MAFG_MOUSE
ID MAFG_MOUSE Reviewed; 162 AA.
AC O54790;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Transcription factor MafG;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog G;
GN Name=Mafg;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, DEVELOPMENTAL
RP STAGE, AND FUNCTION.
RC STRAIN=129/SvJ;
RX PubMed=9679061; DOI=10.1101/gad.12.14.2164;
RA Shavit J.A., Motohashi H., Onodera K., Akasaka J., Yamamoto M., Engel J.D.;
RT "Impaired megakaryopoiesis and behavioral defects in mafG-null mutant
RT mice.";
RL Genes Dev. 12:2164-2174(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUMOYLATION AT LYS-14, AND FUNCTION.
RX PubMed=16738329; DOI=10.1128/mcb.02193-05;
RA Motohashi H., Katsuoka F., Miyoshi C., Uchimura Y., Saitoh H.,
RA Francastel C., Engel J.D., Yamamoto M.;
RT "MafG sumoylation is required for active transcriptional repression.";
RL Mol. Cell. Biol. 26:4652-4663(2006).
RN [4]
RP INTERACTION WITH NFE2L2.
RX PubMed=31398338; DOI=10.1016/j.cell.2019.07.031;
RA Sanghvi V.R., Leibold J., Mina M., Mohan P., Berishaj M., Li Z.,
RA Miele M.M., Lailler N., Zhao C., de Stanchina E., Viale A., Akkari L.,
RA Lowe S.W., Ciriello G., Hendrickson R.C., Wendel H.G.;
RT "The oncogenic action of NRF2 depends on de-glycation by fructosamine-3-
RT kinase.";
RL Cell 178:807-819(2019).
RN [5]
RP STRUCTURE BY NMR OF 24-64.
RX PubMed=11875518; DOI=10.1038/nsb771;
RA Kusunoki H., Motohashi H., Katsuoka F., Morohashi A., Yamamoto M.,
RA Tanaka T.;
RT "Solution structure of the DNA-binding domain of MafG.";
RL Nat. Struct. Biol. 9:252-256(2002).
CC -!- FUNCTION: Since they lack a putative transactivation domain, the small
CC Mafs behave as transcriptional repressors when they dimerize among
CC themselves (PubMed:16738329, PubMed:9679061). However, they seem to
CC serve as transcriptional activators by dimerizing with other (usually
CC larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and
CC recruiting them to specific DNA-binding sites (PubMed:16738329,
CC PubMed:9679061). Small Maf proteins heterodimerize with Fos and may act
CC as 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 (By similarity). Homodimerization
CC leads to transcriptional repression (By similarity). Forms high
CC affinity heterodimers with members of the CNC-bZIP family such as NFE2,
CC NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3 (PubMed:31398338). Interacts
CC with CREBBP; the interaction leads to acetylation of the basic region
CC of MAFG and stimulation of NFE2 transcriptional activity through
CC increased DNA binding (By similarity). {ECO:0000250|UniProtKB:O15525,
CC ECO:0000269|PubMed:31398338}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15525,
CC ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo up until 8.5 dpc
CC with strong expression in the neural tube. Expression continues
CC throughout the embryo with some intense expression also in the
CC epithelium of the intestine, skeletal muscle, lens, retina, cranial
CC nerve, and dorsal root ganglion cells. After birth, strong expression
CC in the epidermis, hair follicles, epithelium of the digestive and
CC respiratory tracts, and kidney tubules. {ECO:0000269|PubMed:9679061}.
CC -!- PTM: Sumoylation at Lys-14 is required for active transcriptional
CC repression. {ECO:0000269|PubMed:16738329}.
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 -!- DISRUPTION PHENOTYPE: Mice, although viable and fertile, exhibit
CC abnormal megakaryocyte proliferation as well as age-dependent
CC behavioral defects. Megakaryocytes display both anti-glycoprotein IIb
CC immunoreactivity and anti-acetylcholinesterase activity.
CC {ECO:0000269|PubMed:9679061}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; AB009693; BAA24028.1; -; Genomic_DNA.
DR EMBL; BC002092; AAH02092.1; -; mRNA.
DR EMBL; BC052633; AAH52633.1; -; mRNA.
DR CCDS; CCDS25748.1; -.
DR RefSeq; NP_034886.1; NM_010756.3.
DR RefSeq; XP_017169797.1; XM_017314308.1.
DR RefSeq; XP_017169798.1; XM_017314309.1.
DR RefSeq; XP_017169799.1; XM_017314310.1.
DR RefSeq; XP_017169800.1; XM_017314311.1.
DR PDB; 1K1V; NMR; -; A=24-64.
DR PDB; 3A5T; X-ray; 2.80 A; A/B=21-123.
DR PDBsum; 1K1V; -.
DR PDBsum; 3A5T; -.
DR AlphaFoldDB; O54790; -.
DR SMR; O54790; -.
DR BioGRID; 201283; 4.
DR DIP; DIP-46344N; -.
DR IntAct; O54790; 3.
DR STRING; 10090.ENSMUSP00000053899; -.
DR iPTMnet; O54790; -.
DR PhosphoSitePlus; O54790; -.
DR EPD; O54790; -.
DR MaxQB; O54790; -.
DR PaxDb; O54790; -.
DR PeptideAtlas; O54790; -.
DR PRIDE; O54790; -.
DR ProteomicsDB; 292162; -.
DR Antibodypedia; 19851; 131 antibodies from 26 providers.
DR DNASU; 17134; -.
DR Ensembl; ENSMUST00000058162; ENSMUSP00000053899; ENSMUSG00000051510.
DR Ensembl; ENSMUST00000106180; ENSMUSP00000101786; ENSMUSG00000051510.
DR Ensembl; ENSMUST00000106181; ENSMUSP00000101787; ENSMUSG00000051510.
DR Ensembl; ENSMUST00000106182; ENSMUSP00000101788; ENSMUSG00000051510.
DR GeneID; 17134; -.
DR KEGG; mmu:17134; -.
DR UCSC; uc007mtu.2; mouse.
DR CTD; 4097; -.
DR MGI; MGI:96911; Mafg.
DR VEuPathDB; HostDB:ENSMUSG00000051510; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000160070; -.
DR HOGENOM; CLU_112948_0_0_1; -.
DR InParanoid; O54790; -.
DR OMA; IREQEHP; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; O54790; -.
DR TreeFam; TF325689; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 17134; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mafg; mouse.
DR EvolutionaryTrace; O54790; -.
DR PRO; PR:O54790; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O54790; protein.
DR Bgee; ENSMUSG00000051510; Expressed in granulocyte and 278 other tissues.
DR Genevisible; O54790; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; TAS:ParkinsonsUK-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; ISO:MGI.
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; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ParkinsonsUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0030641; P:regulation of cellular pH; ISO:MGI.
DR GO; GO:0045604; P:regulation of epidermal cell differentiation; IGI:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..162
FT /note="Transcription factor MafG"
FT /id="PRO_0000076501"
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:0000269|PubMed:16738329"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15525"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:3A5T"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:3A5T"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:3A5T"
FT HELIX 46..83
FT /evidence="ECO:0007829|PDB:3A5T"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3A5T"
FT TURN 89..94
FT /evidence="ECO:0007829|PDB:3A5T"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3A5T"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3A5T"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3A5T"
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
