3-kinase activity is conserved and directly assayed in S. pombe. PomBase:SPAC458.05 SUPPORTS TRANSFER Target's own IDA (PMID:8719881) is among the experimental seeds of the node. SGD:S000004230 SUPPORTS TRANSFER S. cerevisiae Vps34 lipid kinase activity supports clade-wide conservation. Supporting Evidence: PMID:8719881 Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IDA PMID:8719881 Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-spe... | ACCEPT | Summary: Immunoisolated Vps34p phosphorylates PI on the D-3 position, and PI3K activity is absent in vps34 deletion cells. Reason: Direct biochemical assay of immunoisolated S. pombe Vps34p showing specific phosphorylation of phosphatidylinositol at the D-3 position, abolished in vps34 deletion cells (PMID:8719881). Supporting Evidence: PMID:8719881 Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring PMID:8719881 while wild-type strains exhibit substantial levels of phosphatidylinositol 3-kinase activity, this activity is not detected in the vps34 delta strain |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EC/RHEA mapping; consistent. Reason: Electronic mapping from EC 2.7.1.137 / RHEA:12709 matches the directly assayed 1-phosphatidylinositol-3-kinase activity (PMID:8719881). Supporting Evidence: PMID:8719881 Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring |
| GO:0016303 1-phosphatidylinositol-3-kinase activity | IMP PMID:7772832 Phosphatidylinositol-3 kinase in fission yeast: a possible r... | ACCEPT | Summary: Disruption drastically lowers PI3P. Reason: Gene disruption of pik3 in S. pombe causes extremely low cellular PI3P levels, corroborating the direct biochemical assay of 1-phosphatidylinositol-3-kinase activity (PMID:7772832). Supporting Evidence: PMID:7772832 Disruption of the gene resulted in extremely low levels of PI-3-P and higher levels of PI-4-P, supporting the idea that the gene codes for the PI-3 kinase of S. pombe. |
| GO:0031321 ascospore-type prospore assembly | IMP PMID:12557273 Role of phosphatidylinositol 3-phosphate in formation of for... | ACCEPT | Summary: pik3 deletion spores are inviable, with misoriented forespore membrane growth; an S. pombe-specific role of PI3P. Reason: In pik3 deletion cells, forespore membrane growth is misoriented and spores are inviable, demonstrating a requirement for Pik3-generated PI3P in ascospore-type prospore assembly (PMID:12557273). Supporting Evidence: PMID:12557273 the growth of the forespore membrane of deltapik3 cells was not correctly orientated |
| GO:0032120 ascospore-type prospore membrane formation | IMP PMID:15189449 Sorting nexin homologues are targets of phosphatidylinositol... | ACCEPT | Summary: PI3P effectors Vps5/Vps17 reach the forespore membrane in a pik3-dependent way. Reason: Pik3-generated PI3P recruits the sorting nexin effectors Vps5p and Vps17p to the forespore membrane to support proper forespore membrane formation (PMID:15189449). Supporting Evidence: PMID:15189449 Vps5p and Vps17p migrated toward the the forespore membrane in a pik3+-dependent manner |
| GO:0034271 phosphatidylinositol 3-kinase complex, class III, type I | EXP PMID:34499173 Visual detection of binary, ternary and quaternary protein i... | ACCEPT | Summary: Complex I membership (co-tethering assay). Reason: Direct Pil1 co-tethering assay in S. pombe demonstrates incorporation of Vps34/Pik3 into PtdIns3K complex I via interaction with Atg38 (PMID:34499173). Supporting Evidence: PMID:34499173 incorporated into the PtdIns3K complex I via an Atg38-Vps34 interaction |
| GO:0034271 phosphatidylinositol 3-kinase complex, class III, type I | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; consistent. Reason: Directly supported in S. pombe by co-purification and co-tethering assays (PMID:31941401, PMID:34499173); PomBase:SPAC458.05 is itself an experimental seed of PTN000005955. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K clade node; complex I membership is conserved and directly demonstrated in S. pombe. PomBase:SPAC458.05 SUPPORTS TRANSFER Target's own experimental complex I membership (PMID:31941401) grounds the clade annotation. SGD:S000004230 SUPPORTS TRANSFER S. cerevisiae Vps34 complex I membership supports conservation across yeasts. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0034271 phosphatidylinositol 3-kinase complex, class III, type I | IDA PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | ACCEPT | Summary: Co-purification of Vps34 with complex I subunits. Reason: Direct affinity purification shows S. pombe Vps34, Vps15, Atg6, and Atg14 (but not Vps38) co-purify with Atg38/SPBC660.08 as PtdIns3K complex I (PMID:31941401). Supporting Evidence: PMID:31941401 Furthermore, Vps34, Vps15, Atg6, and Atg14, but not Vps38, a complex II-specific subunit, were co-purified with SPBC660. |
