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 14-OCT-2015, entry version 135. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA 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 RT project: 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 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 CC small Mafs behave as transcriptional repressors when they dimerize CC among themselves. However, they seem to serve as transcriptional CC activators by dimerizing with other (usually larger) basic-zipper CC proteins and recruiting them to specific DNA-binding sites. Small CC Maf proteins heterodimerize with Fos and may act as competitive CC repressors of the NF-E2 transcription factor. Transcription CC factor, component of erythroid-specific transcription factor NF- CC E2. Activates globin gene expression when associated with NF-E2. CC May be involved in signal transduction of extracellular H(+) (By CC similarity). {ECO:0000250}. 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, CC NFE2L2/NRF2 and NFE2L3/NRF3. Interacts with NFE2; the interaction CC results in transactivation activation. Interacts with CREBBP; the CC interaction leads to acetylation of the basic region of MAFG and CC stimulation of NFE2 transcriptional activity through increased DNA CC binding (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE- CC ProRule:PRU00978}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo up until E8.5 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, CC cranial nerve, and dorsal root ganglion cells. After birth, strong CC expression in the epidermis, hair follicles, epithelium of the CC digestive and respiratory tracts, and kidney tubules. CC {ECO:0000269|PubMed:9679061}. CC -!- PTM: Acetylated in erythroid cells by CREB-binding protein (CBP). CC Acetylation augments the DNA-binding activity of NF-E2. CC -!- PTM: Sumoylation at Lys-14 is required for active transcriptional CC repression. {ECO:0000269|PubMed:16738329}. 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 CC IIb immunoreactivity and anti-acetylcholinesterase activity. CC {ECO:0000269|PubMed:9679061}. CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 bZIP (basic-leucine zipper) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00978}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Mm.268010; -. DR UniGene; Mm.292957; -. DR UniGene; Mm.393664; -. 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 ProteinModelPortal; O54790; -. DR SMR; O54790; 21-111. DR BioGrid; 201283; 4. DR DIP; DIP-46344N; -. DR IntAct; O54790; 2. DR MINT; MINT-4101043; -. DR STRING; 10090.ENSMUSP00000053899; -. DR PhosphoSite; O54790; -. DR MaxQB; O54790; -. DR PaxDb; O54790; -. DR PRIDE; O54790; -. 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 eggNOG; NOG236209; -. DR GeneTree; ENSGT00550000074549; -. DR HOGENOM; HOG000045475; -. DR HOVERGEN; HBG001725; -. DR InParanoid; O54790; -. DR KO; K09037; -. DR OMA; ITASMGP; -. DR OrthoDB; EOG7BGHMQ; -. DR PhylomeDB; O54790; -. DR TreeFam; TF325689; -. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR ChiTaRS; Mafg; mouse. DR EvolutionaryTrace; O54790; -. DR NextBio; 291340; -. DR PRO; PR:O54790; -. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; O54790; -. DR Genevisible; O54790; MM. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; TAS:ParkinsonsUK-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IBA:GO_Central. 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 from RNA polymerase II promoter; IBA:GOC. DR GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI. DR GO; GO:0030641; P:regulation of cellular pH; IEA:Ensembl. DR GO; GO:0045604; P:regulation of epidermal cell differentiation; IGI:MGI. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IBA:GOC. DR Gene3D; 1.10.880.10; -; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR004826; bZIP_Maf. DR InterPro; IPR028551; MafG. DR InterPro; IPR008917; TF_DNA-bd. DR InterPro; IPR024874; Transciption_factor_Maf. 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 PROSITE; PS50217; BZIP; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1 162 Transcription factor MafG. FT /FTId=PRO_0000076501. FT DOMAIN 51 114 bZIP. {ECO:0000255|PROSITE- FT ProRule:PRU00978}. FT REGION 53 76 Basic motif. {ECO:0000255|PROSITE- FT ProRule:PRU00978}. FT REGION 79 93 Leucine-zipper. {ECO:0000255|PROSITE- FT ProRule:PRU00978}. FT MOD_RES 53 53 N6-acetyllysine. {ECO:0000305}. FT MOD_RES 60 60 N6-acetyllysine. {ECO:0000305}. FT MOD_RES 71 71 N6-acetyllysine. {ECO:0000305}. FT MOD_RES 76 76 N6-acetyllysine. {ECO:0000305}. FT MOD_RES 124 124 Phosphoserine. FT {ECO:0000250|UniProtKB:O15525}. FT CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO); FT alternate. FT CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. FT {ECO:0000250|UniProtKB:O15525}. FT HELIX 26 31 {ECO:0000244|PDB:3A5T}. FT HELIX 34 39 {ECO:0000244|PDB:3A5T}. FT TURN 40 43 {ECO:0000244|PDB:3A5T}. FT HELIX 46 83 {ECO:0000244|PDB:3A5T}. FT TURN 84 86 {ECO:0000244|PDB:3A5T}. FT TURN 89 94 {ECO:0000244|PDB:3A5T}. FT HELIX 99 102 {ECO:0000244|PDB:3A5T}. FT TURN 103 105 {ECO:0000244|PDB:3A5T}. FT STRAND 106 109 {ECO:0000244|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 //