Transcription factor MafA - Mus musculus (Mouse)

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Q8CF90 (MAFA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transcription factor MafA

Alternative name(s):
Pancreatic beta-cell-specific transcriptional activator
V-maf musculoaponeurotic fibrosarcoma oncogene homolog A

Gene names

Name:

Mafa

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a transcriptional factor. Specifically binds the insulin enhancer element RIPE3b. Cooperates synergistically with NEUROD1 and PDX1. Phosphorylation by GSK3 increases its transcriptional activity and is required for its oncogenic activity By similarity. Regulates the insulin gene transcription. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Ref.3 Ref.4 Ref.9
Subunit structure	Binds DNA as a homodimer By similarity. Interacts with PCAF By similarity. Interacts with NEUROD1 and PDX1. Ref.6
Subcellular location	Nucleus. Note: Detected in nuclei of pancreas islet beta cells. Ref.4
Tissue specificity	Selectively expressed in pancreatic beta but not in alpha cells (at protein level). Expressed in eyes and at low levels in thymus. Expressed in brain, lung, spleen and kidney. Expressed in embryo. Ref.1 Ref.2 Ref.3
Developmental stage	Expressed on E14. During fetal period (12.5 dpc) detected in each formed somite and expression appears to be in the myotomal cells. Also expressed in the head neural tube and liver cells. Expressed at low levels some mesenchyme-like cells. Ref.2 Ref.3
Post-translational modification	Ubiquitinated, leading to its degradation by the proteasome By similarity. Phosphorylation by GSK3 requires prior phosphorylation of Ser-65 by another kinase. Phosphorylation proceeds then from Ser-61 to Thr-57, Thr-53 and Ser-49. GSK3-mediated phosphorylation increases its transcriptional activity through the recruitment of the coactivator PCAF, is required for its transforming activity and leads to its degradation through an ubiquitin/proteasome-dependent pathway By similarity. Ser-14 and Ser-65 appear to be the major phosphorylation sites. Phosphorylated by MAPK13 on serine and threonine residues Probable. Ref.5 Ref.8
Disruption phenotype	Mice show a normal pancreatic morphology at birth, but after birth a reduction in the proportion of beta-cells with resulting impaired glucose tolerance and diabetes. Ref.7
Sequence similarities	Belongs to the bZIP family. Maf subfamily. Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Disease	Proto-oncogene Tumor suppressor
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	insulin secretion Inferred from electronic annotation. Source: Compara nitric oxide mediated signal transduction Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.4 PubMed 16890542. Source: MGI response to glucose stimulus Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 359

359

Transcription factor MafA

PRO_0000320275

Regions

Domain

260 – 323

bZIP

Region

260 – 285

Basic motif By similarity

Region

288 – 309

Leucine-zipper By similarity

Compositional bias

74 – 83

Poly-Gly

Compositional bias

145 – 226

His-rich

Amino acid modifications

Modified residue

Phosphoserine; by MAPK1 By similarity

Modified residue

Phosphoserine; by GSK3 By similarity

Modified residue

Phosphothreonine; by GSK3 By similarity

Modified residue

Phosphothreonine; by GSK3 By similarity

Modified residue

Phosphoserine; by GSK3 By similarity

Modified residue

Phosphoserine; by MAPK1 By similarity

Experimental info

Mutagenesis

S → A: Reduces phosphorylation. Ref.8

Mutagenesis

S → A: Reduces phosphorylation. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

Q8CF90 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: B10BC396218AB8A5
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FASTA

359

37,576

        10         20         30         40         50         60 
MAAELAMGAE LPSSPLAIEY VNDFDLMKFE VKKEPPEAER FCHRLPPGSL SSTPLSTPCS 

        70         80         90        100        110        120 
SVPSSPSFCA PSPGTGGGAG GGGSAAQAGG APGPPSGGPG TVGGASGKAV LEDLYWMSGY 

       130        140        150        160        170        180 
QHHLNPEALN LTPEDAVEAL IGSGHHGAHH GAHHPAAAAA YEAFRGQSFA GGGGADDMGA 

       190        200        210        220        230        240 
GHHHGAHHTA HHHHSAHHHH HHHHHHGGSG HHGGGAGHGG GGAGHHVRLE ERFSDDQLVS 

       250        260        270        280        290        300 
MSVRELNRQL RGFSKEEVIR LKQKRRTLKN RGYAQSCRFK RVQQRHILES EKCQLQSQVE 

