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Q8CF90 (MAFA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor MafA
Alternative name(s):
Pancreatic beta-cell-specific transcriptional activator
V-maf musculoaponeurotic fibrosarcoma oncogene homolog A
Gene names
Name:Mafa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence 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 a 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Transcription factor MafA
PRO_0000320275

Regions

Domain260 – 32364bZIP
Region260 – 28526Basic motif
Region266 – 28015Interaction with DNA By similarity
Region288 – 30922Leucine-zipper
Compositional bias74 – 8310Poly-Gly
Compositional bias145 – 22682His-rich

Amino acid modifications

Modified residue141Phosphoserine; by MAPK1 By similarity
Modified residue491Phosphoserine; by GSK3 By similarity
Modified residue531Phosphothreonine; by GSK3 By similarity
Modified residue571Phosphothreonine; by GSK3 By similarity
Modified residue611Phosphoserine; by GSK3 By similarity
Modified residue651Phosphoserine; by MAPK1 By similarity

Experimental info

Mutagenesis141S → A: Reduces phosphorylation. Ref.8
Mutagenesis651S → A: Reduces phosphorylation. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q8CF90 [UniParc].

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

FASTA35937,576
        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 

« Hide

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.
RefSeqNP_919331.1. NM_194350.1.
UniGeneMm.309589.

3D structure databases

ProteinModelPortalQ8CF90.
SMRQ8CF90. Positions 232-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid237545. 1 interaction.
STRING10090.ENSMUSP00000054226.

PTM databases

PhosphoSiteQ8CF90.

Proteomic databases

PaxDbQ8CF90.
PRIDEQ8CF90.

Protocols and materials databases

DNASU378435.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062002; ENSMUSP00000054226; ENSMUSG00000047591.
GeneID378435.
KEGGmmu:378435.
UCSCuc007whe.1. mouse.

Organism-specific databases

CTD389692.
MGIMGI:2673307. Mafa.

Phylogenomic databases

eggNOGNOG241084.
GeneTreeENSGT00550000074549.
HOGENOMHOG000261683.
HOVERGENHBG000313.
InParanoidQ8CF90.
KOK07595.
OMAQRHILES.
OrthoDBEOG7BGHMQ.
PhylomeDBQ8CF90.
TreeFamTF325689.

Gene expression databases

BgeeQ8CF90.
GenevestigatorQ8CF90.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028562. MafA.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF13. PTHR10129:SF13. 1 hit.
PfamPF03131. bZIP_Maf. 1 hit.
PF08383. Maf_N. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio400973.
PROQ8CF90.
SOURCESearch...

Entry information

Entry nameMAFA_MOUSE
AccessionPrimary (citable) accession number: Q8CF90
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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