ID   GAG_AVIER               Reviewed;         555 AA.
AC   P03373; Q85511;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   29-SEP-2021, entry version 142.
DE   RecName: Full=Gag polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p19;
DE   Contains:
DE     RecName: Full=p2A;
DE   Contains:
DE     RecName: Full=p2B;
DE   Contains:
DE     RecName: Full=p10;
DE   Contains:
DE     RecName: Full=V-erbA oncogene;
DE   Flags: Fragment;
GN   Name=gag;
OS   Avian erythroblastosis virus (strain ES4).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=79685;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2884103; DOI=10.1002/j.1460-2075.1987.tb04765.x;
RA   Damm K., Beug H., Graf T., Vennstroem B.;
RT   "A single point mutation in erbA restores the erythroid transforming
RT   potential of a mutant avian erythroblastosis virus (AEV) defective in both
RT   erbA and erbB oncogenes.";
RL   EMBO J. 6:375-382(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-551.
RX   PubMed=6328658; DOI=10.1126/science.6328658;
RA   Debuire B., Henry C., Benaissa M., Biserte G., Claverie J.-M., Saule S.,
RA   Martin P., Stehelin D.;
RT   "Sequencing the erbA gene of avian erythroblastosis virus reveals a new
RT   type of oncogene.";
RL   Science 224:1456-1459(1984).
RN   [3]
RP   FUNCTION.
RX   PubMed=2733791; DOI=10.1038/339593a0;
RA   Damm K., Thompson C.C., Evans R.M.;
RT   "Protein encoded by v-erbA functions as a thyroid-hormone receptor
RT   antagonist.";
RL   Nature 339:593-597(1989).
CC   -!- FUNCTION: Acts as a thyroid-hormone receptor antagonist. The v-ErbA
CC       oncogene cooperates with v-ErbB and other primarily sarcoma-inducing
CC       oncogenes in transformation of erythroblasts. It is non transforming by
CC       itself and cannot induce self-renewal of erythroblasts. Instead it
CC       blocks the residual capacity of the v-ErbB cells to differentiate
CC       terminally. {ECO:0000269|PubMed:2733791}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC   -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC       sequence motifs essential for viral particle budding. They recruit
CC       proteins of the host ESCRT machinery (Endosomal Sorting Complex
CC       Required for Transport) or ESCRT-associated proteins. Gag contains one
CC       L domain: a PPXY motif which potentially interacts with the WW domain 3
CC       of NEDD4 E3 ubiquitin ligase (Potential). {ECO:0000305}.
CC   -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC       mature proteins. {ECO:0000250|UniProtKB:P03322}.
CC   -!- MISCELLANEOUS: THRA, the cellular counterpart of v-ErbA, is a thyroid
CC       hormone receptor alpha.
CC   -!- MISCELLANEOUS: [Gag polyprotein]: This protein is synthesized as a Gag-
CC       vErbA-vErbB polyprotein. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42393.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Y00044; CAA68260.1; -; Genomic_DNA.
DR   EMBL; K02006; AAA42393.1; ALT_FRAME; Genomic_RNA.
DR   PIR; A03248; TVFVVR.
DR   SMR; P03373; -.
DR   BindingDB; P03373; -.
DR   ChEMBL; CHEMBL5824; -.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016032; P:viral process; IEA:InterPro.
DR   Gene3D; 1.10.375.10; -; 1.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR001728; ThyrH_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   PRINTS; PR00546; THYROIDHORMR.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF47943; SSF47943; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS51843; NR_LBD; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Hormone; Metal-binding; Oncogene; Receptor; Repressor;
KW   Thyroid hormone; Transcription; Transcription regulation; Virion; Zinc;
KW   Zinc-finger.
FT   CHAIN           <1..555
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000442133"
FT   CHAIN           <1..71
FT                   /note="Matrix protein p19"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000289147"
FT   CHAIN           72..80
FT                   /note="p2A"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000289148"
FT   CHAIN           81..93
FT                   /note="p2B"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000289149"
FT   CHAIN           94..154
FT                   /note="p10"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000289150"
FT   CHAIN           155..555
FT                   /note="V-erbA oncogene"
FT                   /id="PRO_0000053445"
FT   DOMAIN          317..555
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   ZN_FING         37..57
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         75..99
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   DNA_BIND        204..281
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          14..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           88..91
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   COMPBIAS        30..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   555 AA;  61661 MW;  AA751B8343B68C73 CRC64;
     REEQVTSEQA KFWLGLGGGR VSPPGPECIE KPATERRIDK GEEMGETTVQ RDAKMAPEKM
     ATPKTVGTSC YQCGTATGCN CVTASAPPPP YVGSGLYPSL AGAGEQGQGG DTPRGAEQPR
     AEPGHAGQAP GPALTDWARI REELASTGPP VVAMPVVIKT EGPAWTPLEP EDTRWLDGKH
     KRKSSQCLVK SSMSGYIPSC LDKDEQCVVC GDKATGYHYR CITCEGCKSF FRRTIQKNLH
     PTYSCTYDGC CVIDKITRNQ CQLCRFKKCI SVGMAMDLVL DDSKRVAKRK LIEENRERRR
     KEEMIKSLQH RPSPSAEEWE LIHVVTEAHR STNAQGSHWK QRRKFLLEDI GQSPMASMLD
     GDKVDLEAFS EFTKIITPAI TRVVDFAKNL PMFSELPCED QIILLKGCCM EIMSLRAAVR
     YDPESETLTL SGEMAVKREQ LKNGGLGVVS DAIFDLGKSL SAFNLDDTEV ALLQAVLLMS
     SDRTGLICVD KIEKCQESYL LAFEHYINYR KHNIPHFWSK LLMKVADLRM IGAYHASRFL
     HMKVECPTEL SPQEV