MAFB_RAT
ID MAFB_RAT Reviewed; 323 AA.
AC P54842;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transcription factor MafB;
DE Short=Maf-B;
DE AltName: Full=Transcription factor Maf-1;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog B;
GN Name=Mafb; Synonyms=Maf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=9038383; DOI=10.1038/sj.onc.1200869;
RA Sakai M., Imaki J., Yoshida K., Ogata A., Matsushima-Hibaya Y., Kuboki Y.,
RA Nishizawa M., Nishi S.;
RT "Rat maf related genes: specific expression in chondrocytes, lens and
RT spinal cord.";
RL Oncogene 14:745-750(1997).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9375588;
RA Yoshida K., Imaki J., Koyama Y., Harada T., Shinmei Y., Oishi C.,
RA Matsushima-Hibiya Y., Matsuda A., Nishi S., Matsuda H., Sakai M.;
RT "Differential expression of maf-1 and maf-2 genes in the developing rat
RT lens.";
RL Invest. Ophthalmol. Vis. Sci. 38:2679-2683(1997).
RN [3]
RP DIMERIZATION, AND DNA-BINDING.
RX PubMed=9571165; DOI=10.1006/bbrc.1998.8447;
RA Matsushima-Hibiya Y., Nishi S., Sakai M.;
RT "Rat maf-related factors: the specificities of DNA binding and heterodimer
RT formation.";
RL Biochem. Biophys. Res. Commun. 245:412-418(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as a transcriptional activator or repressor. Plays a
CC pivotal role in regulating lineage-specific hematopoiesis by repressing
CC ETS1-mediated transcription of erythroid-specific genes in myeloid
CC cells. Required for monocytic, macrophage, osteoclast, podocyte and
CC islet beta cell differentiation. Involved in renal tubule survival and
CC F4/80 maturation. Activates the insulin and glucagon promoters.
CC Together with PAX6, transactivates weakly the glucagon gene promoter
CC through the G1 element. SUMO modification controls its transcriptional
CC activity and ability to specify macrophage fate. Binds element G1 on
CC the glucagon promoter. Involved either as an oncogene or as a tumor
CC suppressor, depending on the cell context (By similarity). Required for
CC the transcriptional activation of HOXB3 in the rhombomere r5 in the
CC hindbrain (By similarity). {ECO:0000250|UniProtKB:P54841,
CC ECO:0000250|UniProtKB:Q9Y5Q3}.
CC -!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription
CC factors. Forms homodimers and heterodimers with FOS, FOSB and FOSL2,
CC but not with JUN proteins (JUN, JUNB and JUND). Binds DNA as a
CC homodimer or a heterodimer. Interacts with the intracellular
CC cytoplasmic domain of LRP1 (LRPICD); the interaction results in a
CC moderate reduction of MAFB transcriptional potential. Interacts with
CC PAX6; the interaction is direct. Interacts with ETS1 and LRP1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:9038383}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in a variety of tissues,
CC including liver, muscle and spleen. Strongly expressed in hypertrophic
CC chondrocytes of the femur epiphysis, while expression is very weak in
CC immature proliferating chondrocytes (at protein level).
CC {ECO:0000269|PubMed:9038383, ECO:0000269|PubMed:9375588}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the cartilage of ribs and limbs, in
CC the eyes and spinal cord at 15 dpc (at protein level). Expressed in the
CC lens epithelium at 13 and 16 dpc; not detected in the fiber cells of
CC the lens. In the eyes, confined in the equator of the lens; not
CC detected in the retina at 15 dpc. In spinal cord, expressed in the
CC ventral part of the dorsal horn and the ventral horn at 15 dpc.
CC Predominantly expressed in postmitotic cells.
CC {ECO:0000269|PubMed:9038383, ECO:0000269|PubMed:9375588}.
CC -!- DOMAIN: The leucine-zipper domain is involved in the interaction with
CC LRPICD.
CC -!- PTM: Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its
CC transcriptional repression activity and promotes macrophage
CC differentiation from myeloid progenitors (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; U56241; AAB50062.1; -; mRNA.
DR RefSeq; NP_062189.1; NM_019316.1.
DR AlphaFoldDB; P54842; -.
DR SMR; P54842; -.
DR STRING; 10116.ENSRNOP00000021452; -.
DR PaxDb; P54842; -.
DR Ensembl; ENSRNOT00000021452; ENSRNOP00000021452; ENSRNOG00000016037.
DR GeneID; 54264; -.
DR KEGG; rno:54264; -.
DR UCSC; RGD:2982; rat.
DR CTD; 9935; -.
DR RGD; 2982; Mafb.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000160486; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; P54842; -.
DR OMA; ESHQPLH; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; P54842; -.
DR TreeFam; TF325689; -.
DR PRO; PR:P54842; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000016037; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; P54842; RN.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:RGD.
DR GO; GO:0021599; P:abducens nerve formation; ISS:UniProtKB.
DR GO; GO:0035284; P:brain segmentation; ISO:RGD.
DR GO; GO:1903575; P:cornified envelope assembly; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISO:RGD.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; ISO:RGD.
DR GO; GO:0021571; P:rhombomere 5 development; ISO:RGD.
DR GO; GO:0021572; P:rhombomere 6 development; ISO:RGD.
DR GO; GO:0007379; P:segment specification; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013592; Maf_TF_N.
DR InterPro; IPR028571; MafB.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF10; PTHR10129:SF10; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR Pfam; PF08383; Maf_N; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Proto-oncogene;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..323
FT /note="Transcription factor MafB"
FT /id="PRO_0000076496"
FT DOMAIN 238..301
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 34..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..263
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 266..287
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 50..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ 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
