Fig. 2

Variant filtering strategy, interactions, and illustration of ACER3 mutations. A Precise prioritization scheme was used to identify the disease-causing variant in each understudied family. B Studying the interaction of tyrosine residue in normal and mutated state revealed that one putative interaction with Thr133 residue is being lost upon the mutation. C The schematic representation of ACER3 protein which is consisted of seven transmembrane domains and several extracellular loops. Two previously reported variants (black) and three novel variants identified in the current study (red) are demonstrated