ID   MYBE_AVILE              Reviewed;         669 AA.
AC   P01105; Q64998;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 133.
DE   RecName: Full=p135Gag-Myb-Ets-transforming protein;
DE   Contains:
DE     RecName: Full=Transforming protein v-Myb;
DE   Contains:
DE     RecName: Full=Transforming protein v-Ets;
DE   Flags: Fragment;
GN   Name=GAG;
OS   Avian leukemia virus E26.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11913;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6316155; DOI=10.1038/306391a0;
RA   Nunn M.F., Seeburg P.H., Moscovici C., Duesberg P.H.;
RT   "Tripartite structure of the avian erythroblastosis virus E26 transforming
RT   gene.";
RL   Nature 306:391-395(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6097027; DOI=10.1016/0042-6822(84)90378-7;
RA   Nunn M., Weiher H., Bullock P., Duesberg P.;
RT   "Avian erythroblastosis virus E26: nucleotide sequence of the tripartite
RT   onc gene and of the LTR, and analysis of the cellular prototype of the
RT   viral ets sequence.";
RL   Virology 139:330-339(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 589-669, AND VARIANT TS1.1.
RX   PubMed=3203383; DOI=10.1016/0092-8674(88)90259-0;
RA   Golay J., Introna M., Graf T.;
RT   "A single point mutation in the v-ets oncogene affects both erythroid and
RT   myelomonocytic cell differentiation.";
RL   Cell 55:1147-1158(1988).
CC   -!- FUNCTION: DNA-binding protein that specifically recognizes the sequence
CC       5'-YAAC[GT]G-3'. The Myb-Ets protein induces predominantly
CC       erythroblastosis in chicken and transforms avian erythroblasts and
CC       immature myelomonocytic cells in culture. It appears that the Ets
CC       domain is responsible for the effects on erythroid cells and that the
CC       Myb domain encodes the myeloid-transforming capacity.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X00144; CAA24979.1; -; Genomic_DNA.
DR   EMBL; M23542; AAB59928.1; -; Genomic_DNA.
DR   PIR; B01348; TVFVES.
DR   BMRB; P01105; -.
DR   SMR; P01105; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd08542; SAM_PNT-ETS-1; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR045688; Ets1_N_flank.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR046328; ETS_fam.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041886; SAM_PNT-ETS-1.
DR   InterPro; IPR012642; Tscrpt_reg_Wos2-domain.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11849; PTHR11849; 1.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF19525; Ets1_N_flank; 1.
DR   Pfam; PF07988; LMSTEN; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   4: Predicted;
KW   DNA-binding; Host nucleus; Oncogene.
FT   CHAIN           <1..178
FT                   /note="Transforming protein v-Myb"
FT                   /id="PRO_0000019298"
FT   CHAIN           179..669
FT                   /note="Transforming protein v-Ets"
FT                   /id="PRO_0000019299"
FT   DOMAIN          276..361
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        556..640
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..142
FT                   /note="Transcriptional activation domain"
FT                   /evidence="ECO:0000250"
FT   REGION          132..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         628
FT                   /note="H -> D (in mutant TS1.1)"
FT   CONFLICT        610
FT                   /note="D -> N (in Ref. 3; AAB59928)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   669 AA;  74727 MW;  E7AF8A605B72303E CRC64;
     NSTMRRKVEQ EGYLQESSKA GLPSATTGFQ KSSHLMAFAH NPPAGPLPGA GQAPLGSDYP
     YYHIAEPQNV PGQIPYPVAL HVNIVNVPQP AAAAIQRHYN DEDPEKEKRI KELELLLMST
     ENELKGQQAL PTQNHTANYP GWHSTTVADN TMTSGDNAPV SCLGEHHHCT PSPPVDHGTS
     EMMSYYMDTT IGSTGPYPLA RPGVMQGASS CCEDPWMPCR LQSACCPPRS CCPPWDEAAI
     QEVPTGLEHY STDMECADVP LLTPSSKEMM SQALKATFSG FAKEQQRLGI PKDPQQWTET
     HVRDWVMWAV NEFSLKGVDF QKFCMNGAAL CALGKECFLE LAPDFVGDIL WEHLEILQKE
     EAKPYPANGV NAAYPESRYT SDYFISYGIE HAQCVPPSEF SEPSFITESY QTLHPISSEE
     LLSLKYENDY PSVILRDPVQ TDSLQTDYFT IKQEVVTPDN MCMGRVSRGK LGGQDSFESI
     ESYDSCDRLT QSWSSQSSFQ SLQRVPSYDS FDSEDYPAAL PNHKPKGTFK DYVRDRADMN
     KDKPVIPAAA LAGYTGSGPI QLWQFLLELL TDKSCQSFIS WTGDGWEFKL SDPDEVARRW
     GKRKNKPKMD YEKLSRGLRY YYDKNVIHKT AGKRYVYRFV CDLQSLLGYT PEEHSSASGL
     TSSMACSSF