ID   MYC_FLVTT               Reviewed;         437 AA.
AC   P21438;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   02-JUN-2021, entry version 125.
DE   RecName: Full=Viral myc transforming protein;
DE            Short=v-Myc;
GN   Name=MYC;
OS   Feline leukemia virus FTT.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11923;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2539507; DOI=10.1128/jvi.63.5.2108-2117.1989;
RA   Doggett D.L., Drake A.L., Hirsch V., Rowe M.E., Stallard V., Mullins J.I.;
RT   "Structure, origin, and transforming activity of feline leukemia virus-myc
RT   recombinant provirus FTT.";
RL   J. Virol. 63:2108-2117(1989).
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.
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DR   EMBL; M10973; AAA43059.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M25762; AAA30812.1; -; Genomic_DNA.
DR   PIR; A26268; TVMVFT.
DR   SMR; P21438; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
DR   GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB.
DR   GO; GO:0045656; P:negative regulation of monocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR   GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0032204; P:regulation of telomere maintenance; ISS:UniProtKB.
DR   GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
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..437
FT                   /note="Viral myc transforming protein"
FT                   /id="PRO_0000127312"
FT   DOMAIN          354..406
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          201..358
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   437 AA;  48309 MW;  1C39AD24B1CEB4D7 CRC64;
     MPLNVSFANR NYDLDYDSVQ PYFYCDEEEN FYQQQQQSEL QPPAPSEDIW KKFELLPTPP
     LSPSRRSGLC SPSYVAFASF SPRGDDDGGG GSFSTADQLE MVTELLGGDM VNQSFICDPD
     DETFIKNIII QDCMWSGFSA AAKLVSEKLA SYQAARKDSG SPSPARGPGG CPTSSLYLQD
     LTAAASECID PSVVFPYPLN DSSSPKPCAS PDSAAFSPSS DSLLSSAESS PRASPKPLGL
     HEETPPTTSS DSEEEQEEEE EIDVVSVEKR QPPAKRSESG SPSAGGHSKP PHSPLVLKRC
     HVPTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCISPRSSDT EENDKRRTDN
     VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSVQAGE QKLISEKDLL
     RKRREQLKHK LEQLRNS