ID   MNT_MOUSE               Reviewed;         591 AA.
AC   O08789; P97349; Q6GTJ3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Max-binding protein MNT;
DE   AltName: Full=Myc antagonist MNT;
DE   AltName: Full=Protein ROX;
GN   Name=Mnt; Synonyms=Rox;
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=Embryo;
RX   PubMed=9000049; DOI=10.1101/gad.11.1.44;
RA   Hurlin P.J., Queva C., Eisenman R.N.;
RT   "Mnt, a novel Max-interacting protein is coexpressed with Myc in
RT   proliferating cells and mediates repression at Myc binding sites.";
RL   Genes Dev. 11:44-58(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=9184233; DOI=10.1093/emboj/16.10.2892;
RA   Meroni G., Reymond A., Alcalay M., Borsani G., Tanigami A., Tonlorenzi R.,
RA   Lo Nigro C., Messali S., Zollo M., Ledbetter D.H., Brent R., Ballabio A.,
RA   Carrozzo R.;
RT   "Rox, a novel bHLHZip protein expressed in quiescent cells that
RT   heterodimerizes with Max, binds a non-canonical E box and acts as a
RT   transcriptional repressor.";
RL   EMBO J. 16:2892-2906(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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: Binds DNA as a heterodimer with MAX and represses
CC       transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and,
CC       with higher affinity, to 5'-CACGCG-3'.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a homodimer or a heterodimer with MAX.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; U77356; AAB38687.1; -; mRNA.
DR   EMBL; Y07609; CAA68878.1; -; mRNA.
DR   EMBL; AL604066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466596; EDL12780.1; -; Genomic_DNA.
DR   EMBL; BC054534; AAH54534.1; -; mRNA.
DR   CCDS; CCDS25037.1; -.
DR   RefSeq; NP_034943.3; NM_010813.3.
DR   AlphaFoldDB; O08789; -.
DR   SMR; O08789; -.
DR   BioGRID; 201461; 6.
DR   IntAct; O08789; 1.
DR   STRING; 10090.ENSMUSP00000000291; -.
DR   GlyGen; O08789; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O08789; -.
DR   PhosphoSitePlus; O08789; -.
DR   EPD; O08789; -.
DR   MaxQB; O08789; -.
DR   PaxDb; 10090-ENSMUSP00000000291; -.
DR   PeptideAtlas; O08789; -.
DR   ProteomicsDB; 295572; -.
DR   Pumba; O08789; -.
DR   Antibodypedia; 22924; 161 antibodies from 31 providers.
DR   DNASU; 17428; -.
DR   Ensembl; ENSMUST00000000291.9; ENSMUSP00000000291.3; ENSMUSG00000000282.13.
DR   GeneID; 17428; -.
DR   KEGG; mmu:17428; -.
DR   UCSC; uc011xzb.1; mouse.
DR   AGR; MGI:109150; -.
DR   CTD; 4335; -.
DR   MGI; MGI:109150; Mnt.
DR   VEuPathDB; HostDB:ENSMUSG00000000282; -.
DR   eggNOG; KOG2483; Eukaryota.
DR   GeneTree; ENSGT00510000048287; -.
DR   HOGENOM; CLU_020165_1_0_1; -.
DR   InParanoid; O08789; -.
DR   OMA; WMDALEM; -.
DR   OrthoDB; 5357261at2759; -.
DR   TreeFam; TF315654; -.
DR   BioGRID-ORCS; 17428; 14 hits in 80 CRISPR screens.
DR   ChiTaRS; Mnt; mouse.
DR   PRO; PR:O08789; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; O08789; Protein.
DR   Bgee; ENSMUSG00000000282; Expressed in rostral migratory stream and 261 other cell types or tissues.
DR   ExpressionAtlas; O08789; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IC:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MGI.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0090398; P:cellular senescence; IMP:MGI.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd11402; bHLHzip_Mnt; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR11969; MAX DIMERIZATION, MAD; 1.
DR   PANTHER; PTHR11969:SF104; MAX-BINDING PROTEIN MNT; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   Genevisible; O08789; MM.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q99583"
FT   CHAIN           2..591
FT                   /note="Max-binding protein MNT"
FT                   /id="PRO_0000127282"
FT   DOMAIN          222..273
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          17..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..301
FT                   /note="Leucine-zipper"
FT   REGION          321..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..88
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..118
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..200
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..393
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        406..425
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99583"
FT   CONFLICT        379
FT                   /note="P -> T (in Ref. 1; AAB38687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="A -> V (in Ref. 1; AAB38687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402..403
FT                   /note="QQ -> EE (in Ref. 1; AAB38687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        414
FT                   /note="A -> G (in Ref. 1; AAB38687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431
FT                   /note="A -> V (in Ref. 1; AAB38687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        465
FT                   /note="P -> A (in Ref. 1; AAB38687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525
FT                   /note="A -> T (in Ref. 1; AAB38687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        558
FT                   /note="A -> G (in Ref. 1; AAB38687)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   591 AA;  63274 MW;  17C2B830381D2190 CRC64;
     MSIETLLEAA RFLEWQAQQQ QRAREEQERL RLEREREREQ EQKRASNLAR LAHALPVEEP
     RIEAPPLPLS PPAPPPAPPP PLATPAPLTV IPIPVVTNSP QSLPPPPPLP PAAQPLPLAP
     RQPALVSTPG LSIKEPVTLP TRPQVPTPAP LLPDAKTTVA PTGSPKPLQP LPAPILTIAP
     HPGVQPQLAP QQPPPPTLGT LKLAPAEEAK SSEQKKRPGG IGTREVHNKL EKNRRAHLKE
     CFETLKRNIP NVDDKKTSNL SVLRTALRYI QSLKRKEKEY EHEMERLARE KIATQQRLAE
     LKHELSQWMD VLEIDRVLRQ TGQPEDDQAS TSTASEGEDN VDEEMEGDRA GLGPPKLNHR
     PQPELLKSAL PTPSTAPAPL PTHPHPHPHP VALSPAHLPV QQQQPPQQKT PLPAPPPPPA
     TPTQTLVPAP AHLVATAGGG STVIAHTATT HASVIQTVNH VLQGPGGKHI AHIAPSAPSP
     AVQLAPATPP IGHITVHPAT LNHVAHLGSQ LPLYPQPVAV SQPVAVSHIA HTLSHQQVNG
     TAGLGPPATV MAKPAVGAQV VHHPQLVGQT VLNPVTMVTM PSFPVSTLKL A
//