ID   MAFB_COTJA              Reviewed;         311 AA.
AC   Q90370;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Transcription factor MafB;
DE            Short=Maf-B;
GN   Name=MAFB;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ETS1, DNA-BINDING,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=8620536; DOI=10.1016/s0092-8674(00)81081-8;
RA   Sieweke M.H., Tekotte H., Frampton J., Graf T.;
RT   "MafB is an interaction partner and repressor of Ets-1 that inhibits
RT   erythroid differentiation.";
RL   Cell 85:49-60(1996).
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. Binds DNA via its basic region-leucine zipper domain.
CC       {ECO:0000269|PubMed:8620536}.
CC   -!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription
CC       factors. Binds DNA as a homodimer or a heterodimer (By similarity).
CC       Interacts with ETS1. {ECO:0000250, ECO:0000269|PubMed:8620536}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- TISSUE SPECIFICITY: Expressed in bursa, gut, liver, spleen, bone marrow
CC       and brain. {ECO:0000269|PubMed:8620536}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR   EMBL; X96511; CAA65360.1; -; mRNA.
DR   AlphaFoldDB; Q90370; -.
DR   SMR; Q90370; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..311
FT                   /note="Transcription factor MafB"
FT                   /id="PRO_0000366124"
FT   DOMAIN          226..289
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          35..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..251
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          254..275
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        49..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   311 AA;  35476 MW;  7D1F3FA05D5CD683 CRC64;
     MAGELSIGAE LPTSPLAMEY VNDFDLMKFD VKKEPLGRND RSGRHCTRLQ PAGSVSSTPI
     STPCSSVPSS PSFSPTEQKT HLEDLYWMAN SYQQMNPEAL NLTPEDAVEA LIGSHQVSQQ
     LQGFESFRAH HHHHHHHQHH HHQYPAVTHE DLAGSGHPHH HHHHHHHASP TPSTSSSSSQ
     QLQTSHQQHP PSSSVEDRFS DDQLVSMSVR ELNRHLRGFT KDEVIRLKQK RRTLKNRGYA
     QSCRYKRVQQ KHHLENEKTQ LIQQVEQLKQ EVTRLARERD AYKLKCEKLA SNGFREAGST
     SDNPSSPEFF M