ID   MAD3_RAT                Reviewed;         206 AA.
AC   Q62912;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Max dimerization protein 3;
DE            Short=Max dimerizer 3;
DE   AltName: Full=Max-associated protein 3;
DE   AltName: Full=Max-interacting transcriptional repressor MAD3;
DE   AltName: Full=Myx;
GN   Name=Mxd3; Synonyms=Mad3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang T., Li B., Danielson P., Wang Y., Zervos A.S., Haqq T., Rockwell S.,
RA   Teixeira J., Donahoe P.;
RT   "Myx: a novel interactor that also binds to a membrane serine threonine
RT   kinase receptor.";
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence-
CC       specific DNA-binding protein complex which recognizes the core sequence
CC       5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing
CC       for MAX and suppresses MYC dependent cell transformation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MAX. Interacts with SIN3A AND
CC       SIN3B. Interacts with RNF17 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR   EMBL; U45986; AAA91185.1; -; mRNA.
DR   RefSeq; NP_665716.1; NM_145773.1.
DR   AlphaFoldDB; Q62912; -.
DR   SMR; Q62912; -.
DR   STRING; 10116.ENSRNOP00000021946; -.
DR   PaxDb; Q62912; -.
DR   GeneID; 252915; -.
DR   KEGG; rno:252915; -.
DR   UCSC; RGD:628624; rat.
DR   CTD; 83463; -.
DR   RGD; 628624; Mxd3.
DR   eggNOG; KOG2483; Eukaryota.
DR   InParanoid; Q62912; -.
DR   OrthoDB; 1545091at2759; -.
DR   PhylomeDB; Q62912; -.
DR   PRO; PR:Q62912; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
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   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..206
FT                   /note="Max dimerization protein 3"
FT                   /id="PRO_0000253709"
FT   DOMAIN          57..109
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          8..25
FT                   /note="Interaction with SIN3A and SIN3B"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  23671 MW;  7B84C1935FC61667 CRC64;
     MEPVASNIQV LLQAAEFLER REREAEHGYA SLCPHHSPGT VCRRRKAPLQ APGALNSGRH
     VHNELEKRRR AQLKRCLEQL RQQMPLGVDH TRYTTLSLLR GARMHIQKLE EQEQQAQRLK
     EKLRSRQQSL QQQLEQLQGL LGVRERDRLR ADSLDSSGLS SERFDSDQED LEVDVESLVF
     GTETELLQSF SAGQEHSYSH STGTWL