ID   MXI1_DANRE              Reviewed;         243 AA.
AC   P50541;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Max-interacting protein 1;
DE            Short=Max interactor 1;
GN   Name=mxi1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7936639;
RA   Schreiber-Agus N., Chin L., Chen K., Torres R., Thomson C.T.,
RA   Sacchettini J.C., DePinho R.A.;
RT   "Evolutionary relationships and functional conservation among vertebrate
RT   Max-associated proteins: the zebra fish homolog of Mxi1.";
RL   Oncogene 9:3167-3177(1994).
CC   -!- FUNCTION: Transcriptional repressor. MXI1 binds with MAX to form a
CC       sequence-specific DNA-binding protein complex which recognizes the core
CC       sequence 5'-CAC[GA]TG-3'. MXI1 thus antagonizes MYC transcriptional
CC       activity by competing for MAX.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MAX.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Barely detectable during early stages of active
CC       growth and differentiation, exhibits dramatic increase between 30 and
CC       48 hours of development. This late embryonic stage marks a period of
CC       continued maturation and moderate growth of most organs, but is also
CC       characterized by initiation of cellular growth arrest and terminal
CC       differentiation in many cell types.
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DR   EMBL; U10638; AAA19324.1; -; mRNA.
DR   AlphaFoldDB; P50541; -.
DR   SMR; P50541; -.
DR   STRING; 7955.ENSDARP00000095521; -.
DR   PaxDb; P50541; -.
DR   ZFIN; ZDB-GENE-990415-151; mxi1.
DR   eggNOG; KOG2483; Eukaryota.
DR   InParanoid; P50541; -.
DR   PRO; PR:P50541; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0032502; P:developmental process; IEA:UniProt.
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..243
FT                   /note="Max-interacting protein 1"
FT                   /id="PRO_0000127288"
FT   DOMAIN          76..128
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          164..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   243 AA;  27643 MW;  60932411CC137610 CRC64;
     MSTCPFNDVF NSTDSSMINT FLKNVQVLLE AASYIESAER KDGKCEHGYA STFPSIQHSS
     YQRQRKFRNK KCNNNHYRST HNELEKNRRA HLRLCLERLK TLIPLGPECS RHTTLGLLNK
     AKAHIKKLEE ADRKSRYQLE SLEREQRHLR RRLDLLRDGG GSLEAERIRT DSMGSTPCSE
     RSDRSDSDQE EMEVDVESTE FSHGELDSVS TASTSDLDDH SSLQSTASDE GYSSCSIKLA
     FSS