       310        320        330        340        350 
QLKLEVGRLA KERDLYKEKY EKLAGRGGPG GAGGAGFPRE PSPAQAGPGA AKGAPDFFL

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References

[1]	"MafA is a glucose-regulated and pancreatic beta-cell-specific transcriptional activator for the insulin gene." Kataoka K., Han S.I., Shioda S., Hirai M., Nishizawa M., Handa H. J. Biol. Chem. 277:49903-49910(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[2]	"Identification of beta-cell-specific insulin gene transcription factor RIPE3b1 as mammalian MafA." Olbrot M., Rud J., Moss L.G., Sharma A. Proc. Natl. Acad. Sci. U.S.A. 99:6737-6742(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[3]	"Mouse MafA, homologue of zebrafish somite Maf 1, contributes to the specific transcriptional activity through the insulin promoter." Kajihara M., Sone H., Amemiya M., Katoh Y., Isogai M., Shimano H., Yamada N., Takahashi S. Biochem. Biophys. Res. Commun. 312:831-842(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[4]	"Members of the large Maf transcription family regulate insulin gene transcription in islet beta cells." Matsuoka T.A., Zhao L., Artner I., Jarrett H.W., Friedman D., Means A., Stein R. Mol. Cell. Biol. 23:6049-6062(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"MafA transcription factor is phosphorylated by p38 MAP kinase." Sii-Felice K., Pouponnot C., Gillet S., Lecoin L., Girault J.-A., Eychene A., Felder-Schmittbuhl M.-P. FEBS Lett. 579:3547-3554(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[6]	"The islet beta cell-enriched MafA activator is a key regulator of insulin gene transcription." Zhao L., Guo M., Matsuoka T.A., Hagman D.K., Parazzoli S.D., Poitout V., Stein R. J. Biol. Chem. 280:11887-11894(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NEUROD1 AND PDX1.
[7]	"MafA is a key regulator of glucose-stimulated insulin secretion." Zhang C., Moriguchi T., Kajihara M., Esaki R., Harada A., Shimohata H., Oishi H., Hamada M., Morito N., Hasegawa K., Kudo T., Engel J.D., Yamamoto M., Takahashi S. Mol. Cell. Biol. 25:4969-4976(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[8]	"GSK-3-mediated phosphorylation enhances Maf-transforming activity." Rocques N., Abou Zeid N., Sii-Felice K., Lecoin L., Felder-Schmittbuhl M.-P., Eychene A., Pouponnot C. Mol. Cell 28:584-597(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-14 AND SER-65, MUTAGENESIS OF SER-14 AND SER-65.
[9]	"A new MAFia in cancer." Eychene A., Rocques N., Pouponnot C. Nat. Rev. Cancer 8:683-693(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB086961 Genomic DNA. Translation: BAC20390.1.
IPI	IPI00229250.
RefSeq	NP_919331.1. NM_194350.1.
UniGene	Mm.309589.
3D structure databases
HSSP	HSSP built from PDB template 1K1V based on UniProtKB O54790.
ProteinModelPortal	Q8CF90.
SMR	Q8CF90. Positions 232-323.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000054226.
PTM databases
PhosphoSite	Q8CF90.
Proteomic databases
PaxDb	Q8CF90.
PRIDE	Q8CF90.
Protocols and materials databases
DNASU	378435.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000062002; ENSMUSP00000054226; ENSMUSG00000047591.
GeneID	378435.
KEGG	mmu:378435.
UCSC	uc007whe.1. mouse.
Organism-specific databases
CTD	389692.
MGI	MGI:2673307. Mafa.
Phylogenomic databases
eggNOG	NOG241084.
GeneTree	ENSGT00550000074549.
HOGENOM	HOG000261683.
HOVERGEN	HBG000313.
InParanoid	Q8CF90.
KO	K07595.
OMA	VQQRHML.
OrthoDB	EOG4F1X44.
Gene expression databases
Bgee	Q8CF90.
Genevestigator	Q8CF90.
Family and domain databases
Gene3D	1.10.880.10. 1 hit.
InterPro	IPR004827. bZIP. IPR004826. bZIP_Maf. IPR008917. Euk_TF_DNA-bd. IPR013592. Maf_TF_N. IPR024874. Transciption_factor_Maf. [Graphical view]
PANTHER	PTHR10129. PTHR10129. 1 hit.
Pfam	PF03131. bZIP_Maf. 1 hit. PF08383. Maf_N. 1 hit. [Graphical view]
SMART	SM00338. BRLZ. 1 hit. [Graphical view]
SUPFAM	SSF47454. Euk_transcr_DNA. 1 hit.
PROSITE	PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	400973.
SOURCE	Search...

Entry information

Entry name

MAFA_MOUSE

Accession

Primary (citable) accession number: Q8CF90

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents