MAFB_MACFA
ID MAFB_MACFA Reviewed; 323 AA.
AC Q2PFS4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Transcription factor MafB;
DE Short=Maf-B;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog B;
GN Name=MAFB; ORFNames=QnpA-17255;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA Hashimoto K.;
RT "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT oligo-chips.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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. Binds DNA as a homodimer or a heterodimer. Forms homodimers
CC and heterodimers with FOS, FOSB and FOSL2, but not with JUN proteins
CC (JUN, JUNB and JUND). Interacts with PAX6; the interaction is direct.
CC Interacts with ETS1 and LRP1. Interacts with the intracellular
CC cytoplasmic domain of LRP1 (LRPICD); the interaction results in a
CC moderate reduction of MAFB transcriptional potential (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- DOMAIN: The leucine-zipper domain is involved in the interaction with
CC LRPICD. {ECO:0000250}.
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; AB220513; BAE73046.1; -; mRNA.
DR RefSeq; NP_001306451.1; NM_001319522.1.
DR AlphaFoldDB; Q2PFS4; -.
DR SMR; Q2PFS4; -.
DR STRING; 9541.XP_005569058.1; -.
DR PRIDE; Q2PFS4; -.
DR GeneID; 102136706; -.
DR CTD; 9935; -.
DR eggNOG; KOG4196; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0021599; P:abducens nerve formation; ISS:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
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 2: Evidence at transcript 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_0000366122"
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..210
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; 35780 MW; AB881A9F8E756017 CRC64;
MAAELSMGPE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ PAGSLSSTPL
STPCSSVPSS PSFSPTEQKT HLEDLYWMAS NYQQMNPEAL NLTPEDAVEA LIGSHPVPQP
LQSFDSFRGA HHHHHHHHPH PHHAYPGAGV AHDELGPHAH PHHHHHHQAS PPPSSAASPA
QQLPTSHPGP GPHATASATA AGGNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK
QKRRTLKNRG YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAHKVKCEK
LANSGFREAG STSDSPSSPE FFL
