The MADF (myb/SANT-like domain in Adf-1) domain is an approximately 80-amino-acid module that directs sequence specific DNA binding to a site consisting of multiple tri-nucleotide repeats. The MADF domain is found in one or more copies in eukaryotic and viral proteins and is often associated with the BESS domain [ (PUBMED:12459265) ]. MADF is related to the Myb DNA-binding domain ( IPR001005 ). The retroviral oncogene v-myb, and its cellular counterpart c-myb, are nuclear DNA-binding proteins that specifically recognise the sequence YAAC(G/T)G. It is likely that the MADF domain is more closely related to the myb/SANT domain than it is to other HTH domains. Some proteins known to contain a MADF domain are listed below:
Drosophila Adf-1, a transcription factor first identified on the basis of its interaction with the alcohol dehydrogenase promoter but that binds the promoters of a diverse group of genes [ (PUBMED:1731341) ].
Drosophila Dorsal-interacting protein 3 (Dip3), which functions both as an activator to bind DNA in a sequence specific manner and a coactivator to stimulate synergistic activation by Dorsal and Twist [ (PUBMED:9528796) ].
Drosophila Stonewall (Stwl), a putative transcription factor required for maintenance of female germline stem cells as well as oocyte differentiation.
Family alignment:
There are 7635 MADF domains in 6627 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing MADF domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with MADF domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing MADF domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Cloning of Drosophila transcription factor Adf-1 reveals homology to Myboncoproteins.
Proc Natl Acad Sci U S A. 1992; 89: 683-7
Display abstract
The Drosophila sequence-specific DNA binding protein, Adf-1, is capable ofactivating transcription of the alcohol dehydrogenase gene, Adh, and isimplicated in the transcriptional control of other developmentallyregulated genes. We have cloned the cDNA encoding Adf-1 by generatingspecific DNA probes deduced from partial amino acid sequence of theprotein. Several cDNA clones encoding an extended open reading frame wereisolated from a phage lambda library. The complete amino acid sequence ofAdf-1 deduced from the longest cDNA reveals structural similarities to theputative helix-turn-helix DNA binding motif of Myb and Myb-relatedproteins. DNA sequence analysis of genomic clones and Northern blotanalysis of mRNA suggest that Adf-1 is a single-copy gene encoding a1.9-kb transcript. Purified recombinant Adf-1 expressed in Escherichiacoli binds specifically to Adf-1 recognition sites and activatestranscription of a synthetic Adh promoter in vitro in a mannerindistinguishable from the protein purified from Drosophila. Temporallystaged Drosophila embryos immunochemically stained with affinity-purifiedanti-Adf-1 antibodies indicate that Adf-1 protein is not detectable invery early embryos and does not appear to be maternally inherited. Duringlater stages of embryogenesis, Adf-1 appears to be expressed in thenucleus of most somatic cells in the embryo with possibly higherconcentrations found in some tissues.
Purified Drosophila transcription factor, Adh distal factor-1 (Adf-1),binds to sites in several Drosophila promoters and activatestranscription.
J Biol Chem. 1990; 265: 5086-94
Display abstract
Adh distal factor-1 (Adf-1) is a sequence-specific DNA-binding activityoriginally identified in Drosophila tissue culture cells and embryos.Adf-1 binds to upstream recognition elements in each of the two promotersof the Drosophila alcohol dehydrogenase gene (Adh), and binding of Adf-1to the Adh distal promoter site activates transcription. We have carriedout a mutational analysis of the Adh distal promoter using both an invitro transcription assay and a transient transfection assay in Drosophilatissue culture cells, and in both cases find that deletion of sequencesrequired for Adf-1 binding leads to a 3-4-fold drop in transcription. Wehave purified Adf-1 and demonstrate by a sodium dodecyl sulfate-gelrenaturation assay that it is a 34-kDa protein. Purified Adf-1 activatesAdh distal promoter transcription in vitro in a binding site-dependentmanner. DNase I footprint analysis shows that the purified protein bindsnot only to the two previously characterized sites in Adh but also totranscriptional regulatory elements in the dopa decarboxylase (Ddc) andAntennapedia (Antp) P1 promoters. Thus, it appears that Adf-1 may play animportant role not only in the regulation of Adh expression but also inthe transcription of other Drosophila genes as well.
Links (links to other resources describing this domain)
