ID B8LFL5_CYPCA Unreviewed; 398 AA.
AC B8LFL5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 28-JUN-2023, entry version 52.
DE SubName: Full=Cellular myelocytomatosis oncogene {ECO:0000313|EMBL:ABP73372.1};
DE Flags: Fragment;
GN Name=c-myc {ECO:0000313|EMBL:ABP73372.1};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|EMBL:ABP73372.1};
RN [1] {ECO:0000313|EMBL:ABP73372.1}
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; EF194882; ABP73372.1; -; Genomic_DNA.
DR AlphaFoldDB; B8LFL5; -.
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 320..372
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..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 398
FT /evidence="ECO:0000313|EMBL:ABP73372.1"
SQ SEQUENCE 398 AA; 45577 MW; C980A63A1AA302F1 CRC64;
MPVSSSLAYK NYDYDYDSIQ PYFYFDNDDE DFYHHQQGQT QPPAPSEDIW KKFELLPTPP
LSPSRRQSLS TAEQLEMVSE FLGDDVVNQS FICDADYSQS FIKSIIIQDC MWSGFSAAAK
LEKVVSERLA SLHAARKELI SDSSSNRLNA SYLQDLSTSA SECIDPSVVF PYPLTESSKS
SKVAPSEPML VLDTPPNSSS SSGSDSEDEE EEEEEEEEEE EEEEEEEEEE EIDVVTVEKR
QKRNEAEVSD SRYPSPLVLK RCHVSTHQHN YAAHPSTRHD QPAVKRLRLE SSSSNNSSSN
RQGKQRKCTS PRTSDSEDND KRRTHNVLER QRRNELKLSF FALRDEIPEV ANNEKAAKVV
ILKKATECIH SMQLDEQRLL SLKEQLRRKS EQLKHRLQ
//
