MNT_XENLA
ID MNT_XENLA Reviewed; 574 AA.
AC Q0VH32; Q58EX1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Max-binding protein MNT;
DE AltName: Full=Myc antagonist MNT;
GN Name=mnt;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15973701; DOI=10.1002/dvdy.20470;
RA Juergens K., Rust B., Pieler T., Henningfeld K.A.;
RT "Isolation and comparative expression analysis of the Myc-regulatory
RT proteins Mad1, Mad3, and Mnt during Xenopus development.";
RL Dev. Dyn. 233:1554-1559(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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' (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a homodimer or a heterodimer with MAX (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Expression in the CNS is localized anteriorly and
CC in addition is present in the migrating neural crest cells.
CC {ECO:0000269|PubMed:15973701}.
CC -!- DEVELOPMENTAL STAGE: First detected at neurula stages, and are
CC localized anteriorly in the neural plate, neural crest and weakly in
CC the spinal cord. As development proceeds, localized throughout the CNS,
CC eye vesicle, and the streams of migrating branchial and hyoid neural
CC crest and is also present weakly in the cement gland. Embryos at stage
CC 27 show a strong expression in the retina and spinal chord, as well as
CC a weak expression in the forebrain and midbrain. Predominately located
CC in the outermost marginal layer of the ventral hindbrain, where
CC terminally differentiated neurons are located.
CC {ECO:0000269|PubMed:15973701}.
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; AY964106; AAY32593.1; -; mRNA.
DR EMBL; BC091719; AAH91719.1; -; mRNA.
DR RefSeq; NP_001089310.1; NM_001095841.1.
DR AlphaFoldDB; Q0VH32; -.
DR SMR; Q0VH32; -.
DR PRIDE; Q0VH32; -.
DR DNASU; 734360; -.
DR GeneID; 734360; -.
DR KEGG; xla:734360; -.
DR CTD; 734360; -.
DR Xenbase; XB-GENE-6087152; mnt.L.
DR OrthoDB; 445807at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 734360; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..574
FT /note="Max-binding protein MNT"
FT /id="PRO_0000253713"
FT DOMAIN 223..274
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 17..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..302
FT /note="Leucine-zipper"
FT REGION 323..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 46
FT /note="E -> EE (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..82
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="T -> S (in Ref. 2; AAH91719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 63408 MW; 13A225014E2A123A CRC64;
MSLETLLQAA LFLEWQAQQQ QQRTREENDK ILVEQEEEEE EEEEEENKSV LRTEEHINQL
PPDPVAPPAP APPPPPPPPP PPSAPVTVIP LPVVSCTPQP VVQTTVSPPV LQRHAPVVSP
PVLNKEVSLP PVIQRPPSTV LPEIKTTPLN MGSPKPLHHY QAPVLAITHH HLMQQQQQQP
IQPQPTSLQP QQQPHPQPLG ALRLPVTDDG RSNEQRRRPG GAGTREVHNK LEKNRRAHLK
ECFETLKRNI PNVDDKKTSN LSVLRSALRY IQSLKRKEKE YEHEMERLAR EKIATQQRLA
DLKNDLSQWM DIIEIDRIVR QTVQPEDDQA STSTASEGED NIDEDMDDDR PVNALSKRQQ
PGLIKMIPSS AAVHNHHSTI LPQHVSIQQK QVPSPHTQPQ ISSQALVPTQ AMVPAQTHIV
TASAVQSTVI AHTATTHASV IQTLNHVISG PQTKHIAHIA PSTSSPVQLT TAAQPIGHIT
VHPATINHMT HLGQQLPIYP QPVAVSQPMM SHIAHTISHP QVNGTTNLGQ PAVMTKPTVG
TQMVHHPQLV GQTVLNPVTM VTMPSFPVST LKLA
