ID   MAFK_MOUSE              Reviewed;         156 AA.
AC   Q61827; Q60600;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Transcription factor MafK;
DE   AltName: Full=Erythroid transcription factor NF-E2 p18 subunit;
GN   Name=Mafk; Synonyms=Nfe2u;
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 [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7706310; DOI=10.1074/jbc.270.13.7615;
RA   Igarashi K., Itoh K., Motohashi H., Hayashi N., Matuzaki Y., Nakauchi H.,
RA   Nishizawa M., Yamamoto M.;
RT   "Activity and expression of murine small Maf family protein MafK.";
RL   J. Biol. Chem. 270:7615-7624(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA; TISSUE=Hematopoietic;
RX   PubMed=8265578; DOI=10.1073/pnas.90.24.11488;
RA   Andrews N.C., Kotkow K.J., Ney P.A., Erdjument-Bromage H., Tempst P.,
RA   Orkin S.H.;
RT   "The ubiquitous subunit of erythroid transcription factor NF-E2 is a small
RT   basic-leucine zipper protein related to the v-maf oncogene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11488-11492(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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   [4]
RP   FUNCTION, AND INTERACTION WITH NFE2L2.
RX   PubMed=9240432; DOI=10.1006/bbrc.1997.6943;
RA   Itoh K., Chiba T., Takahashi S., Ishii T., Igarashi K., Katoh Y., Oyake T.,
RA   Hayashi N., Satoh K., Hatayama I., Yamamoto M., Nabeshima Y.;
RT   "An Nrf2/small Maf heterodimer mediates the induction of phase II
RT   detoxifying enzyme genes through antioxidant response elements.";
RL   Biochem. Biophys. Res. Commun. 236:313-322(1997).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 act as transcriptional
CC       activators by dimerizing with other (usually larger) basic-zipper
CC       proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3, and
CC       recruiting them to specific DNA-binding sites (PubMed:9240432). Small
CC       Maf proteins heterodimerize with Fos and may act as competitive
CC       repressors of the NF-E2 transcription factor (By similarity).
CC       {ECO:0000250|UniProtKB:O60675, ECO:0000269|PubMed:9240432}.
CC   -!- SUBUNIT: Homodimer or heterodimer (By similarity). It can form high
CC       affinity heterodimers with members of the CNC-bZIP family such as NFE2,
CC       NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3 (PubMed:9240432).
CC       {ECO:0000250|UniProtKB:O60675, ECO:0000269|PubMed:9240432}.
CC   -!- INTERACTION:
CC       Q61827; P97302: Bach1; NbExp=5; IntAct=EBI-15740843, EBI-2552417;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC       placenta. Also expressed in erythroid cells.
CC   -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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; D42124; BAA07704.1; -; mRNA.
DR   EMBL; U01036; AAC52132.1; -; mRNA.
DR   EMBL; BC014295; AAH14295.1; -; mRNA.
DR   CCDS; CCDS19814.1; -.
DR   PIR; A49391; A49391.
DR   PIR; A56124; A56124.
DR   RefSeq; NP_034887.1; NM_010757.2.
DR   RefSeq; XP_006504716.1; XM_006504653.3.
DR   AlphaFoldDB; Q61827; -.
DR   SMR; Q61827; -.
DR   BioGRID; 201284; 6.
DR   DIP; DIP-46345N; -.
DR   IntAct; Q61827; 3.
DR   STRING; 10090.ENSMUSP00000106460; -.
DR   GlyGen; Q61827; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; Q61827; -.
DR   PhosphoSitePlus; Q61827; -.
DR   EPD; Q61827; -.
DR   MaxQB; Q61827; -.
DR   PaxDb; 10090-ENSMUSP00000018287; -.
DR   ProteomicsDB; 252714; -.
DR   Pumba; Q61827; -.
DR   Antibodypedia; 24241; 182 antibodies from 25 providers.
DR   DNASU; 17135; -.
DR   Ensembl; ENSMUST00000018287.10; ENSMUSP00000018287.4; ENSMUSG00000018143.11.
DR   Ensembl; ENSMUST00000110836.2; ENSMUSP00000106460.2; ENSMUSG00000018143.11.
DR   GeneID; 17135; -.
DR   KEGG; mmu:17135; -.
DR   UCSC; uc009ahd.1; mouse.
DR   AGR; MGI:99951; -.
DR   CTD; 7975; -.
DR   MGI; MGI:99951; Mafk.
DR   VEuPathDB; HostDB:ENSMUSG00000018143; -.
DR   eggNOG; KOG4196; Eukaryota.
DR   GeneTree; ENSGT00940000160044; -.
DR   HOGENOM; CLU_112948_0_0_1; -.
DR   InParanoid; Q61827; -.
DR   OMA; VITIDWA; -.
DR   OrthoDB; 2958941at2759; -.
DR   PhylomeDB; Q61827; -.
DR   TreeFam; TF325689; -.
DR   Reactome; R-MMU-9707616; Heme signaling.
DR   Reactome; R-MMU-9708530; Regulation of BACH1 activity.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 17135; 2 hits in 79 CRISPR screens.
DR   PRO; PR:Q61827; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q61827; Protein.
DR   Bgee; ENSMUSG00000018143; Expressed in granulocyte and 206 other cell types or tissues.
DR   ExpressionAtlas; Q61827; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0071535; F:RING-like zinc finger domain binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; ISO:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd14717; bZIP_Maf_small; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR004826; bZIP_Maf.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   InterPro; IPR024874; Transcription_factor_Maf_fam.
DR   PANTHER; PTHR10129; TRANSCRIPTION FACTOR MAF; 1.
DR   PANTHER; PTHR10129:SF26; TRANSCRIPTION FACTOR MAFK; 1.
DR   Pfam; PF03131; bZIP_Maf; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   Genevisible; Q61827; MM.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..156
FT                   /note="Transcription factor MafK"
FT                   /id="PRO_0000076504"
FT   DOMAIN          51..114
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          51..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         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        130
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O60675"
FT   CONFLICT        36..37
FT                   /note="EL -> DV (in Ref. 2; AAC52132)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   156 AA;  17537 MW;  39F98F8A257F46CB CRC64;
     MTTNPKPNKA LKVKKEAGEN APVLSDDELV SMSVRELNQH LRGLTKEEVT RLKQRRRTLK
     NRGYAASCRI KRVTQKEELE RQRVELQQEV EKLARENSSM RLELDALRSK YEALQTFART
     VARGPVTPTK VATTSVITIV KSAELSSTSV PFSAAS
//