ID   MAD1_XENLA              Reviewed;         221 AA.
AC   Q0VH34;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Max dimerization protein 1;
DE            Short=Max dimerizer 1;
DE   AltName: Full=Protein MAD;
GN   Name=mxd1; Synonyms=mad1;
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).
CC   -!- FUNCTION: Component of a transcriptional repressor complex together
CC       with MAX (By similarity). In complex with MAX binds to the core DNA
CC       sequence 5'-CAC[GA]TG-3' (By similarity). Antagonizes MYC
CC       transcriptional activity by competing with MYC for MAX binding (By
CC       similarity). Binds to the TERT promoter and represses telomerase
CC       expression, possibly by interfering with MYC binding (By similarity).
CC       {ECO:0000250|UniProtKB:Q05195}.
CC   -!- SUBUNIT: Heterodimer with MAX; the interaction is required for DNA-
CC       binding (By similarity). DNA binding requires dimerization with another
CC       bHLH protein; does not form homodimers, and does not bind to DNA in the
CC       absence of MAX in vitro (By similarity).
CC       {ECO:0000250|UniProtKB:Q05195}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- TISSUE SPECIFICITY: Expressed primarily in cells that have undergone
CC       terminal differentiation including notochord, floor plate and cement
CC       gland. {ECO:0000269|PubMed:15973701}.
CC   -!- DEVELOPMENTAL STAGE: Localized throughout the animal hemisphere of
CC       early cleavage stage embryos and becomes localized above the dorsal
CC       blastopore lip during early gastrulation. As gastrulation proceeds, the
CC       expression extends along the dorsal midline. In stage 17 embryos,
CC       expressed in the notochord and floor plate. At this stage, also
CC       detected in the cement gland, where they are maintained in later
CC       developmental stages. Additional expression is also detected in the
CC       pineal gland, as well as the trigeminal and geniculate ganglia. In
CC       stage 27 embryos, expressed in the floor plate and in addition, present
CC       in the hypochord and the marginal zone of the ventral neural tube where
CC       postmitotic neurons are located. {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; AY964104; AAY32591.1; -; mRNA.
DR   RefSeq; NP_001090200.1; NM_001096731.1.
DR   AlphaFoldDB; Q0VH34; -.
DR   SMR; Q0VH34; -.
DR   PRIDE; Q0VH34; -.
DR   GeneID; 779097; -.
DR   KEGG; xla:779097; -.
DR   CTD; 779097; -.
DR   Xenbase; XB-GENE-943720; mxd1.L.
DR   OMA; LPYPHEI; -.
DR   OrthoDB; 1311585at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 779097; Expressed in zone of skin 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   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR040157; MXD1.
DR   PANTHER; PTHR11969:SF18; PTHR11969:SF18; 1.
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..221
FT                   /note="Max dimerization protein 1"
FT                   /id="PRO_0000253705"
FT   DOMAIN          55..107
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          29..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           21..49
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        39..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   221 AA;  25233 MW;  B9745F241EAAAE28 CRC64;
     MAAPVCVNIQ MLLEAAEYLE RREREAEHGY ASMLPYNSKE RDGLKRKSKS KKSSSSRSTH
     NEMEKNRRAH LRLCLEKLKM LVPLGPESNR HTTLSLLMRA KLHIKKLEDC DKRSVHQIEQ
     LQREQRHLTR QLEKFGVERT RMDSIGSAMS SERSDSDREE IDVDVESTDY LTAELDWSSS
     SSSVSDLDER ESMQSICSDE GYSSSGLKSI GLQNNPKSIA L