ID B8LFI6_9TELE Unreviewed; 395 AA.
AC B8LFI6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 28-JUN-2023, entry version 55.
DE SubName: Full=Cellular myelocytomatosis oncogene {ECO:0000313|EMBL:ABP73343.1};
DE Flags: Fragment;
GN Name=c-myc {ECO:0000313|EMBL:ABP73343.1};
OS Elopichthys bambusa (yellowcheek carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Xenocyprididae; Xenocypridinae; Elopichthys.
OX NCBI_TaxID=238031 {ECO:0000313|EMBL:ABP73343.1};
RN [1] {ECO:0000313|EMBL:ABP73343.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF194853; ABP73343.1; -; Genomic_DNA.
DR AlphaFoldDB; B8LFI6; -.
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 317..369
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 177..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 395
FT /evidence="ECO:0000313|EMBL:ABP73343.1"
SQ SEQUENCE 395 AA; 45073 MW; AA65CBFF7BFA4468 CRC64;
MPVSSSLAYK NYDYDYDSIQ PYFYFDNDDE DFYHRQQGQT QPPAPSEDIW KKFELLPTPP
LSPSRRQSLS TAEQLEMVSE ILGDDVVNQS FICDADYSQS FIKSIIIQDC MWSGFSAAAK
LEKVVSERLA SLHAARKELM SDSSSNRLNA SYLQDLSTSA SECIDPSVVF PYPLTESGKG
SKVAPSQPML VLDTPPNSSS SSGSDSEDDD EEEEEEEEEE EEEEEEEEID VVTVEKRQKR
SEMEVSDSRH PSPLVLKRCH VSTHQHNYAA HPSTRHDQPA VKRLRLEASS NNNSSSNRHG
KQRKCASPRT SDSEDNDKRR THNVLERQRR NELKLSFFAL RDEIPEVANN EKAAKVVILK
KATECIHSMQ LDEQRLLSIK EQLRRKSEQL KHKLQ
//
