GAG_SFV1
ID GAG_SFV1 Reviewed; 647 AA.
AC Q00071;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Pr71Gag;
DE Contains:
DE RecName: Full=Gag protein;
DE AltName: Full=p68Gag;
DE Contains:
DE RecName: Full=p3;
DE AltName: Full=p3Gag;
GN Name=gag;
OS Simian foamy virus type 1 (SFVmac) (SFV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=338478;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9539; Macaca (macaques).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1647358; DOI=10.1016/0378-1119(91)90410-d;
RA Kupiec J.-J., Kay A., Hayat M., Ravier R., Peries J., Galibert F.;
RT "Sequence analysis of the simian foamy virus type 1 genome.";
RL Gene 101:185-194(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1653483; DOI=10.1016/0042-6822(91)90417-a;
RA Mergia A., Luciw P.A.;
RT "Replication and regulation of primate foamy viruses.";
RL Virology 184:475-482(1991).
RN [3]
RP REVIEW.
RX PubMed=12908768; DOI=10.1007/978-3-642-55701-9_3;
RA Fluegel R.M., Pfrepper K.-I.;
RT "Proteolytic processing of foamy virus Gag and Pol proteins.";
RL Curr. Top. Microbiol. Immunol. 277:63-88(2003).
RN [4]
RP REVIEW.
RX PubMed=15358259; DOI=10.1016/j.mib.2004.06.009;
RA Delelis O., Lehmann-Che J., Saib A.;
RT "Foamy viruses-a world apart.";
RL Curr. Opin. Microbiol. 7:400-406(2004).
CC -!- FUNCTION: Involved in capsid formation and genome binding. Shortly
CC after infection, interaction between incoming particle-associated Gag
CC proteins and host dynein allows centrosomal targeting of the viral
CC genome (associated to Gag), prior to nucleus translocation and
CC integration into host genome (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Gag protein specifically interacts with the N-terminus of
CC leader peptide. This specific interaction between Gag protein and Env
CC glycoprotein may compensate for the lack of a Gag membrane targeting
CC signal, and allow particle egress. The capsid is composed of multimeric
CC Gag protein. Interacts with host TSG101. Interacts with host light
CC chain cytoplasmic dynein DYNLL1; this interaction is critical for
CC intracellular microtubule-dependent viral genome transport toward the
CC centrosome (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Gag protein]: Virion {ECO:0000250}. Host nucleus
CC {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=Gag protein is
CC nuclear at initial phase, cytoplasmic at assembly. Shortly after
CC infection, Gag protein is targeted to centrosomes. It is then actively
CC transported into the nucleus thanks to its nuclear localization signal.
CC In the late phases of infection, Gag proteins assemble in the cytoplasm
CC to form the virion's capsids (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [p3]: Virion {ECO:0000250}.
CC -!- DOMAIN: Gag protein contains 3 glycine-arginine motifs (GR-boxes)
CC necessary for RNA packaging, the first of which has nucleic acid
CC binding properties in vitro. {ECO:0000250}.
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 protein contains a PTAP/PSAP motif,
CC which interacts with the UEV domain of TSG101 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by viral protease yield
CC mature proteins. The protease is not cleaved off from Pol. Since
CC cleavage efficiency is not optimal for all sites, intermediary
CC molecules are expressed (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Foamy viruses are distinct from other retroviruses in
CC many respects. Their protease is active as an uncleaved Pro-Pol
CC protein. Mature particles do not include the usual processed retroviral
CC structural protein (MA, CA and NC), but instead contain two large Gag
CC proteins. Their functional nucleic acid appears to be either RNA or
CC dsDNA (up to 20% of extracellular particles), because they probably
CC proceed either to an early (before integration) or late reverse
CC transcription (after assembly). Foamy viruses have the ability to
CC retrotranspose intracellularly with high efficiency. They bud
CC predominantly into the endoplasmic reticulum (ER) and occasionally at
CC the plasma membrane. Budding requires the presence of Env proteins.
