ID   MYC2_CYPCA              Reviewed;         401 AA.
AC   Q90342;
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-2;
DE            Short=c-Myc-2;
DE   AltName: Full=c-Myc II;
GN   Name=mycb; Synonyms=cam2, myc2;
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}.
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; D37888; BAA07130.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q90342; -.
DR   SMR; Q90342; -.
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..401
FT                   /note="Transcriptional regulator Myc-2"
FT                   /id="PRO_0000127317"
FT   DOMAIN          317..369
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          177..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..397
FT                   /note="Leucine-zipper"
FT   MOTIF           76..84
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P01106"
FT   COMPBIAS        204..230
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..304
FT                   /note="Polar 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   CARBOHYD        58
FT                   /note="O-linked (GlcNAc) threonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   401 AA;  45812 MW;  92501E4A4FCC75EF CRC64;
     MPVSSSLAYK NYDYDYDSIQ PYFYFDNDDE DFYHHQQGQT QPPAPSEDIW KKFELLPTPP
     LSPSRRQSLS TAEQLEMVSE FLGDDVVNQS FICDADYSQS FIKSIIIQDC MWSGFSAAAK
     LEKVVSEKLA SLHAARKELI SDSSSNRLNA SYLQDLSTSA SECIGPSVVF PYPLTESSKS
     SKVAPSEPML VLDTPPNSSS SSGSDSEDEE EEEEEEEEEE EEEEEEEEID VVTVEKRQKR
     NEAEVSDSRY PSPLVLKRCH VSTHQHNYAA HPSTRHDQPA VKRLRLESSS SNNSSSNRQG
     KQRKCTSPRT SDSEDNDKRR THNVLERQRR NELKLSFFAL RDEIPEVANN EKAAKVVILK
     KATECIHSMQ LDEQRLLSIK EQLRRKSEQL KHRLQQLRSS H