MAFB_CHICK
ID MAFB_CHICK Reviewed; 311 AA.
AC Q90888;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Transcription factor MafB;
DE Short=Maf-B;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog B;
GN Name=MAFB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, INTERACTION WITH FOS,
RP SELF-ASSOCIATION, AND TISSUE SPECIFICITY.
RX PubMed=7935473; DOI=10.1128/mcb.14.11.7581-7591.1994;
RA Kataoka K., Fujiwara K.T., Noda M., Nishizawa M.;
RT "MafB,a new Maf family transcription activator that can associate with Maf
RT and Fos but not with Jun.";
RL Mol. Cell. Biol. 14:7581-7591(1994).
RN [2]
RP INTERACTION WITH HOXD12 AND PRRX1.
RX PubMed=11036080; DOI=10.1074/jbc.m007643200;
RA Kataoka K., Yoshitomo-Nakagawa K., Shioda S., Nishizawa M.;
RT "A set of Hox proteins interact with the Maf oncoprotein to inhibit its DNA
RT binding, transactivation, and transforming activities.";
RL J. Biol. Chem. 276:819-826(2001).
RN [3]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=12081646; DOI=10.1046/j.1365-2443.2002.00548.x;
RA Yoshida T., Yasuda K.;
RT "Characterization of the chicken L-Maf, MafB and c-Maf in crystallin gene
RT regulation and lens differentiation.";
RL Genes Cells 7:693-706(2002).
CC -!- FUNCTION: Acts as a transcriptional activator or repressor. Positively
CC regulates the expression of alpha-A crystallin genes during lens fiber
CC cell differentiation. Binds to Maf recognition elements (MARE).
CC {ECO:0000269|PubMed:12081646, ECO:0000269|PubMed:7935473}.
CC -!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription
CC factors (By similarity). Binds DNA as a homodimer or heterodimer. Self-
CC associates; the interaction requires the intact MAFB leucine-zipper
CC domain. Interacts with FOS, HOXD12 and PRRX1. {ECO:0000250,
CC ECO:0000269|PubMed:11036080, ECO:0000269|PubMed:7935473}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, thymus, gut, lung, mesenterium,
CC spleen, kidney, ovary and bursa. {ECO:0000269|PubMed:7935473}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the lens placode at stages 5, 8 and
CC 14. Expressed at stage 18 when the invaginating lens placode closes to
CC form the lens vesicle.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; D28600; BAA05938.1; -; Genomic_DNA.
DR PIR; A56235; A56235.
DR RefSeq; NP_001026023.1; NM_001030852.1.
DR AlphaFoldDB; Q90888; -.
DR SMR; Q90888; -.
DR MINT; Q90888; -.
DR PaxDb; Q90888; -.
DR Ensembl; ENSGALT00000005816; ENSGALP00000055757; ENSGALG00000003670.
DR GeneID; 419173; -.
DR KEGG; gga:419173; -.
DR CTD; 9935; -.
DR VEuPathDB; HostDB:geneid_419173; -.
DR GeneTree; ENSGT00940000160486; -.
DR InParanoid; Q90888; -.
DR OMA; ESHQPLH; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; Q90888; -.
DR PRO; PR:Q90888; -.
DR Proteomes; UP000000539; Chromosome 20.
DR Bgee; ENSGALG00000003670; Expressed in spleen and 10 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
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_0000366123"
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 169..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 35467 MW; DDAE7F698B7D3ABA CRC64;
MAGELSIGAE LPTSPLAMEY VNDFDLMKFD VKKEPLGRND RSGRHCTRLQ PAGSVSSTPI
STPCSSVPSS PSFSPTEQKT HLEDLYWMAN SYQQMNPEAL NLTPEDAVEA LIGSHQVSQQ
LQGFESFRAH HHHHHHHHQH HHQYPAVTHE DLAGSGHPHH HHHHHHQASP TPSTSSSSSQ
QLQTSHQQHP PSSSVEDRFS DDQLVSMSVR ELNRHLRGFT KDEVIRLKQK RRTLKNRGYA
QSCRYKRVQQ KHHLENEKTQ LIQQVEQLKQ EVTRLARERD AYKLKCEKLA SNGFREAGST
SDNPSSPEFF M
