MXI1_RAT
ID MXI1_RAT Reviewed; 228 AA.
AC O09015;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Max-interacting protein 1;
DE Short=Max interactor 1;
GN Name=Mxi1;
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].
RC STRAIN=Wistar;
RA Wang D.Y., Xiang Y.Y., Tanaka M., Sugimura H.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
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. Interacts with SMC3.
CC Interacts with RNF17 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; AF003008; AAB61595.1; -; mRNA.
DR AlphaFoldDB; O09015; -.
DR SMR; O09015; -.
DR STRING; 10116.ENSRNOP00000040770; -.
DR PaxDb; O09015; -.
DR PRIDE; O09015; -.
DR UCSC; RGD:3128; rat.
DR RGD; 3128; Mxi1.
DR eggNOG; KOG2483; Eukaryota.
DR InParanoid; O09015; -.
DR PhylomeDB; O09015; -.
DR PRO; PR:O09015; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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:0001825; P:blastocyst formation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:RGD.
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..228
FT /note="Max-interacting protein 1"
FT /id="PRO_0000127287"
FT DOMAIN 67..119
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 29..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 228 AA; 26022 MW; F03F800082B0F194 CRC64;
MERVKMINVQ PMLEAAEFLE RRERECEHGY ASSFPSMPSP RLQHSKPPRR LSRAQKHSSG
SSNTSTANRS THNELEKNRR AHLRLCLERL KVLIPLGPDC TRHTTLGLLN KAKAHIKKLE
EAERKSQHQL ENLEREQRFL KRRLEQLQGP QEMERIRMDS IGSTISSDRS DSEREEIEVD
VESTEFSHGE VDNISTTSIS DIDDHSSLQS IGSDEGYSSA SVKLSFTS
