ID   MAFG_BOVIN              Reviewed;         162 AA.
AC   A5PJV0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Transcription factor MafG;
DE   AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog G;
GN   Name=MAFG;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Since they lack a putative transactivation domain, the small
CC       Mafs behave as transcriptional repressors when they dimerize among
CC       themselves. However, they seem to serve as transcriptional activators
CC       by dimerizing with other (usually larger) basic-zipper proteins, such
CC       as NFE2, NFE2L1 and NFE2L2, and recruiting them to specific DNA-binding
CC       sites. Small Maf proteins heterodimerize with Fos and may act as
CC       competitive repressors of the NFE2L2 transcription factor.
CC       Transcription factor, component of erythroid-specific transcription
CC       factor NFE2L2. Activates globin gene expression when associated with
CC       NFE2L2 (By similarity). May be involved in signal transduction of
CC       extracellular H(+) (By similarity). {ECO:0000250|UniProtKB:O15525,
CC       ECO:0000250|UniProtKB:Q76MX4}.
CC   -!- SUBUNIT: Homodimer or heterodimer. Homodimerization leads to
CC       transcriptional repression. Forms high affinity heterodimers with
CC       members of the CNC-bZIP family such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2
CC       and NFE2L3/NRF3. Interacts with CREBBP; the interaction leads to
CC       acetylation of the basic region of MAFG and stimulation of NFE2
CC       transcriptional activity through increased DNA binding.
CC       {ECO:0000250|UniProtKB:O15525}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15525,
CC       ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- PTM: Acetylated in erythroid cells by CREB-binding protein (CBP).
CC       Acetylation augments the DNA-binding activity of NFE2, but has no
CC       effect on binding NFE2. {ECO:0000250|UniProtKB:O15525}.
CC   -!- PTM: Sumoylation at Lys-14 is required for active transcriptional
CC       repression. {ECO:0000250|UniProtKB:O54790}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR   EMBL; BC142248; AAI42249.1; -; mRNA.
DR   RefSeq; NP_001092450.1; NM_001098980.1.
DR   RefSeq; XP_005221100.1; XM_005221043.3.
DR   RefSeq; XP_005221101.1; XM_005221044.3.
DR   RefSeq; XP_005221102.1; XM_005221045.3.
DR   AlphaFoldDB; A5PJV0; -.
DR   SMR; A5PJV0; -.
DR   STRING; 9913.ENSBTAP00000000044; -.
DR   PaxDb; A5PJV0; -.
DR   PRIDE; A5PJV0; -.
DR   Ensembl; ENSBTAT00000000044; ENSBTAP00000000044; ENSBTAG00000000040.
DR   GeneID; 515219; -.
DR   KEGG; bta:515219; -.
DR   CTD; 4097; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000040; -.
DR   VGNC; VGNC:31141; MAFG.
DR   eggNOG; KOG4196; Eukaryota.
DR   GeneTree; ENSGT00940000160070; -.
DR   HOGENOM; CLU_112948_0_0_1; -.
DR   InParanoid; A5PJV0; -.
DR   OMA; IREQEHP; -.
DR   OrthoDB; 1395389at2759; -.
DR   TreeFam; TF325689; -.
DR   Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000000040; Expressed in triceps brachii and 104 other tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0030534; P:adult behavior; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0045604; P:regulation of epidermal cell differentiation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR004826; bZIP_Maf.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR028551; MafG.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   InterPro; IPR024874; Transcription_factor_Maf_fam.
DR   PANTHER; PTHR10129; PTHR10129; 1.
DR   PANTHER; PTHR10129:SF15; PTHR10129:SF15; 1.
DR   Pfam; PF03131; bZIP_Maf; 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   Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..162
FT                   /note="Transcription factor MafG"
FT                   /id="PRO_0000370372"
FT   DOMAIN          51..114
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..76
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          79..93
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O15525"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O15525"
FT   MOD_RES         71
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O15525"
FT   MOD_RES         76
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O15525"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O15525"
FT   CROSSLNK        14
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O15525"
FT   CROSSLNK        14
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O15525"
SQ   SEQUENCE   162 AA;  17877 MW;  C7FF19614EB95C7D CRC64;
     MTTPNKGNKA LKVKREPGEN GTSLTDEELV TMSVRELNQH LRGLSKEEII QLKQRRRTLK
     NRGYAASCRV KRVTQKEELE KQKAELQQEV EKLASENASM KLELDALRSK YEALQNFART
     VARSPVAPAR GPLAAGLGPL VPGKVAATSV ITIVKSKTDA RS