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PROSITE documentation PDOC00479TEA domain signature and profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00479
The TEA domain is a DNA-binding region of ~80 amino acids that has been named after the two proteins that originally defined the domain: TEF-1 and AbaA. It is also referred to as the ATTS domain because of the 4 proteins first found to harbor this motif (AbaA and TEC1 in yeast, TEF1/TEAD1 in vertebrates and Scalloped in fly). The TEA domain is located toward the amino terminus of eukaryotic transcription factors of the TEA/ATTS family. The consensus DNA sequence bound by an isolated TEA domain is N-[ATG]-G-[ATC]-A-T-N-T; where, N=A, T, C. or G [1,2,3,4].
The TEA domain is composed of a three-helix bundle with a homeodomain fold (see <PDB:2HZD>). It has a folded globular structure made of three α-helices, H1, H2, and H3. H1 and H2 are nearly anti-parallel and pack on either side of the H3, which is the DNA-recognition helix of the TEA domain. Two conserved serines are found on the DNA-binding surface. Phosphorylation of one or both of these could interfere with DNA-binding activity, by introducing electrostatic repulsion and/or steric hindrance, and help regulate TEA/ATTS transcription factor activity [3,4].
Some of the proteins that contain a TEA domain are listed below:
- Mammalian enhancer factor TEF-1. TEF-1 can bind to two distinct sequences in the SV40 enhancer and is a transcriptional activator.
- Mammalian TEF-3, TEF-4 and TEF-5 [5], putative transcriptional activators highly similar to TEF-1.
- Drosophila scalloped protein (gene sd), a probable transcription factor that functions in the regulation of cell-specific gene expression during Drosophila development, particularly in the differentiation of the nervous system [6].
- Emericella nidulans regulatory protein abaA. AbaA is involved in the regulation of conidiation (asexual spore); its expression leads to the cessation of vegetative growth.
- Yeast trans-acting factor TEC1. TEC1 is involved in the activation of the Ty1 retrotransposon.
- Caenorhabditis elegans hypothetical protein F28B12.2.
We developed both a pattern and a profile. The pattern covers helices H2 and H3, whereas the profile covers the whole domain.
Last update:January 2017 / Profile and text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Buerglin T.R. |
| Title | The TEA domain: a novel, highly conserved DNA-binding motif. | |
| Source | Cell 66:11-12(1991). | |
| PubMed ID | 2070413 |
| 2 | Authors | Hwang J.J. Chambon P. Davidson I. |
| Title | Characterization of the transcription activation function and the DNA binding domain of transcriptional enhancer factor-1. | |
| Source | EMBO J. 12:2337-2348(1993). | |
| PubMed ID | 8389695 |
| 3 | Authors | Anbanandam A. Albarado D.C. Nguyen C.T. Halder G. Gao X. Veeraraghavan S. |
| Title | Insights into transcription enhancer factor 1 (TEF-1) activity from the solution structure of the TEA domain. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 103:17225-17230(2006). | |
| PubMed ID | 17085591 | |
| DOI | 10.1073/pnas.0607171103 |
| 4 | Authors | Landin-Malt A. Benhaddou A. Zider A. Flagiello D. |
| Title | An evolutionary, structural and functional overview of the mammalian TEAD1 and TEAD2 transcription factors. | |
| Source | Gene 591:292-303(2016). | |
| PubMed ID | 27421669 | |
| DOI | 10.1016/j.gene.2016.07.028 |
| 5 | Authors | Jacquemin P. Hwang J.-J. Martial J.A. Dolle P. Davidson I. |
| Title | A novel family of developmentally regulated mammalian transcription factors containing the TEA/ATTS DNA binding domain. | |
| Source | J. Biol. Chem. 271:21775-21785(1996). | |
| PubMed ID | 8702974 |
| 6 | Authors | Campbell S. Inamdar M. Rodrigues V. Raghavan V. Palazzolo M. Chovnick A. |
| Title | The scalloped gene encodes a novel, evolutionarily conserved transcription factor required for sensory organ differentiation in Drosophila. | |
| Source | Genes Dev. 6:367-379(1992). | |
| PubMed ID | 1547938 |
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