Extended Data Fig. 4: C11orf53, COLCA2, and OCA-B share a conserved peptide that corresponds the known binding site of OCA-B with POU2F1/OCT1.
From: OCA-T1 and OCA-T2 are coactivators of POU2F3 in the tuft cell lineage
(a) and (c) Predicted intrinsic disorder for C11orf53 and COLCA2. PONDR (Predictor of Natural Disordered Regions) VLXT scores and IUPred2A (Intrinsically Unstructured Proteins Prediction) scores are shown on the y axis, and the amino acid positions are shown on the x axis. (b) and (d) The conservation analysis of C11orf53 and COLCA2 protein sequences across species with Bayesian method on ConSurf Server. The purple region is the conserved peptide (residues 10–32 for C11orf53 and 5–27 for COLCA2). (e) C11orf53, COLCA2, and Pou2af1/OCA-B gene cluster in the mouse genome (mm10). (f) Architecture and conservation of POU homeodomains of POU2F1/OCT1, POU2F2/OCT2, and POU2F3/OCT11. (g) Summary of residues involved in protein-DNA and protein-protein close contacts (<4.0 Å) for OCA-B with POU2F1, C11orf53 with POU2F3, and COLCA2 with POU2F3. The crystal structure of OCA-B1–44 and POU2F1DBD (PDB: 1CQT25)25 was used as a model for predicting the structure of C11orf53 or COLCA2 with POU2F3DBD on an octamer motif (ATGCAAAT) in PyMOL.
