To access the data, click or select the words “Appendix 4.” The three-dimensional model of the protein with close-up on three missense variants. [A] OTX2 c.278G>C p.(Trp93Ser): Tryptophan is replaced by Serine at position 93. The wild-type and mutant amino acids differ in size, with the mutant residue is smaller, this might lead to loss of interactions. Moreover, the hydrophobicity of the wild-type and mutant residue differs. [B] ATOH7 c.254C>T p.(Ala85Val): Alanine, which is only the residue type found at position 85, is mutated into Valine. First, mutation of a 100% conserved residue is usually damaging for the protein. Second, the wild-type and mutant amino acids differ in size, with the mutant residue bigger, which might lead to bumps. [C]SOX2c.178G>C p.(Ala60Pro): Alanine is replaced by Proline at position 60. First, the wild-type residue is very conserved and based on conservation scores this mutation is probably damaging to the protein. Second, the mutant residue is bigger than the wild-type residue which might lead to bumps. Third, the wild-type residue is located in a region annotated in UniProt to form an α-helix. Proline disrupts an α-helix when not located at one of the first 3 positions of that helix, and in this case can have severe effects on the structure of the protein. Figures [A] and [B] were generated using SWISS-MODEL [15], while the report on the third variant [C] was produced by HOPE [14].