| GO:0034271 phosphatidylinositol 3-kinase complex, class III, type I | NAS PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | ACCEPT | Summary: Author statement; consistent. Reason: Consistent with the co-purification of Vps34 in PtdIns3K complex I reported in PMID:31941401. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | EXP PMID:34499173 Visual detection of binary, ternary and quaternary protein i... | ACCEPT | Summary: Complex II membership (co-tethering assay). Reason: Direct Pil1 co-tethering assay in S. pombe confirms Pik3/Vps34 membership in PtdIns3K complex II with Vps15, Atg6, and Vps38 (PMID:34499173, PMID:31941401). Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; consistent. Reason: Directly supported in S. pombe by complex II subunit interaction assays (PMID:31941401, PMID:34499173); PomBase:SPAC458.05 is itself a seed of PTN000005955. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K clade node; complex II membership is conserved and directly demonstrated in S. pombe. PomBase:SPAC458.05 SUPPORTS TRANSFER Target's own experimental complex II membership grounds the clade annotation. SGD:S000004230 SUPPORTS TRANSFER S. cerevisiae Vps34 complex II membership supports conservation across yeasts. Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | IDA PMID:31941401 Atg38-Atg8 interaction in fission yeast establishes a positi... | ACCEPT | Summary: Complex II membership; consistent. Reason: Direct interaction and complex characterization in S. pombe show Vps34 forms PtdIns3K complex II with Vps15, Atg6, and Vps38 (PMID:31941401). Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0034272 phosphatidylinositol 3-kinase complex, class III, type II | NAS PMID:34499173 Visual detection of binary, ternary and quaternary protein i... | ACCEPT | Summary: Author statement; consistent. Reason: Consistent with the experimental complex II characterization in S. pombe (PMID:31941401, PMID:34499173). Supporting Evidence: PMID:31941401 The former, composed of Vps34, Vps15, Atg6/Vps30, Atg14, and Atg38, functions in autophagy, and the latter, composed of Vps34, Vps15, Atg6, and Vps38, participates in vacuolar protein sorting [31–33]. |
| GO:0036092 phosphatidylinositol-3-phosphate biosynthetic process | EXP PMID:15249580 A novel phosphatidylinositol(3,4,5)P3 pathway in fission yea... | ACCEPT | Summary: vps34p synthesises PI3P but not PI(3,4)P2 or PIP3. Reason: S. pombe Vps34p specifically synthesizes phosphatidylinositol 3-phosphate (PI3P) and does not produce PI(3,4)P2 or PI(3,4,5)P3 (PMID:15249580). Supporting Evidence: PMID:15249580 Unlike the class I enzymes, vps34p synthesizes PI(3)P but not PI(3,4)P2 or PI(3,4,5)P3. |
| GO:0036092 phosphatidylinositol-3-phosphate biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference; consistent. Reason: Core biosynthetic process of Pik3/Vps34p, directly assayed in S. pombe (PMID:8719881, PMID:15249580); PomBase:SPAC458.05 is itself a seed of PTN000005955. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000005955 SUPPORTS TRANSFER Class III PI3K clade node; PI3P biosynthesis is the conserved core process and is directly assayed in S. pombe. PomBase:SPAC458.05 SUPPORTS TRANSFER Target's own IDA (PMID:8719881) grounds the clade annotation. UniProtKB:Q8NEB9 SUPPORTS TRANSFER Human PIK3C3 PI3P biosynthesis evidence supports eukaryotic conservation. Supporting Evidence: PMID:8719881 Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring |
| GO:0036092 phosphatidylinositol-3-phosphate biosynthetic process | IDA PMID:8719881 Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-spe... | ACCEPT | Summary: Direct PI 3-kinase assay. Reason: Direct biochemical assay shows immunoisolated S. pombe Vps34p phosphorylates phosphatidylinositol at the D-3 position to synthesize PI3P (PMID:8719881). Supporting Evidence: PMID:8719881 Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring |
| GO:0046854 phosphatidylinositol phosphate biosynthetic process | IEA GO_REF:0000002 | TOO GENERAL | Summary: Correct but broad parent of PI3P biosynthesis, which is also annotated. Reason: True of Pik3, but uninformative because the specific is_a descendant GO:0036092 (phosphatidylinositol-3-phosphate biosynthetic process) is already annotated by IDA, EXP, and IBA. Supporting Evidence: PMID:8719881 Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring |
| GO:0048015 phosphatidylinositol-mediated signaling | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT inference of PI-mediated signalling; PI3P recruits effectors, but signalling is a loose description of class III PI3K function. Reason: Pik3-generated PI3P acts as a lipid landmark recruiting FYVE/PX/PROPPIN effectors on endosomal, autophagic, and forespore membranes, which fits the broad PI3K-family node (PTN000005673), but class III PI3K function is primarily membrane trafficking and autophagosome biogenesis rather than second-messenger signaling; kept as non-core, matching the worm vps-34 review. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000005673 SUPPORTS TRANSFER PI3K family node; effector recruitment by PI3P fits broadly within phosphoinositide signaling and is retained as non-core. FB:FBgn0015279 SUPPORTS TRANSFER Drosophila PI3K family evidence supports the broad family-level process as non-core. dictyBase:DDB_G0278727 SUPPORTS TRANSFER Dictyostelium PI3K family evidence supports the broad family-level process as non-core. Supporting Evidence: PMID:8719881 Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring |
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