ID Q2L4Q4_ONCMY Unreviewed; 407 AA.
AC Q2L4Q4;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 03-MAY-2023, entry version 76.
DE RecName: Full=Transcriptional regulator {ECO:0000256|PIRNR:PIRNR001705};
GN Name=myc {ECO:0000313|EMBL:CAF25507.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CAF25507.1};
RN [1] {ECO:0000313|EMBL:CAF25507.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang T., Secombes C.J.;
RT "Sequence analysis of rainbow trout genes modulated by bacterial
RT infection.";
RL Submitted (FEB-2004) 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, ECO:0000256|PIRNR:PIRNR001705}.
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|PIRNR:PIRNR001705}.
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DR EMBL; AJ627208; CAF25507.1; -; mRNA.
DR RefSeq; NP_001118094.1; NM_001124622.1.
DR AlphaFoldDB; Q2L4Q4; -.
DR SMR; Q2L4Q4; -.
DR GeneID; 100136645; -.
DR KEGG; omy:100136645; -.
DR CTD; 4609; -.
DR OrthoDB; 3039999at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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 2: Evidence at transcript level;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR001705};
KW Nucleus {ECO:0000256|PIRNR:PIRNR001705}.
FT DOMAIN 317..369
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 185..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 369..400
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 212..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 46082 MW; 474F54FD48FE9E92 CRC64;
MPLNSSLASK NYDYDYDSIQ PYFYVDNEDE DFYHQQPGQL QPPAPSEDIW KKFELLPTPP
LSPSRPSLSS IFPSTADQLE MVTEFLGDDV VNQSFICDAD YSQTFLKSII IQDCMWSGFS
ATAKLEKVVS ERLASLQTAR KDSAVGDNAE CPTRLNANYL QDPNTSASEC IDPSVVFPYP
ITETPKPSKV APPTDLALDT PPNSGSSSSS GSDSEDDDEE EDDEDEEEID VVTVEKRQAV
KRCDPSTSET RHHSPLVLKR CHVSTHQHNY AAHPSTRHEQ PAVKRLRLEN SSSRVLKQIS
SNRKCSSPRT SDTEDYDKRR THNVLERQRR NELKLSFFAL RDEIPDVANN EKAAKVVILK
KATECIYSMQ TDEQRLVNLK EQLRRKSEHL KQKLAQLQNS CLSSKRH
//
