The protein encoded by this gene binds proteins of the TEA domain family of transcription factors (TEFs) through the Vg (vestigial) homology region found in its N-terminus. It may thus function as a specific coactivator for the mammalian TEFs. TDU interacted directly with the TEA domain family member, TEF1, and deletion of the Vg homology region abolished the interaction. The TDU-TEF1 dimer activated a reporter plasmid, and expression of TDU in Drosophila rescued loss of Vg function. The interaction was stronger in cardiac myocytes, suggesting a myocyte-specific factor may participate in the interaction. Vgll1 was weakly active in driving expression of a reporter gene from the mouse skeletal muscle alpha-actin promoter, and Vgll1 could partially reverse the inhibitory effect of TEF1 in this assay.
A synthesized peptide derived from human VGLL2, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human VGLL3.
A synthesized peptide derived from human VGLL4.
A synthesized peptide derived from human VGluT1, corresponding to a region within C-terminal amino acids.
A synthetic peptide from human VGluT1
A synthesized peptide derived from human VGLUT2, corresponding to a region within N-terminal amino acids.
A synthesized peptide derived from human VHL, corresponding to a region within the internal amino acids.
A synthesized peptide derived from human Villin1, corresponding to a region within the internal amino acids.
The protein encoded by this gene belongs to the villin/gelsolin family. It contains 6 gelsolin-like repeats and a headpiece domain. It may play a role in actin-bundling.
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