# Primary-source excerpts for VTC-4

Retrieved 2026-09-09 from https://pmc.ncbi.nlm.nih.gov/articles/PMC4664880/ (PMID:26453652), Table 1 and Results, “Localization of vacuolar proteins VTC-4, PHO-8, and CPY.” The publication cache is abstract-only; these are separately inspected full-text excerpts.

Table 1 maps vtc-4 to NCU08110 and the S. cerevisiae homolog VTC4. The VTC-4–dsRED/VMA-1–GFP experiment reports “both tagged proteins in the PVCs and the tubular vacuolar network” and also large spherical vacuoles.

Retrieved 2026-09-09 from https://pmc.ncbi.nlm.nih.gov/articles/PMC1751332/ (PMID:17079729), Results on calmodulin binding. Purified central domains of budding-yeast Vtc2, Vtc3 and Vtc4 bind immobilized Cmd1, with Vtc4 residues 183–487 tested: “bound to Cmd1p-Sepharose in the presence and in absence of free Ca2+.” This is direct binding by a related Vtc4 central domain, not a target N. crassa assay.

PDB 5IJP (complete entry metadata in vtc-4-PDB-5IJP.json) is a primary structural deposition of the Chaetomium thermophilum Vtc4 SPX domain bound to inositol hexakisphosphate, associated with PMID:27080106. This close filamentous-fungal Vtc4 structure grounds transfer of SPX inositol-phosphate binding; physiological ligand preference is distinct from binding of InsP6.