MYC_AVIM2
ID MYC_AVIM2 Reviewed; 416 AA.
AC P10395;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 23-FEB-2022, entry version 123.
DE RecName: Full=Viral myc transforming protein;
DE Short=v-Myc;
GN Name=MYC;
OS Avian myelocytomatosis virus CMII.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC unclassified Alpharetrovirus.
OX NCBI_TaxID=11869;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3019003; DOI=10.1016/0042-6822(86)90444-7;
RA Walther N., Jansen H.W., Trachmann C., Bister K.;
RT "Nucleotide sequence of the CMII v-myc allele.";
RL Virology 154:219-223(1986).
CC -!- FUNCTION: Transforms avian and murine macrophages and fibroblasts as
CC well as murine B-lymphoid cells.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA42408.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M15241; AAA42408.1; ALT_INIT; Genomic_RNA.
DR PIR; A24297; TVFV2C.
DR SMR; P10395; -.
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_0000127307"
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..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..340
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"
FT COMPBIAS 322..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 46098 MW; 6DF5E4BD3A1A5883 CRC64;
MPLSASLPSK NYDYDYDSVQ PYFYFEEEEE NFYLAAQQRG SELQPPAPSE DIWKKFELLP
TPPLSPSRRS 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 DKRRTHNVLE RQRRNELKLS FFALRDQIPE
VANNEKAPKV VILKKATEYV LSIQSDEHRL IAEKEQLRRR REQLKHKLEQ LRNSRE