ID   GAG_AVIMC               Reviewed;         453 AA.
AC   P03323;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 89.
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=Capsid protein p27, truncated;
GN   Name=gag;
OS   Avian myelocytomatosis virus MC29.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11868;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6302688; DOI=10.1073/pnas.80.9.2500;
RA   Reddy E.P., Reynolds R.K., Watson D.K., Schultz R.A., Lautenberger J.,
RA   Papas T.S.;
RT   "Nucleotide sequence analysis of the proviral genome of avian
RT   myelocytomatosis virus (MC29).";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:2500-2504(1983).
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 mature
CC       proteins. {ECO:0000250|UniProtKB:P03322}.
CC   -!- MISCELLANEOUS: Gag polyprotein: This protein is synthesized as a Gag-
CC       vMyc polyprotein. {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; V01174; CAA24499.1; -; Genomic_DNA.
DR   BMRB; P03323; -.
DR   SMR; P03323; -.
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; 1.10.1200.30; -; 1.
DR   Gene3D; 1.10.150.90; -; 1.
DR   Gene3D; 1.10.375.10; -; 1.
DR   InterPro; IPR004028; Gag_M.
DR   InterPro; IPR000721; Gag_p24_N.
DR   InterPro; IPR012344; Matrix_HIV/RSV_N.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF02813; Retro_M; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
DR   SUPFAM; SSF47943; SSF47943; 1.
PE   3: Inferred from homology;
KW   Host-virus interaction; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral matrix protein;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..155
FT                   /note="Matrix protein p19"
FT                   /id="PRO_0000040815"
FT   CHAIN           156..166
FT                   /note="p2A"
FT                   /id="PRO_0000442119"
FT   CHAIN           167..177
FT                   /note="p2B"
FT                   /id="PRO_0000442120"
FT   CHAIN           178..239
FT                   /note="p10"
FT                   /id="PRO_0000040816"
FT   CHAIN           240..453
FT                   /note="Capsid protein p27, truncated"
FT                   /id="PRO_0000040817"
FT   REGION          128..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           172..175
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
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            177..178
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            239..240
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
SQ   SEQUENCE   453 AA;  47699 MW;  D82A17164726C1AC CRC64;
     MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS WDPITAALTQ
     RAMVLGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ECIEKPATER
     RIDKGEEVGE TTVQRDAKMA PEETATPKTV GTSCYHCGTA IGCNCATASA PPPPYVGSGL
     YPSLAGVGEQ QGQGGDTPRG AEQPRAEPGH AGQAPGPALT DWARVGEELA STGPPVVAMP
     VVINTEGPAW TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSRLLPH DVTNLMRVIL
     GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLDRLKGLAD GMVGNPQGQA
     ALLRPGELVA ITASALQAFR EVARLAEPAG PWADITQGPS ESFVDFANRL IKAVEGSDLP
     PSARAPVIID CFRQKSQPDI QQLIRAAPST VHG