Figure 1

Family pedigrees, mutation traces and positions of predicted amino acid substitutions in FATP4. Multiple sequence alignment is shown of FATP4 protein with orthologs from different species and with the FATP family of proteins. (a) Pedigrees of three of the five families from which healthy family members were available showing the segregation of mutations and IPS (b) Sequence chromatograms of the five mutations identified (c) Schematic overview of FATP4 functional domains; the N-terminal transmembrane region (TM), the ER localization signal (ERx; aa 47-102), the ATP/AMP motif involved in ATP binding and adenylate formation (ATP/AMP; aa 243-345) and the conserved FATP motif of importance for fatty acid binding (FATP; aa 500-551). The arrows indicate positions of the mutated amino acid residues reported herein associated with IPS (d) Multiple sequence alignment of selected regions of the human FATP4 protein and Fatp4 proteins from mouse and dog. Arrows indicate the position of the missense mutations at conserved residues (e) Multiple sequence alignment of FATP4 protein with the human FATP family of proteins (FATP1, FATP2, FATP3, FATP5, and FATP6). The positions of the missense mutations are indicated by arrows