ID   MYC_ONCMY               Reviewed;         414 AA.
AC   P06646;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Transcriptional regulator Myc;
DE            Short=c-Myc;
DE   Flags: Fragment;
GN   Name=myc;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3520551; DOI=10.1073/pnas.83.11.3698;
RA   van Beneden R.J., Watson D.K., Chen T.T., Lautenberger J.A., Papas T.S.;
RT   "Cellular myc (c-myc) in fish (rainbow trout): its relationship to other
RT   vertebrate myc genes and to the transforming genes of the MC29 family of
RT   viruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3698-3702(1986).
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:0000250|UniProtKB:P01106}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Binds DNA as a heterodimer with MAX (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:P01106}.
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DR   EMBL; M13048; AAA49604.1; -; Genomic_DNA.
DR   PIR; A25272; TVTRMC.
DR   AlphaFoldDB; P06646; -.
DR   SMR; P06646; -.
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-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 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   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; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN           <1..414
FT                   /note="Transcriptional regulator Myc"
FT                   /id="PRO_0000127318"
FT   DOMAIN          324..376
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          192..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..404
FT                   /note="Leucine-zipper"
FT   MOTIF           77..85
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P01106"
FT   COMPBIAS        219..237
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   414 AA;  46643 MW;  06830232DB3D961A CRC64;
     NSSLASKNYD YDYDSIQPYF YVDNEDEDFY HQQPGQLQPP APSEDIWKKF ELLPTPPLSP
     SRPSLSSIFP STADQLEMVT EFLGDDVVNQ SFICDADYSQ TFLKSIIIQD CMWSGFSATA
     KLEKVVSERL ASLQTARKDS AVGDNAECPT RLNANYLQDP NTSASECIGP NTSASECIGP
     SVVFPYPITE TPKPSKVAPP TDLALDTPPN SGSSSSSGSD SEDDDEEEDD EDEEEIDVVT
     VEKRQAVKRC DPSTSETRHH SPLVLKRCHV STHQHNYAAH PSTRHEQPAV KRLRLENSSS
     RVLKQISSNR KCSSPRTSDT EDYDKRRTHN VLERQRRNEL KLSFFALRDE IPDVANNEKA
     AKVVILKKAT ECIYSMQTDE QRLVNLKEQL RRKSEHLKQK LAQLQNSCLS SKRH