ID   MYC_AVIMH               Reviewed;         412 AA.
AC   P0C0N9; P06647;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   02-JUN-2021, entry version 74.
DE   RecName: Full=Viral myc transforming protein;
DE            Short=v-Myc;
GN   Name=MYC;
OS   Avian retrovirus MH2.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11870;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6328485; DOI=10.1073/pnas.81.10.3000;
RA   Kan N.C., Flordellis C.S., Mark G.E., Duesberg P.H., Papas T.S.;
RT   "Nucleotide sequence of avian carcinoma virus MH2: two potential onc genes,
RT   one related to avian virus MC29 and the other related to murine sarcoma
RT   virus 3611.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:3000-3004(1984).
CC   -!- FUNCTION: Transforms avian and murine macrophages and fibroblasts as
CC       well as murine B-lymphoid cells. {ECO:0000250}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-vMht-vMyc chimeric
CC       protein. The sequence shown here corresponds to the Myc homolog
CC       fragment of the chimera.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB59930.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; K02082; AAB59930.1; ALT_INIT; Genomic_DNA.
DR   PIR; A29285; TVFV2E.
DR   SMR; P0C0N9; -.
DR   GO; GO:0042025; C:host cell 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   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; 2.
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   DNA-binding; Host nucleus; Oncogene.
FT   CHAIN           1..412
FT                   /note="Viral myc transforming protein"
FT                   /id="PRO_0000127306"
FT   DOMAIN          327..379
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          144..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..407
FT                   /note="Leucine-zipper"
FT   COMPBIAS        153..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..240
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  45133 MW;  DBEBA792C7060AC2 CRC64;
     MPLSVSLPSK NYDYDYDSVQ PYFYFEEEEE NFYSAAQQRS SELQPPAPSE DIWKKFELLP
     APPLSPSCRS NLAAASCFPS TADQLEMVTE LLGGDMVNQS SICDPDDESF VKSIIIRDCM
     WSGFSAAAKL EKVVSEKLAT YKASRREGGP AAASRPGPPP SGPPPPPAGP AASAGLYLHD
     LGAAAAGCIG SSVVFPCPLG RRGPPGAGPA ALLGVDAPPT VGGGSEEEQE EDEEIDVVTL
     AEANESESST ESGTEASEEH CKPHHSPLVL ERCHVNIHQH NYAAPPSTKV EYPAAKRLKL
     DSGRVLKQVS NNRKCSSPRT SDSEVNDKRR THNVLERQRR NELKLSFFAL RDQIPEVANN
     EKAPKVVILK RATEYVLSIQ SDEHRLIAEK EQLRRRREQL KHKLEQLRNS RA