Xenbase Image ID: 136084

Figure 1. Alignment of ASH3a and ASH3b proteins to each other and to other members of the achaete-scute bHLH subfamily. Regions of sequence similarity between the vertebrate ASH1/ASH3 proteins and the Drosophila AS-C proteins are shaded. The bHLH domain of ASH3a/b has 65-71% amino acid identity with the bHLH domains of the Drosophila AS-C proteins (excluding the size difference in the loops), and 78% {ASH3b) or 82% (ASH3a) identity with the Xenopus ASHla bHLH domain. In addition to the bHLH domain, all of these proteins have a related sequence at the carboxyl terminus, within a larger acidic region. ASH3b appears to have a second version of this sequence that is most similar to achaete (ac, underlined). The carboxyl terminus of the Drosophila AS-C proteins has been suggested to be a regulatory site (Villares and Cabrera 1987). Limited sequence similarity is also present aminoterminal to the basic region in the vertebrate proteins and lethal of scute (l'sc). (sc) Scute. Sources for sequences: ac and sc (Villares and Cabrera 1987); l'sc (Alonso and Cabrera 1988); MASH1 (Johnson et al. 1990); and ASHla (Ferreiro et al. 1992). Image published in: Turner DL and Weintraub H (1994) Copyright © 1994. Image reproduced on with permission of the Publisher, Cold Spring Harbor Laboratory Press. This is an Open Access article. Larger Image Printer Friendly View

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