ID   MYC_FLV                 Reviewed;         439 AA.
AC   P68272; P06877; P06878; Q28413;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   02-JUN-2021, entry version 80.
DE   RecName: Full=Viral myc transforming protein;
DE            Short=v-Myc;
GN   Name=MYC;
OS   Feline leukemia virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11768;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2989554; DOI=10.1128/jvi.55.1.177-183.1985;
RA   Braun M.J., Deininger P.L., Casey J.W.;
RT   "Nucleotide sequence of a transduced myc gene from a defective feline
RT   leukemia provirus.";
RL   J. Virol. 55:177-183(1985).
CC   -!- FUNCTION: Participates in the regulation of gene transcription. Binds
CC       DNA in a non-specific manner, yet also specifically recognizes the core
CC       sequence CAC[GA]TG. Seems to activate the transcription of growth-
CC       related genes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-vMyc chimeric
CC       protein. The sequence shown here corresponds to the Myc homolog
CC       fragment of the chimera.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA43059.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M10973; AAA43059.1; ALT_INIT; Genomic_DNA.
DR   SMR; P68272; -.
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; 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; Host nucleus; Oncogene; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..439
FT                   /note="Viral myc transforming protein"
FT                   /id="PRO_0000127311"
FT   DOMAIN          354..406
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          201..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..434
FT                   /note="Leucine-zipper"
FT   COMPBIAS        201..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   439 AA;  48520 MW;  4B263D36F1A1F36E CRC64;
     MPLNVSFANR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP
     LSPSRRSGLC SPSYVAFASF SPRGDDDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD
     DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPSPARGPGG CPTSSLYLQD
     LTAAASECID PSVVFPYPLN DSSSPKPCAS PDSAAFSPSS DSLLSSAESS PRASPEPLAL
     HEETPPTTSS DSEEEQEEEE EIDVVSVEKR QPPAKRSESG SPSAGGHSKP PHSPLVLKRC
     HVPTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCISPRSSDT EENDKRRTHN
     VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAGE QKLISEKDLL
     RKRREQLKHK LEQLRNSCA