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Transcription factor MafB (Maf-B) (Transcription factor Maf-1) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog B)

 MAFB_RAT                Reviewed;         323 AA.
P54842;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
20-JUN-2018, entry version 133.
RecName: Full=Transcription factor MafB;
Short=Maf-B;
AltName: Full=Transcription factor Maf-1;
AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog B;
Name=Mafb; Synonyms=Maf1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
STRAIN=Wistar; TISSUE=Liver;
PubMed=9038383; DOI=10.1038/sj.onc.1200869;
Sakai M., Imaki J., Yoshida K., Ogata A., Matsushima-Hibaya Y.,
Kuboki Y., Nishizawa M., Nishi S.;
"Rat maf related genes: specific expression in chondrocytes, lens and
spinal cord.";
Oncogene 14:745-750(1997).
[2]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9375588;
Yoshida K., Imaki J., Koyama Y., Harada T., Shinmei Y., Oishi C.,
Matsushima-Hibiya Y., Matsuda A., Nishi S., Matsuda H., Sakai M.;
"Differential expression of maf-1 and maf-2 genes in the developing
rat lens.";
Invest. Ophthalmol. Vis. Sci. 38:2679-2683(1997).
[3]
DIMERIZATION, AND DNA-BINDING.
PubMed=9571165; DOI=10.1006/bbrc.1998.8447;
Matsushima-Hibiya Y., Nishi S., Sakai M.;
"Rat maf-related factors: the specificities of DNA binding and
heterodimer formation.";
Biochem. Biophys. Res. Commun. 245:412-418(1998).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Acts as a transcriptional activator or repressor. Plays
a pivotal role in regulating lineage-specific hematopoiesis by
repressing ETS1-mediated transcription of erythroid-specific genes
in myeloid cells. Required for monocytic, macrophage, osteoclast,
podocyte and islet beta cell differentiation. Involved in renal
tubule survival and F4/80 maturation. Activates the insulin and
glucagon promoters. Together with PAX6, transactivates weakly the
glucagon gene promoter through the G1 element. SUMO modification
controls its transcriptional activity and ability to specify
macrophage fate. Binds element G1 on the glucagon promoter.
Involved either as an oncogene or as a tumor suppressor, depending
on the cell context (By similarity).
{ECO:0000250|UniProtKB:P54841, ECO:0000250|UniProtKB:Q9Y5Q3}.
-!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip
transcription factors. Forms homodimers and heterodimers with FOS,
FOSB and FOSL2, but not with JUN proteins (JUN, JUNB and JUND).
Binds DNA as a homodimer or a heterodimer. Interacts with the
intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction
results in a moderate reduction of MAFB transcriptional potential.
Interacts with PAX6; the interaction is direct. Interacts with
ETS1 and LRP1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978, ECO:0000269|PubMed:9038383}.
-!- TISSUE SPECIFICITY: Expressed at low levels in a variety of
tissues, including liver, muscle and spleen. Strongly expressed in
hypertrophic chondrocytes of the femur epiphysis, while expression
is very weak in immature proliferating chondrocytes (at protein
level). {ECO:0000269|PubMed:9038383, ECO:0000269|PubMed:9375588}.
-!- DEVELOPMENTAL STAGE: Expressed in the cartilage of ribs and limbs,
in the eyes and spinal cord at 15 dpc (at protein level).
Expressed in the lens epithelium at 13 and 16 dpc; not detected in
the fiber cells of the lens. In the eyes, confined in the equator
of the lens; not detected in the retina at 15 dpc. In spinal cord,
expressed in the ventral part of the dorsal horn and the ventral
horn at 15 dpc. Predominantly expressed in post-mitotic cells.
{ECO:0000269|PubMed:9038383, ECO:0000269|PubMed:9375588}.
-!- DOMAIN: The leucine-zipper domain is involved in the interaction
with LRPICD.
-!- PTM: Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its
transcriptional repression activity and promotes macrophage
differentiation from myeloid progenitors (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. Maf subfamily.
{ECO:0000305}.
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EMBL; U56241; AAB50062.1; -; mRNA.
RefSeq; NP_062189.1; NM_019316.1.
UniGene; Rn.10725; -.
ProteinModelPortal; P54842; -.
SMR; P54842; -.
STRING; 10116.ENSRNOP00000021452; -.
PaxDb; P54842; -.
Ensembl; ENSRNOT00000021452; ENSRNOP00000021452; ENSRNOG00000016037.
GeneID; 54264; -.
KEGG; rno:54264; -.
UCSC; RGD:2982; rat.
CTD; 9935; -.
RGD; 2982; Mafb.
eggNOG; KOG4196; Eukaryota.
eggNOG; ENOG41102C7; LUCA.
GeneTree; ENSGT00550000074549; -.
HOGENOM; HOG000261683; -.
HOVERGEN; HBG000313; -.
InParanoid; P54842; -.
KO; K09036; -.
OMA; CNRLQPQ; -.
OrthoDB; EOG091G0H46; -.
PhylomeDB; P54842; -.
TreeFam; TF325689; -.
PRO; PR:P54842; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000016037; -.
Genevisible; P54842; RN.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:RGD.
GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:RGD.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0021599; P:abducens nerve formation; ISS:UniProtKB.
GO; GO:0035284; P:brain segmentation; IEA:Ensembl.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IEA:Ensembl.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0007585; P:respiratory gaseous exchange; IEA:Ensembl.
GO; GO:0021571; P:rhombomere 5 development; IEA:Ensembl.
GO; GO:0021572; P:rhombomere 6 development; IEA:Ensembl.
GO; GO:0007379; P:segment specification; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR013592; Maf_TF_N.
InterPro; IPR028571; MafB.
InterPro; IPR008917; TF_DNA-bd_sf.
InterPro; IPR024874; Transciption_factor_Maf_fam.
PANTHER; PTHR10129; PTHR10129; 1.
PANTHER; PTHR10129:SF10; PTHR10129:SF10; 1.
Pfam; PF03131; bZIP_Maf; 1.
Pfam; PF08383; Maf_N; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Activator; Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Proto-oncogene; Reference proteome; Repressor; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation.
CHAIN 1 323 Transcription factor MafB.
/FTId=PRO_0000076496.
DOMAIN 238 301 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 238 263 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 266 287 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 131 143 Poly-His.
COMPBIAS 158 167 Poly-His.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 297 297 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
SEQUENCE 323 AA; 35792 MW; 6E386340D1F840A5 CRC64;
MAAELSMGPE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ PAGSVSSTPL
STPCSSVPSS PSFSPTEQKT HLEDLYWMAS NYQQMNPEAL NLTPEDAVEA LIGSHPVPQP
LQSFDGFRSA HHHHHHHHPH PHHGYPGAGV THDELGPHAH PHHHHHHQAS PPPSSAASPA
QQLPTSHPGP GPHAAAAATA AGSNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK
QKRRTLKNRG YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK
LANSGFREAG STSDSPSSPE FFL


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