Extended Data Fig. 5: Sequence alignment of SLC49A family members and identified disease-associated substitutions.
From: Structural basis of lipid head group entry to the Kennedy pathway by FLVCR1

a, Sequence alignment of human FLVCR1 (SLC49A1), human FLVCR2 (SLC49A2), human MFSD7 (SLC49A3), human DIRC2 (SLC49A4) and Drosophila CG1358 performed using Clustal Omega54 and pyBoxshade (https://github.com/mdbaron42/pyBoxshade). Substrate-binding site residues are highlighted by red boxes. Residues whose substitution leads to PCARP or Fowler syndrome are highlighted by blue and green boxes, respectively. b, Structure of choline-bound FLVCR1 (left) and Alphafold2 model of FLVCR2 (right)55 with residues whose mutation leads to PCARP and Fowler syndrome highlighted in blue and green, respectively. FLVCR1 substrate binding site residues and the corresponding residues in FLVCR2 are highlighted in red.