ID   MAD1_XENTR              Reviewed;         221 AA.
AC   Q0VFI9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Max dimerization protein 1;
DE            Short=Max dimerizer 1;
DE   AltName: Full=Protein MAD;
GN   Name=mxd1; Synonyms=mad1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional repressor. MAD binds with MAX to form a
CC       sequence-specific DNA-binding protein complex which recognizes the core
CC       sequence 5'-CAC[GA]TG-3'. MAD thus antagonizes MYC transcriptional
CC       activity by competing for MAX (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MAX (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR   EMBL; BC118812; AAI18813.1; -; mRNA.
DR   RefSeq; NP_001072228.1; NM_001078760.1.
DR   AlphaFoldDB; Q0VFI9; -.
DR   SMR; Q0VFI9; -.
DR   PaxDb; Q0VFI9; -.
DR   DNASU; 779675; -.
DR   GeneID; 779675; -.
DR   KEGG; xtr:779675; -.
DR   CTD; 4084; -.
DR   Xenbase; XB-GENE-943715; mxd1.
DR   eggNOG; KOG2483; Eukaryota.
DR   InParanoid; Q0VFI9; -.
DR   OrthoDB; 1311585at2759; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000033966; Expressed in testis and 12 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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_0000253706"
FT   DOMAIN          55..107
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          28..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..202
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;  25297 MW;  E1D2DE3A68721B29 CRC64;
     MAAPVCVNIQ MLLEAAEYLE RREREAEHGY ASMLPYNSKE RDGLKRKSKS KKSSNSRSTH
     NEMEKNRRAH LRLCLEKLKI LVPLGPESNR HTTLSLLTRA KSHIKKLEDC DKRSLHQIEQ
     LQREQRHLKR QLEKFGVERT RMDSIGSAMS SERSDSDREE IDVDVESTDY LTADLDWSSS
     SSSVSDLDER GSMQSICSDE GYSSSGLKRI ELQDNPKITA L