ID B8LFK9_9TELE Unreviewed; 402 AA.
AC B8LFK9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 28-JUN-2023, entry version 59.
DE SubName: Full=Cellular myelocytomatosis oncogene {ECO:0000313|EMBL:ABP73366.1};
DE Flags: Fragment;
GN Name=c-myc {ECO:0000313|EMBL:ABP73366.1};
OS Schizothorax lissolabiata.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Schizothoracinae; Schizothorax.
OX NCBI_TaxID=327692 {ECO:0000313|EMBL:ABP73366.1};
RN [1] {ECO:0000313|EMBL:ABP73366.1}
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; EF194876; ABP73366.1; -; Genomic_DNA.
DR AlphaFoldDB; B8LFK9; -.
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 324..376
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 183..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 402
FT /evidence="ECO:0000313|EMBL:ABP73366.1"
SQ SEQUENCE 402 AA; 46099 MW; C4663F049616C87D CRC64;
MPVSASLAYK NYDYDYDSIQ PYFYFDNDDE DFYHHQQGQT QPPAPSEDIW KKFELLPTPP
LSPSRRQSLS TAEQLEMVSE FLGDDVVNQS FICDADYSQS FIKSIIIQDC MWSGFSAAAK
LEKVVSERLA SLHAARKELM SDSSSNRLNA SYLQDLSTSA SECIDPSVVF PYPLMESSKS
SKVAPSEPIL VLDTPPNSSS SSGSDSEDEE EEEEEEDEEE EEEEEEEEEE EEEEIDVVTV
EKRQKKNEAE VSDSRYPSPL VLKRCHVSTH QHNYAAHPST RHDQPAVKRL RLEASSNNNS
SRSNRHGKQR KCTSPRTSDS EDNDKRRTHN VLERQRRNEL KLSFFALRDE IPEVANNEKA
AKVVILKKAS ECIHSMQLDE QRLLSIKEQL RRKSEQLKHR LQ
//
