MAFG_RAT
ID MAFG_RAT Reviewed; 189 AA.
AC Q76MX4; Q99N83;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Transcription factor MafG;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog G;
GN Name=Mafg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=CNS;
RX PubMed=10724342; DOI=10.1023/a:1007017902194;
RA Shimokawa N., Okada J., Miura M.;
RT "Cloning of MafG homologue from the rat brain by differential display and
RT its expression after hypercapnic stimulation.";
RL Mol. Cell. Biochem. 203:135-141(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11583919; DOI=10.1016/s0898-6568(01)00213-3;
RA Shimokawa N., Kumaki I., Takayama K.;
RT "MafG-2 is a novel Maf protein that is expressed by stimulation of
RT extracellular H(+).";
RL Cell. Signal. 13:835-839(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Since they lack a putative transactivation domain, the small
CC Mafs behave as transcriptional repressors when they dimerize among
CC themselves (By similarity). However, they seem to serve as
CC transcriptional activators by dimerizing with other (usually larger)
CC basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and recruiting
CC them to specific DNA-binding sites (By similarity). Small Maf proteins
CC heterodimerize with Fos and may act as competitive repressors of the
CC NFE2L2 transcription factor (By similarity). Transcription factor,
CC component of erythroid-specific transcription factor NFE2L2 (By
CC similarity). Activates globin gene expression when associated with
CC NFE2L2 (By similarity). May be involved in signal transduction of
CC extracellular H(+) (PubMed:11583919). {ECO:0000250|UniProtKB:O15525,
CC ECO:0000269|PubMed:11583919}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=MafG2;
CC IsoId=Q76MX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76MX4-2; Sequence=VSP_036798;
CC -!- TISSUE SPECIFICITY: High expression in the ventral medulla surface
CC (VMS), heart and skeletal muscle. Lower expression in the cerebral
CC cortex, cerebellum, liver, stomach and intestine.
CC {ECO:0000269|PubMed:10724342}.
CC -!- INDUCTION: Increased levels in the VMS after hypercapnic stimulation.
CC {ECO:0000269|PubMed:10724342, ECO:0000269|PubMed:11583919}.
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-41 is required for active transcriptional
CC repression. {ECO:0000250|UniProtKB:O54790}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; AB026487; BAA85331.1; -; mRNA.
DR EMBL; AB050011; BAB41097.1; -; mRNA.
DR EMBL; CH473948; EDM06874.1; -; Genomic_DNA.
DR EMBL; CH473948; EDM06875.1; -; Genomic_DNA.
DR EMBL; CH473948; EDM06876.1; -; Genomic_DNA.
DR EMBL; BC078828; AAH78828.1; -; mRNA.
DR RefSeq; NP_071781.1; NM_022386.2. [Q76MX4-2]
DR RefSeq; XP_006247976.1; XM_006247914.3. [Q76MX4-1]
DR RefSeq; XP_006247978.1; XM_006247916.3. [Q76MX4-1]
DR RefSeq; XP_006247980.1; XM_006247918.3. [Q76MX4-1]
DR RefSeq; XP_006247983.1; XM_006247921.3. [Q76MX4-2]
DR RefSeq; XP_006247984.1; XM_006247922.3. [Q76MX4-2]
DR RefSeq; XP_008766704.1; XM_008768482.2. [Q76MX4-2]
DR RefSeq; XP_017453010.1; XM_017597521.1. [Q76MX4-1]
DR AlphaFoldDB; Q76MX4; -.
DR SMR; Q76MX4; -.
DR iPTMnet; Q76MX4; -.
DR PhosphoSitePlus; Q76MX4; -.
DR Ensembl; ENSRNOT00000104193; ENSRNOP00000091294; ENSRNOG00000036697. [Q76MX4-1]
DR GeneID; 64188; -.
DR KEGG; rno:64188; -.
DR CTD; 4097; -.
DR RGD; 619953; Mafg.
DR GeneTree; ENSGT00940000160070; -.
DR HOGENOM; CLU_112948_0_0_1; -.
DR InParanoid; Q76MX4; -.
DR OMA; IREQEHP; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; Q76MX4; -.
DR TreeFam; TF325689; -.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q76MX4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000036697; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q76MX4; RN.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
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:RGD.
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; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0030641; P:regulation of cellular pH; IDA:RGD.
DR GO; GO:0045604; P:regulation of epidermal cell differentiation; ISO:RGD.
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; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..189
FT /note="Transcription factor MafG"
FT /id="PRO_0000368188"
FT DOMAIN 78..141
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 80..103
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 106..120
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15525"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15525"
FT MOD_RES 98
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15525"
FT MOD_RES 103
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15525"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15525"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15525"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O15525"
FT VAR_SEQ 14..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10724342,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036798"
SQ SEQUENCE 189 AA; 20533 MW; 65F5CF89284DC9D4 CRC64;
MTTPNKGNKA LKVSGEAGLG VCWAGHSYSA LTPCAVPLQV KREPGENGTS LTDEELVTMS
VRELNQHLRG LSKEEIIQLK QRRRTLKNRG YAASCRVKRV TQKEELEKQK AELQQEVEKL
ASENASMKLE LDALRSKYEA LQNFARTVAR SPVAPARGPL AAGLGPLVPG KVAATSVITI
VKSKTDARS