CC Most viral particles probably remain within the infected cell.
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DR EMBL; X58484; CAA41393.1; -; Genomic_DNA.
DR EMBL; X54482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; YP_001961121.1; NC_010819.1.
DR SMR; Q00071; -.
DR PRIDE; Q00071; -.
DR Proteomes; UP000007216; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044163; C:host cytoskeleton; IEA:InterPro.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019076; P:viral release from host cell; IEA:InterPro.
DR InterPro; IPR004957; Gag.
DR Pfam; PF03276; Gag_spuma; 1.
PE 3: Inferred from homology;
KW Capsid protein; Cytoplasmic inwards viral transport; DNA-binding;
KW Host cytoplasm; Host nucleus; Host-virus interaction;
KW Microtubular inwards viral transport; RNA-binding; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral nucleoprotein;
KW Viral release from host cell; Virion; Virus entry into host cell.
FT CHAIN 1..647
FT /note="Gag polyprotein"
FT /id="PRO_0000125476"
FT CHAIN 1..616
FT /note="Gag protein"
FT /id="PRO_0000245439"
FT CHAIN 617..647
FT /note="p3"
FT /id="PRO_0000245440"
FT REGION 33..56
FT /note="Involved in viral assembly and export"
FT /evidence="ECO:0000255"
FT REGION 175..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..500
FT /note="Nucleic acid-binding; GR-box 1"
FT /evidence="ECO:0000250"
FT REGION 536..557
FT /note="GR-box 2"
FT REGION 581..613
FT /note="GR-box 3"
FT MOTIF 258..261
FT /note="PTAP/PSAP motif"
FT MOTIF 536..557
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 180..194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 301..302
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 329..330
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 342..343
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 616..617
FT /note="Cleavage; by viral protease; partial"
FT /evidence="ECO:0000250"
FT CONFLICT 334
FT /note="S -> P (in Ref. 2; CAA41393)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="R -> G (in Ref. 2; CAA41393)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="R -> G (in Ref. 2; CAA41393)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="R -> G (in Ref. 2; CAA41393)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="E -> G (in Ref. 2; CAA41393)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="E -> G (in Ref. 2; CAA41393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 69236 MW; 961B35349E742E73 CRC64;
MAAIEGDLDV QALANLFNDL GINRNPRHRE VIALRMTGGW WGPATRYNLV SLLLQDDQGQ
PLPQPRWRAE GRAANPAVMF TLEAPWQDLR LAFDNIDVGE GTLRFGPLAN GNYIPGDEFS
LEFLPPAMQE ITQMQRDELE EVLDVVGQIT MQMNDLIGMQ DAQIRGLEGQ LRGLRGNLPV
AGTPPPPPPS LDLQPAAASS PYVAPAPSAP AASAAAADLG WFAGGPGPGS LDPRLARVAY
NPFLPGPSDG SGAAPAQPSA PPVASPLPSL LPAQPMQPVI QYVHPPPINP AQQVIPIQHI
RAVTGNAPSN PREIPMWIGR NASAIEGVFP IPTSDIRSRV INALLGRQLG LNLDPQHCIT
WASAIATLYV RTHGSYPLHQ LAEVLRRVSN SEGAAAAWQL GMMLTNQDYN LVWGMVRPLL
PGQAVVTAMQ HRLDQEVSDA ARIVSFVNHL NAVYELLGLN ARGQNLRVST GGQTTARTSA
GRGARGRRSQ QGTPGRQSSG QAPPQGRRSS QGQQPRQSES GDQNNQRQLQ GGNNRGGYNL
RPRTYQPQRY GGGRGRRWND QTARADNQQR SQSQQPQSEA RGEQSRTSGA GREQGGRGNQ
NRNQRSAGEN TDRSVNTVTA TSASISASGQ NGSSTTPPAS GSGNQGN
