Fig. 3. Structural features of human NUANCE. (A) The ABD is represented by an empty box; 22 spectrin repeats with considerable homology to dystrophin are shown as filled ovals; and the TMD is indicated by a black bar. The positions of nuclear localization signals and leucine zippers are indicated. Coiled-coil regions were detected by the MultiCoil program (Wolf et al., 1997) with a window size of 21. Blue and red lines mark the location of predicted dimeric or trimeric coiled coils, respectively. (B) Alignment of the ABDs of NUANCE, enaptin, calmin (BAB59010), ß-spectrin (AAA60580) and MACF (AAD32244). NUANCE, enaptin and calmin harbor long stretches between both CH domains unlike conventional ABDs of ß-spectrin and MACF. (C) A phylogenetic tree of the ABDs of NUANCE and other proteins of the -actinin superfamily on the basis of calculations from ClustalW alignment of these domains. The accession numbers are: human filamin (AF184126), human dystrophin (P11532), Dictyostelium cortexillin (L49527), human ß-spectrin (M96803), Drosophila kakapo (AJ011924), Dictyostelium interaptin (AF057019), chicken fimbrin (A37097), mouse -actinin (P12814), human utrophin (P46939), mouse plectin (AF188012), mouse MACF (AF150755), mouse dystonin (AF252549) and human calmin (BAB59010). (D) Klarsicht-like domain of NUANCE. The C-termini of NUANCE, human Syne-1 (KIAA0796 protein, BAA34516), mouse Syne-1 (AAG24392), human lymphocyte membrane associated protein (LMAP, AAC02992), an uncharacterised C. elegans protein similar to myosin-like proteins (AAF40010) and D. melanogaster Klarsicht protein (AAD43129) are aligned with ClustalW version 4.2. The amino acids similar in more than 40% of the sequences are shaded. Three parts of the Klarsicht-like domain are marked. (E) Alignment of 22 selected spectrin repeats of human NUANCE. The multiple alignment was made using the CLUSTAL W program (EMBL). The bars indicate positions of three helices according to the structure-based alignment of Winder and colleagues (Winder et al., 1995).

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