GAG_FSVST
ID GAG_FSVST Reviewed; 297 AA.
AC P03338;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 2.
DT 02-JUN-2021, entry version 97.
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 Snyder-Theilen).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11780;
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 by
CC 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 (By similarity). {ECO:0000250}.
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 preintegration complex (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p30 forms the spherical core of the virion
CC that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- SUBUNIT: Capsid protein p30 is a homohexamer, that further associates
CC as homomultimer. The virus core is composed of a lattice formed from
CC hexagonal rings, each containing six capsid monomers (By similarity).
CC {ECO:0000250}.
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=P03338-1; Sequence=Displayed;
CC Name=Glyco-Gag protein;
CC IsoId=P0DOG9-1; Sequence=External;
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. RNA-binding phosphoprotein p12 contains one
CC L domain: a PPXY motif which potentially interacts with the WW domain 3
CC of NEDD4 E3 ubiquitin ligase. Matrix protein p15 contains one L domain:
CC a PTAP/PSAP motif, which potentially interacts with the UEV domain of
CC TSG101. The junction between the matrix protein p15 and RNA-binding
CC phosphoprotein p12 also contains one L domain: a LYPX(n)L which
CC potentially interacts with PDCD6IP (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. The protease is released by autocatalytic cleavage. The
CC polyprotein is cleaved during and after budding, this process is termed
CC maturation (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein is synthesized as a Gag-Fes polyprotein.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA43046.2; Type=Erroneous gene model prediction; Evidence={ECO:0000250|UniProtKB:P03336};
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DR EMBL; J02088; AAA43046.2; ALT_SEQ; Genomic_RNA.
DR PIR; A03935; FOMVCS.
DR SMR; P03338; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; -; 1.
DR Gene3D; 1.10.375.10; -; 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 Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF01141; Gag_p12; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 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..297
FT /note="Gag polyprotein"
FT /id="PRO_0000390803"
FT CHAIN 2..127
FT /note="Matrix protein p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040857"
FT CHAIN 128..197
FT /note="RNA-binding phosphoprotein p12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040858"
FT CHAIN 198..297
FT /note="Capsid protein p30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040859"
FT REGION 97..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..297
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..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..174
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 297 AA; 33115 MW; A738F562DAECEC57 CRC64;
MGQTVTTPLS LTLDHWSEVR ARAHNQGVEV RKKKWITLCK AEWVMMNVGW PREGTFSLDN
ISQVKKKIFA PGPHGHPDQV PYITTWRSLA TDPPSWVRPF LPPPKPPTPL PQPLSPQPSA
PLTSSLYPVV PKPDPPKPPV LPPDPSSPLI DLLTEEPPPY PGGHGPPPSG PRTPAASPIV
SRLRERRENP AEESQALPLR EGPNNRPQYW PFSASDLYNW KSHNPPFSQD PVALTNLIES
ILVTHQPTWD DCQQLLQALL TGEERQRVLL EARKQVPGED GRPTQLPNVI DETFPLT
