Figure 2

Patatin domain amino acid sequence alignment of chicken PNPLAs. Chicken patatin domains were aligned using ClustalW2. Overall, the sequences show little conservation. The active-site motifs, however, are well conserved (shown in red, as in Figure 1). The lipase consensus motif with the catalytic serine, GXSXG, is fully conserved. In addition, the active site aspartate is fully conserved within the consensus DGG-motif. These catalytic dyad residues are indicated by triangles. The valine in the oxyanion hole (the consensus sequence of the motif, (G/A)XGXXG, is indicated by the superscript rectangle) of chicken PNPLA1 corresponds to a serine in the human ortholog. The non-conserved serine (instead of glycine) of the PNPLA4-oxyanion hole is also present in the rat ortholog. The unidentified N-terminal part of PNPLA3 is indicated with blanks. Identical amino acids in all 8 proteins are marked with an asterisk (*), conservative substitutions with a colon (:), and semi-conservative substitutions with a period (.).