ID   GAG_FUJSV               Reviewed;         309 AA.
AC   P03326; Q85558;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 96.
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   Fujinami sarcoma virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11885;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6291784; DOI=10.1016/0092-8674(82)90283-5;
RA   Shibuya M., Hanafusa H.;
RT   "Nucleotide sequence of Fujinami sarcoma virus: evolutionary relationship
RT   of its transforming gene with transforming genes of other sarcoma
RT   viruses.";
RL   Cell 30:787-795(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-p19 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
CC       mature proteins. {ECO:0000250|UniProtKB:P03322}.
CC   -!- MISCELLANEOUS: [Gag polyprotein]: This protein is synthesized as a Gag-
CC       vFps polyprotein. {ECO:0000305}.
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DR   EMBL; J02194; AAA42402.1; ALT_TERM; Genomic_RNA.
DR   PIR; A03926; FOFVF.
DR   RefSeq; NP_056889.1; NC_001403.1.
DR   SMR; P03326; -.
DR   GeneID; 1491921; -.
DR   KEGG; vg:1491921; -.
DR   Proteomes; UP000124870; Genome.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
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   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; 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   Capsid protein; 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..309
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000442128"
FT   CHAIN           1..151
FT                   /note="Matrix protein p19"
FT                   /id="PRO_0000040860"
FT   CHAIN           152..162
FT                   /note="p2A"
FT                   /id="PRO_0000442129"
FT   CHAIN           163..173
FT                   /note="p2B"
FT                   /id="PRO_0000442130"
FT   CHAIN           174..235
FT                   /note="p10"
FT                   /id="PRO_0000040861"
FT   CHAIN           236..309
FT                   /note="Capsid protein p27, truncated"
FT                   /id="PRO_0000040862"
FT   REGION          127..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           168..171
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            151..152
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            162..163
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            173..174
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
FT   SITE            235..236
FT                   /note="Cleavage; by viral protease p15"
FT                   /evidence="ECO:0000250|UniProtKB:P03322"
SQ   SEQUENCE   309 AA;  32082 MW;  4FA60BC95B618A5C CRC64;
     MEAVIKVISS ACKTYCGKTS PSKKEIGAML SQLQKEGLLM SLSDLYSPGS WDPITAALTQ
     RAMVLGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ECIEKPATER
     RIDKGETTVQ RDTKMAPEET ATPKTVGTSC YHCGTAIGCN CATASAPPPP YVGSGLYPSL
     AGVGEQQGQG GDTPRGAEQP RAEPGRTGLA PGPALTDWAR IREELASTGP PMVAMPVVIK
     TEGPAWTPLE PKLIAGLAGA VGAGGLRSPI AVAGVEALMS SPLLPHDVTN PMRVILGPAP
     HALWMDAWA