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. 2017 May 9;112(9):1742–1760. doi: 10.1016/j.bpj.2017.03.034

Figure 1.

Figure 1

Tmod and Lmod isoforms. Sequence alignment of the four Tmod and three Lmod human isoforms is given. Amino acid conservation decreases from blue to white backgrounds. UniProt accession codes: hTmod1, P28289; hTmod2, Q9NZR1; hTmod3, Q9NYL9; hTmod4, Q9NZQ9; hLmod1, P29536; hLmod2, Q6P5Q4; hLmod3, Q0VAK6. Boxed regions include TM-binding sites 1 and 2 (TMBS1 and TMBS2, light green), actin-binding sites 1 and 2 (ABS1 and ABS2, magenta), proline-rich domain (PRD, cyan), and the WASP-Homology 2 domain (WH2, red). The region of Tmod that interacts with the DNase I-binding loop (D-loop) of actin, called here the D-loop-binding site (DBS), is highlighted inside an orange box. Note that Lmods lack TMBS2, DBS, and part of ABS1, whereas Tmods lack the PRD- and WH2-containing C-terminal extension. However, a recent study (41) suggests that ABS1 is N-terminally shifted in Lmods compared to Tmods (corresponding to human Lmod2 residues D43–E90, contoured magenta). Fig. S1 extends this alignment to other organisms. To see this figure in color, go online.