ID   GAG_AVISY               Reviewed;         284 AA.
AC   P03327;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   29-SEP-2021, entry version 84.
DE   RecName: Full=Gag-yes 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, truncated;
DE   Contains:
DE     RecName: Full=V-yes oncogene;
GN   Name=gag;
OS   Avian sarcoma virus (strain Y73).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11884;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=6281656; DOI=10.1038/297205a0;
RA   Kitamura N., Kitamura A., Toyoshima K., Hirayama Y., Yoshida M.;
RT   "Avian sarcoma virus Y73 genome sequence and structural similarity of its
RT   transforming gene product to that of Rous sarcoma virus.";
RL   Nature 297:205-208(1982).
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC   -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC       essential for viral particle budding. They recruit proteins of the host
CC       ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC       ESCRT-associated proteins. Gag contains one L domain: a PPXY motif
CC       which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC       ligase (Potential). {ECO:0000305}.
CC   -!- PTM: Gag polyprotein: Specific enzymatic cleavages in vivo yield mature
CC       proteins. {ECO:0000250|UniProtKB:P03322}.
CC   -!- MISCELLANEOUS: Gag polyprotein: This protein is synthesized as a Gag-
CC       vYes polyprotein. {ECO:0000305}.
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DR   EMBL; V01170; CAA24496.1; ALT_TERM; Unassigned_RNA.
DR   PIR; A03927; FOFVG9.
DR   SMR; P03327; -.
DR   Proteomes; UP000164967; Genome.
DR   GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.90; -; 1.
DR   InterPro; IPR004028; Gag_M.
DR   InterPro; IPR012344; Matrix_HIV/RSV_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   Pfam; PF02813; Retro_M; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
PE   3: Inferred from homology;
KW   Host-virus interaction; Oncogene; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral matrix protein;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..284
FT                   /note="Gag-yes polyprotein"
FT                   /id="PRO_0000442124"
FT   CHAIN           1..155
FT                   /note="Matrix protein p19"
FT                   /id="PRO_0000040824"
FT   CHAIN           156..166
FT                   /note="p2A"
FT                   /id="PRO_0000442125"
FT   CHAIN           167..179
FT                   /note="p2B"
FT                   /id="PRO_0000442126"
FT   CHAIN           180..222
FT                   /note="p10, truncated"
FT                   /id="PRO_0000040825"
FT   CHAIN           223..284
FT                   /note="V-yes oncogene"
FT                   /id="PRO_0000442127"
FT   REGION          128..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           174..177
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   COMPBIAS        191..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            155..156
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            166..167
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            179..180
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            231..232
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
SQ   SEQUENCE   284 AA;  29526 MW;  F01317AB142C69FA CRC64;
     MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS WDPITAALSQ
     RAMVLGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ECIEKPATER
     RIDKGEEVGE TTVQRDAKMA PEETATPKTV GTSCYHCGTA SGCNCATATA SAPPPPYVGS
     GLCPSLAGVG EQRKRGDDTP RGAEQPRAEP RHTGLTLGPA RSARLPPPAP LPSSLPLLPP
     FPPRVAAVPG GAGGAPLPSL SPSFFHPRRR GRAEATVGCI KSKE