Fig. 1. Mouse dispatched (Disp) belongs to an emerging family of proteins containing a sterol-sensing domain (SSD). (A) Predicted 1521 amino acids translation product of the Disp gene. The SSD (blue) and the 12 putative transmembrane domains (red) are colored. Transmembrane domain prediction was performed using the TopPred2 program (http://www.sbc.su.se/~erikw/toppred2). (B) Amino acid alignment between SSD-containing proteins. In addition to dispatched, several other major classes of SSD-containing proteins are incorporated in the alignment, including patched 1 (PTC1 in figure), the Hh receptor (Goodrich et al., 1996); the sterol regulatory element-binding protein [SREBP]-cleavage activation protein (SCAP) (Brown and Goldstein, 1999; Goldstein and Brown, 1990); NPC1, a protein affected in the lipid storage disorder Niemann-Pick disease type C1 (Carstea et al., 1997; Loftus et al., 1997); and HMG CoA reductase (HMGCR), a cholesterol biosynthetic enzyme (Gil et al., 1985). Che-14 encodes a C. elegans orthologue of disp and is likely to be involved in apical secretions of proteins (Michaux et al., 2000). KIAA 1742 encodes the Disp-related protein and its function is unknown. Only the SSD domains are shown and conserved amino acid residues are shown in green. Numbers to the right of the genes represent the amino acid positions in the corresponding protein used in the sequence alignment. Sequence alignment was performed using the CLUSTAL W algorithm (Thompson et al., 1994) in the DNASTAR program.

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