MYC_AVIME
ID MYC_AVIME Reviewed; 412 AA.
AC P0C0N8; P06647;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 02-JUN-2021, entry version 78.
DE RecName: Full=Viral myc transforming protein;
DE Short=v-Myc;
GN Name=MYC;
OS Avian retrovirus MH2E21.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=11916;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3016301; DOI=10.1128/jvi.59.2.341-353.1986;
RA Patschinsky T., Jansen H.W., Bloecker H., Frank R., Bister K.;
RT "Structure and transforming function of transduced mutant alleles of the
RT chicken c-myc gene.";
RL J. Virol. 59:341-353(1986).
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-vMyc chimeric
CC protein. The sequence shown here corresponds to the Myc homolog
CC fragment of the chimera.
CC -!- MISCELLANEOUS: The MH2E21 virus appears to be a recombinant between
CC ring-necked pheasant virus and a deletion mutant of MH2 that was
CC constructed in vitro. The MH2E21 virus lacks Gag, Pol and Env genes,
CC and thus needs a helper virus to reproduce.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42389.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M14008; AAA42389.1; ALT_INIT; Genomic_RNA.
DR PIR; A29285; TVFV2E.
DR SMR; P0C0N8; -.
DR PRIDE; P0C0N8; -.
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_0000127305"
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..263
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; 45162 MW; 19A1248A5E9A0FB1 CRC64;
MPLSVSLPSK NYDYDYDSVQ PYFYFEEEEE NFYLAAQQRS SELQPPAPSE DIWKKFELLP
APPLSPSCRS NLAAASCFPS TADQLEMVTE LLGGDMVNQS SICDPDDESF VKSIIIRDCM
WSGFSAAAKL EKVVSEKLAT YKASRREGGP AAASRPGPPP SGPPPPPAGP AASAGLYLHD
LGAAAAGCIG SSVVFPCPLG RRGPPGAGPA ALLGVDAPPT AGGGSEEEQE EDEEIDVVTL
AEANESESST ESSTEASEEH CKPHHSPLVL ERCHVNIHQH NYAAPPSTKV EYPAAKRLKL
DSGRVLKQVS NNRKCSSPRT SDSEVNDKRR THNVLERQRR NELKLSFFAL RDQIPEVANN
EKAPKVVILK RATEYVLSIQ SDEHRLIAEK EQLRRRREQL KHKLEQLRNS RA