ID   GAG_FSVGA               Reviewed;         348 AA.
AC   P03337;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 2.
DT   28-JAN-2026, entry version 104.
DE   RecName: Full=Gag polyprotein;
DE   AltName: Full=Core polyprotein;
DE   Contains:
DE     RecName: Full=Matrix protein p15;
DE              Short=MA;
DE   Contains:
DE     RecName: Full=RNA-binding phosphoprotein p12;
DE     AltName: Full=pp12;
DE   Contains:
DE     RecName: Full=Capsid protein p30;
DE              Short=CA;
GN   Name=gag;
OS   Feline sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein
OS   feline leukemia oncovirus B).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11774;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6183005; DOI=10.1016/0092-8674(82)90282-3;
RA   Hampe A., Laprevotte I., Galibert F., Fedele L.A., Sherr C.J.;
RT   "Nucleotide sequences of feline retroviral oncogenes (v-fes) provide
RT   evidence for a family of tyrosine-specific protein kinase genes.";
RL   Cell 30:775-785(1982).
CC   -!- FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed
CC       by the viral protease during virion maturation outside the cell. During
CC       budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
CC       like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
CC       Gag binding host factors. Interaction with HECT ubiquitin ligases
CC       probably link the viral protein to the host ESCRT pathway and
CC       facilitate release. {ECO:0000250|UniProtKB:P03332}.
CC   -!- FUNCTION: [Matrix protein p15]: Targets Gag and gag-pol polyproteins to
CC       the plasma membrane via a multipartite membrane binding signal, that
CC       includes its myristoylated N-terminus. Also mediates nuclear
CC       localization of the pre-integration complex.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-
CC       integration complex (PIC) which tethers the latter to mitotic
CC       chromosomes. {ECO:0000250|UniProtKB:P03332}.
CC   -!- FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion
CC       that encapsulates the genomic RNA-nucleocapsid complex.
CC       {ECO:0000250|UniProtKB:P03336}.
CC   -!- SUBUNIT: [Gag polyprotein]: Interacts (via PPXY motif) with host NEDD4
CC       (By similarity). Interacts (via PSAP motif) with host TSG101 (By
CC       similarity). {ECO:0000250|UniProtKB:P03332}.
CC   -!- SUBUNIT: [Capsid protein p30]: Homohexamer. Further associates as
CC       homomultimer. The virus core is composed of a lattice formed from
CC       hexagonal rings, each containing six capsid monomers.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250}. Host
CC       cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Gag polyprotein;
CC         IsoId=P03337-1; Sequence=Displayed;
CC       Name=Glyco-Gag protein;
CC         IsoId=P0DOH1-1; Sequence=External;
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. RNA-binding
CC       phosphoprotein p12 contains one L domain: a PPXY motif which
CC       potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC       ligase. Matrix protein p15 contains one L domain: a PTAP/PSAP motif,
CC       which potentially interacts with the UEV domain of TSG101.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral
CC       protease yield mature proteins. The protease is released by
CC       autocatalytic cleavage. The polyprotein is cleaved during and after
CC       budding, this process is termed maturation.
CC       {ECO:0000250|UniProtKB:P03332}.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Fes polyprotein.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA43041.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000250|UniProtKB:P03336};
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DR   EMBL; J02086; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; J02087; AAA43041.1; ALT_SEQ; Genomic_RNA.
DR   PIR; A03934; FOMVGC.
DR   SMR; P03337; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; 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; 1.10.150.180; Gamma-retroviral matrix domain; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   InterPro; IPR000840; G_retro_matrix.
DR   InterPro; IPR036946; G_retro_matrix_sf.
DR   InterPro; IPR002079; Gag_p12.
DR   InterPro; IPR003036; Gag_P30.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR050462; Retroviral_Gag-Pol_poly.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01140; Gag_MA; 1.
DR   Pfam; PF01141; Gag_p12; 1.
DR   Pfam; PF02093; Gag_p30; 1.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Capsid protein; Host cell membrane; Host membrane;
KW   Host-virus interaction; Lipoprotein; Membrane; Myristate; RNA-binding;
KW   Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral matrix protein; Viral release from host cell; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03336"
FT   CHAIN           2..348
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000390800"
FT   CHAIN           2..127
FT                   /note="Matrix protein p15"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040844"
FT   CHAIN           128..197
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040845"
FT   CHAIN           198..348
FT                   /note="Capsid protein p30"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040846"
FT   REGION          97..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           118..121
FT                   /note="PTAP/PSAP motif"
FT   MOTIF           157..160
FT                   /note="PPXY motif"
FT   COMPBIAS        100..119
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..132
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..146
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            127..128
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            197..198
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   348 AA;  38886 MW;  C38BBAE39A1CEA25 CRC64;
     MGQTITTPLS LTLDHWSEVR ARAHNQGVEV RKKKWITLCE AEWVMMNVGW PREGTFSLDN
     ISQVEKKIFA PGPYGHPDQV PYITTWRSLA TDPPSWVRPF LPPPKPPTSL PQPLSPQPSA
     PLTSSLYPVL PKSDPPKPPV LPPDPSSPLI DLLTEEPPPY PGGHGPPPSG PRTPTASPIA
     SRLRERRENP AEESQALPLR EGPNNRPQYW PFSASDLYNW KSHNPPFSQD PVALTNLIES
     ILVTHQPTWD DCQQLLQALL TGEERQRVLL EARKQVPGED GRPTQLPNVI DETFPLTRPN
     WDFATPAGRE HLRLYRQLLL AGLRGAARRP TNLAQVKQVV QGKEETPA
//