ID   GAG_FSVMD               Reviewed;         459 AA.
AC   P03340;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 2.
DT   27-MAR-2024, entry version 101.
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;
DE   Contains:
DE     RecName: Full=Nucleocapsid protein p10-gag;
DE              Short=NC-gag;
GN   Name=gag;
OS   Feline sarcoma virus (strain McDonough).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Feline leukemia virus.
OX   NCBI_TaxID=11778;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6582485; DOI=10.1073/pnas.81.1.85;
RA   Hampe A., Gobet M., Sherr C.J., Galibert F.;
RT   "Nucleotide sequence of the feline retroviral oncogene v-fms shows
RT   unexpected homology with oncogenes encoding tyrosine-specific protein
RT   kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:85-89(1984).
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   -!- FUNCTION: [Nucleocapsid protein p10-gag]: Involved in the packaging and
CC       encapsidation of two copies of the genome. Binds with high affinity to
CC       conserved UCUG elements within the packaging signal, located near the
CC       5'-end of the genome. This binding is dependent on genome dimerization.
CC       {ECO:0000250|UniProtKB:P03332}.
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=P03340-1; Sequence=Displayed;
CC       Name=Glyco-Gag protein;
CC         IsoId=P0DOH2-1; 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-Fms polyprotein.
CC   -!- CAUTION: This gag polyprotein encodes a truncated nucleoprotein.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA43045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000250|UniProtKB:P03336};
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DR   EMBL; K01643; AAA43045.1; ALT_SEQ; Genomic_RNA.
DR   PIR; A03938; FOMVMD.
DR   SMR; P03340; -.
DR   ELM; P03340; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; 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; IPR010999; Retrovr_matrix.
DR   PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR33166:SF8; POM121 TRANSMEMBRANE NUCLEOPORIN LIKE 2; 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 nucleoprotein; Viral release from host cell;
KW   Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03336"
FT   CHAIN           2..459
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000390802"
FT   CHAIN           2..127
FT                   /note="Matrix protein p15"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040852"
FT   CHAIN           128..197
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040853"
FT   CHAIN           198..445
FT                   /note="Capsid protein p30"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040854"
FT   CHAIN           446..459
FT                   /note="Nucleocapsid protein p10-gag"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040855"
FT   REGION          97..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           118..121
FT                   /note="PTAP/PSAP motif"
FT   MOTIF           126..130
FT                   /note="LYPX(n)L motif"
FT   MOTIF           157..160
FT                   /note="PPXY motif"
FT   COMPBIAS        97..173
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..443
FT                   /note="Basic and acidic 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   SITE            445..446
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   459 AA;  52197 MW;  A10AAF4A18E75305 CRC64;
     MGQTVTTPPS LTLDHWSEVR TRAHNQGIEV RKKKWITLCE AEWVMMNVGW PREGTPPLDN
     TSQVEKRIFA PGPHGHPDQV PYITTWRSLA TDPPSWVRPF LPPPKPPTPL PQPLSPQPSA
     PPTSSLYPVL PKTNPPKPPV LPPDPSSPLI DLLTEEPPPY PGGHGPPPSG LRTPAASPIA
     SRLRERRENP AEESQALPLR EGPNNRPQYW PFSASDLYNW KLHNPPFSQD PVALTNLIES
     ILVTHQPTWD DCQQLLQALL TAEERQRVLL EARKQVPGED GRPTQLPNVI DEAFPLTRPN
     WDFATPAGRE HLRLYRQLLL AGLRGAARRP TNLAQVKQVV QGKEETPASF LERLKEAYRM
     YTPYDPEDPG QAASVILSFI YQSSPDIRNK LQRLEGLQGF TLSDLLKEAE KIYNKRETPE
     EREERLWQRQ EERDKKRHKE MTKVLATVVT QNRNKDREE
//