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15  structures 557  species 0  interactions 4031  sequences 55  architectures

Family: bZIP_Maf (PF03131)

Summary: bZIP Maf transcription factor

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This is the Wikipedia entry entitled "BZIP Maf". More...

BZIP Maf Edit Wikipedia article

Crystal structure of the MafA homodimer.png
Crystal structure of the MafA homodimer bound to DNA. PDB entry 3a5t[1]
Symbol bZIP_Maf
Pfam PF03131
Pfam clan CL0018
InterPro IPR004826
SCOP 1k1v

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 adjacent image) 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.[2] 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.


  1. ^ 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 2786689Freely accessible. PMID 19797082. 
  2. ^ 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. 

This article incorporates text from the public domain Pfam and InterPro IPR004826

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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 [1]. 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].

Literature references

  1. 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

  2. Blackwell TK, Bowerman B, Priess JR, Weintraub H;, Science. 1994;266:621-628.: Formation of a monomeric DNA binding domain by Skn-1 bZIP and homeodomain elements. PUBMED:7939715 EPMC:7939715

  3. Rupert PB, Daughdrill GW, Bowerman B, Matthews BW;, Nat Struct Biol. 1998;5:484-491.: A new DNA-binding motif in the Skn-1 binding domain-DNA complex. PUBMED:9628487 EPMC:9628487

Internal database links

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 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan bZIP (CL0018), which has the following description:

This family of eukaryotic transcription factors contain a basic region adjacent to a leucine zipper.

The clan contains the following 3 members:

bZIP_1 bZIP_2 bZIP_Maf


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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Curation and family details

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Seed source: Pfam-B_482 (release 6.5)
Previous IDs: none
Type: Coiled-coil
Sequence Ontology: SO:0001080
Author: Mifsud W , Eberhardt R
Number in seed: 14
Number in full: 4031
Average length of the domain: 90.90 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 19.31 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.7 20.7
Noise cut-off 20.6 20.6
Model length: 92
Family (HMM) version: 19
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Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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 sequence.

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