ID B8LFI8_CULAL Unreviewed; 400 AA.
AC B8LFI8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 28-JUN-2023, entry version 56.
DE SubName: Full=Cellular myelocytomatosis oncogene {ECO:0000313|EMBL:ABP73345.1};
DE Flags: Fragment;
GN Name=c-myc {ECO:0000313|EMBL:ABP73345.1};
OS Culter alburnus (Topmouth culter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Culter.
OX NCBI_TaxID=194366 {ECO:0000313|EMBL:ABP73345.1};
RN [1] {ECO:0000313|EMBL:ABP73345.1}
RP NUCLEOTIDE SEQUENCE.
RA Kong X., He S.;
RT "Molecular phylogenetic relationships of eastern Asia cyprinidae inferred
RT from c-myc CDS sequence and analysis of high variation in coding regions.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that binds DNA in a non-specific manner,
CC yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'.
CC Activates the transcription of growth-related genes.
CC {ECO:0000256|ARBA:ARBA00003607}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX.
CC {ECO:0000256|ARBA:ARBA00025872}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; EF194855; ABP73345.1; -; Genomic_DNA.
DR AlphaFoldDB; B8LFI8; -.
DR GO; GO:0005634; C:nucleus; 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 PIRSF; PIRSF001705; Myc_protein; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}.
FT DOMAIN 322..374
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 186..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:ABP73345.1"
SQ SEQUENCE 400 AA; 45609 MW; 92AF679B4900005D CRC64;
MPVSSSLVYK NYDYDYDSIQ PYFYFDNDDE DFYHHQQGQT QPPAPSEDIW KKFELLPTPP
LSPSRRQSLS TAEQLEMVSE FLGDDVVNQS FICDADYSQS FIKSIIIQDC MWSGFSAAAK
LEKVVSERLA SLHAARKGLM SDSSSNRLNA SYLQDLSTSA SECIDPSVVF PYPLTESCKA
RKVAPSQPLL VLDTPPNSSS SSGSDSEDDE EEEEEEEEEE EEEEEEEEEE IDVVTVEKRQ
KRSETEVSDS RHPSPLVLKR CHVSTHQHNY AAHPSTRHDQ PAVKRLRLEA SSNNNSSSSS
SNRHGKQRKC ASPRTSDSED NGKRRTHNVL ERQRRNELKL SFFALRDEIP EVANNEKAAK
VVILKKATEC IHSMHLDEQR LLSIKEQLRR KSEQLKHKLQ
//
