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MYC_AVIOK
ID   MYC_AVIOK               Reviewed;         416 AA.
AC   P12523;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   23-FEB-2022, entry version 115.
DE   RecName: Full=Viral myc transforming protein;
DE            Short=v-Myc;
GN   Name=MYC;
OS   Avian retrovirus OK10.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC   unclassified Alpharetrovirus.
OX   NCBI_TaxID=11871;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2986131; DOI=10.1073/pnas.82.9.2718;
RA   Hayflick J., Seeburg P.H., Ohlsson R., Pfeifer-Ohlsson S., Watson D.,
RA   Papas T., Duesberg P.H.;
RT   "Nucleotide sequence of two overlapping myc-related genes in avian
RT   carcinoma virus OK10 and their relation to the myc genes of other viruses
RT   and the cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:2718-2722(1985).
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-Pol-vMyc-Env
CC       chimeric protein. The sequence shown here corresponds to the Myc
CC       homolog fragment of the chimera.
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DR   EMBL; M11352; AAA42391.1; -; Genomic_RNA.
DR   PIR; A22669; TVFVAC.
DR   SMR; P12523; -.
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   DNA-binding; Host nucleus; Oncogene.
FT   CHAIN           1..416
FT                   /note="Viral myc transforming protein"
FT                   /id="PRO_0000127310"
FT   DOMAIN          331..383
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          144..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..411
FT                   /note="Leucine-zipper"
FT   COMPBIAS        153..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..244
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  46040 MW;  C09350E8D9691214 CRC64;
     MPLSASLPSK NYDYDYDSVQ PYFYFEEEEE NFYLAAQQRG SELQPPAPSE DIWKKFELLP
     APPLSPSRRS SLAAASCFPS TADQLEMVTE LLGGDMVNQS FICDPDDESF VKSIIIQDCM
     WSGFSAAAKL EKVVSEKLAT YQASRREGGP AAASRPGPPP SGPPPPPAGP AASAGLYLHD
     LGAAAADCID PSVVFPYPLS ERAPRAAPPG ANPAALLGVD TPPTTSSDSE EEQEEDEEID
     VVTLAEANES ESSTESSTEA SEEHCKPHHS PLVLKRCHVN IHQHNYAAPP STKVEYPAAK
     RLKLDSGRVL KQISNNRKCS SPRTSDSEEN DKRRMHNVLE RQRRNELKLS FFALRDQIPE
     VANNEKAPKV VILKKATEYV LSIQSDEHRL IAEKEQLRRR REQLKHKLEQ LRNSRA
 
 
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