ID   MYC1_CYPCA              Reviewed;         394 AA.
AC   Q90341;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Transcriptional regulator Myc-1;
DE            Short=c-Myc-1;
DE   AltName: Full=c-Myc I;
GN   Name=myca; Synonyms=cam1, myc1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Hepatopancreas;
RX   PubMed=7875594; DOI=10.1016/0378-1119(94)00813-8;
RA   Zhang H., Okamoto N., Ikeda Y.;
RT   "Two c-myc genes from a tetraploid fish, the common carp (Cyprinus
RT   carpio).";
RL   Gene 153:231-236(1995).
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; D37887; BAA07129.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90341; -.
DR   SMR; Q90341; -.
DR   Ensembl; ENSCCRT00010112801; ENSCCRP00010101549; ENSCCRG00010044683.
DR   Proteomes; UP000694384; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   GO; GO:0032502; P:developmental process; IEA:UniProt.
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; Glycoprotein; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..394
FT                   /note="Transcriptional regulator Myc-1"
FT                   /id="PRO_0000127316"
FT   DOMAIN          310..362
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          177..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..390
FT                   /note="Leucine-zipper"
FT   MOTIF           76..84
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P01106"
FT   COMPBIAS        204..226
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..318
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        58
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  44996 MW;  7146C81C920D71D0 CRC64;
     MPVSASLAYK NYDYDYDSIQ PYFYFDNDDE DFYHHQQGQT QPPAPSEDIW KKFELLPTPP
     LSPSRRQSLS TAEQLEMVSE FLGDDVVNQS FICDADYSQS FIKSIIIQDC MWSGFSAAAK
     LEKVVSERLA SLHAARKELM SDSSSNRLNA SYLQDVSTSA SECIDPSVVF PYPLPESGKS
     SKVAPSEPMP VLDTPPNSSS SSGSDSEEEE EEEEEEEEEE EEEEIDVVTV EKRQKKNETA
     VSDSRYPSPL VLKRCHVSTH QHNYAAHPST RHDQPAVKRL RLEASSNSNS RHVKQRKCTS
     PRTSDSEDND KRRTHNVLER QRRNELKLSF FALRDEIPDV ANNEKAAKVV ILKKATECIH
     SMQLDEQRLL SIKEQLRRKS EQLKHRLQLL RSSH