Summary: bZIP Maf transcription factor
This is the Wikipedia entry entitled "BZIP Maf". More...
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BZIP Maf Edit Wikipedia article
|This article relies largely or entirely upon a single source. (July 2011)|
Crystal structure of the MafA homodimer bound to DNA. PDB entry 
bZIP Maf is a domain found in Maf transcription factor proteins. It contains a leucine zipper (bZIP) domain, which mediates the transcription factor's dimerization and DNA binding properties. The Maf extended homology region (EHR) is present at the N-terminus of the protein. This region (shown in yellow in the image to the right) exists only within the Maf family and allows the family to recognize longer DNA motifs than other leucine zippers. These motifs are termed the Maf recognition element (MARE) and is 13 or 14 base pairs long. In particular, the two residues at the beginning of helix H2 are positioned to recognise the flanking region of the DNA. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF2-E2 transcription factor.
In mouse, Maf1 may play an early role in axial patterning. Defects in these proteins are a cause of autosomal dominant retinitis pigmentosa. Neural retina-specific leucine zipper proteins belong to this family.
- Kurokawa, H.; Motohashi, H.; Sueno, S.; Kimura, M.; Takagawa, H.; Kanno, Y.; Yamamoto, M.; Tanaka, T. (2009). "Structural Basis of Alternative DNA Recognition by Maf Transcription Factors". Molecular and Cellular Biology 29 (23): 6232–6244. doi:10.1128/MCB.00708-09. PMC 2786689. PMID 19797082.
- Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T (April 2002). "Solution structure of the DNA-binding domain of MafG". Nat. Struct. Biol. 9 (4): 252–6. doi:10.1038/nsb771. PMID 11875518.
bZIP Maf transcription factor Provide feedback
Maf transcription factors contain a conserved basic region leucine zipper (bZIP) domain, which mediates their dimerisation and DNA binding property . Thus, this family is probably related to PF00170. This family also includes the DNA_binding domain of Skn-1 (P34707), this domain lacks the leucine zipper found in other bZip domains, and binds DNA is a monomer [2,3].
Benkhelifa S, Provot S, Nabais E, Eychene A, Calothy G, Felder-Schmittbuhl MP; , Mol Cell Biol 2001;21:4441-4452.: Phosphorylation of mafa is essential for its transcriptional and biological properties. PUBMED:11416124 EPMC:11416124
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004826
Maf transcription factors contain a conserved basic region leucine zipper (bZIP) domain, which mediates their dimerisation and DNA binding property [PUBMED:11416124]. This entry also includes the DNA binding domain of Skn-1 (SWISSPROT); this domain lacks the leucine zipper found in other bZip domains, and binds DNA as a monomer [PUBMED:7939715, PUBMED:9628487].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||nucleus (GO:0005634)|
|Molecular function||DNA binding (GO:0003677)|
|Biological process||regulation of transcription, DNA-templated (GO:0006355)|
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_482 (release 6.5)|
|Author:||Mifsud W, Eberhardt R|
|Number in seed:||15|
|Number in full:||1411|
|Average length of the domain:||90.20 aa|
|Average identity of full alignment:||35 %|
|Average coverage of the sequence by the domain:||20.51 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the bZIP_Maf domain has been found. There are 15 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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