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Figure 3 | Journal of Biology

Figure 3

From: The short coiled-coil domain-containing protein UNC-69 cooperates with UNC-76 to regulate axonal outgrowth and normal presynaptic organization in Caenorhabditis elegans

Figure 3

UNC-69 is homologous to mammalian SCOCO. (a) Sequence alignment of UNC-69/SCOCO proteins from S. cerevisiae, C. elegans, C. briggsae, mosquito, Drosophila, Fugu, zebrafish, Xenopus, mouse and human. Residues identical in all ten sequences are shaded black; similar residues are shaded gray. The underlined region is predicted in all cases to form a coiled-coil domain. The region boxed in green is acidic, and the region boxed in red is serine/threonine-rich. The bracket indicates the carboxy-terminal basic region. Asterisks mark mutations in unc-69. (b) mRNA of the human unc-69 homolog SCOCO is enriched in fetal brain and is also present in fetal kidney, liver and lung. (c) Expression of human SCOCO rescues the locomotion defect of unc-69 mutant. Movement of the wild type (WT), mutants, and transgenic L4-stage hermaphrodites was scored as complete sine waves per minute. For each genotype n = 10. Error bars represent the standard error of the mean.

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