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