ID Q6XC23_XERIN Unreviewed; 186 AA.
AC Q6XC23;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Myc proto-oncogene protein {ECO:0000256|ARBA:ARBA00013423};
DE AltName: Full=Proto-oncogene c-Myc {ECO:0000256|ARBA:ARBA00033247};
DE AltName: Full=Transcription factor p64 {ECO:0000256|ARBA:ARBA00030496};
DE Flags: Fragment;
OS Xerus inauris (South African ground squirrel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Xerini; Xerus.
OX NCBI_TaxID=234690 {ECO:0000313|EMBL:AAP76467.1};
RN [1] {ECO:0000313|EMBL:AAP76467.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15012949; DOI=10.1016/S1055-7903(03)00204-5;
RA Steppan S.J., Storz B.L., Hoffmann R.S.;
RT "Nuclear DNA phylogeny of the squirrels (Mammalia: Rodentia) and the
RT evolution of arboreality from c-myc and RAG1.";
RL Mol. Phylogenet. Evol. 30:703-719(2004).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
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DR EMBL; AY241528; AAP76467.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6XC23; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd11458; bHLHzip_c-Myc; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR003327; Myc-LZ.
DR InterPro; IPR002418; Tscrpt_reg_Myc.
DR InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR PANTHER; PTHR45851; MYC PROTO-ONCOGENE; 1.
DR PANTHER; PTHR45851:SF1; MYC PROTO-ONCOGENE PROTEIN; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF02344; Myc-LZ; 1.
DR Pfam; PF01056; Myc_N; 1.
DR PRINTS; PR00044; LEUZIPPRMYC.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}.
FT DOMAIN 101..153
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..184
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 92..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP76467.1"
SQ SEQUENCE 186 AA; 21451 MW; 78D55A6846C0A25B CRC64;
EEQEDEEEID VVSVEKRQPP ARRSESVSPP AGSHSKPPYS PLVLKRCHVS THQHNYAAPP
STRKDCPAAK RAKLDSGRVL KQISNNRKCA SPRSSDTEEN DKRRTHNVLE RQRRNELKRS
FFALRDQIPE LENNEKAPKV IILKKATAYI LSIQAEEQKL ISEKDLLRKR REQLKQKLEQ
LRNSCA
//
