GAG_SFV3L
ID GAG_SFV3L Reviewed; 643 AA.
AC P27400;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Pr71Gag;
DE Contains:
DE RecName: Full=Gag protein;
DE AltName: Full=p68;
DE Contains:
DE RecName: Full=p3;
GN Name=gag;
OS Simian foamy virus type 3 (strain LK3) (SFVagm) (SFV-3).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=11644;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1310187; DOI=10.1016/0042-6822(92)90026-l;
RA Renne R., Friedl E., Schweizer M., Fleps U., Turek R., Neumann-Haefelin D.;
RT "Genomic organization and expression of simian foamy virus type 3 (SFV-
RT 3).";
RL Virology 186:597-608(1992).
RN [2]
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 [3]
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA47795.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M74895; AAA47795.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_001956721.2; NC_010820.1.
DR SMR; P27400; -.
DR GeneID; 6386656; -.
DR KEGG; vg:6386656; -.
DR Proteomes; UP000007217; 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; Reference proteome; RNA-binding;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral nucleoprotein; Viral release from host cell; Virion;
KW Virus entry into host cell.
FT CHAIN 1..643
FT /note="Gag polyprotein"
FT /id="PRO_0000125477"
FT CHAIN 1..610
FT /note="Gag protein"
FT /id="PRO_0000245441"
FT CHAIN 611..643
FT /note="p3"
FT /id="PRO_0000245442"
FT REGION 31..54
FT /note="Involved in viral assembly and export"
FT /evidence="ECO:0000255"
FT REGION 180..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..493
FT /note="Nucleic acid-binding; GR-box 1"
FT /evidence="ECO:0000250"
FT REGION 523..544
FT /note="GR-box 2"
FT REGION 575..607
FT /note="GR-box 3"
FT MOTIF 251..254
FT /note="PTAP/PSAP motif"
FT MOTIF 523..544
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 191..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 293..294
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 321..322
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 334..335
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 610..611
FT /note="Cleavage; by viral protease; partial"
SQ SEQUENCE 643 AA; 69786 MW; C53A0575BA9B5949 CRC64;
MGDHNLNVQE LLNLFQNLGI PRQPNHREVI GLRMLGGWWG PGTRYILVSI FLQDDSGQPL
QQPRWRPEGR PVNPLVHNTI EAPWGELRQA FEDLDVAEGT LRFGPLANGN WIPGDEYSME
FQPPLAQEIA QMQRDELEEI LDITGQICAQ VIDLVDMQDA QIRGLERRIQ DRLGLRDNLP
VAGIQAPPSS PIGQPIASSS LQPIPGSSSS PADLDGIWTP RQIDPRLSRV AYNPFLPGSS
DGSGGSIPVQ PSAPPAVLPS LPSLPAPVSQ PIIQYVAQPP VPAPQAIPIQ HIRAVTGNTP
TNPRDIPMWL GRHSAAIEGV FPMTTPDLRC RVVNALIGGS LGLSLEPIHC VNWAAVVAAL
YVRTHGSYPI HELANVLRAV VTQEGVATGF QLGIMLSNQD YNLVWGILRP LLPGQAVVTA
MQQRLDQEVN DAARITSFNG HLNDIYQLLG LNARGQSIAR AQSASTSGNS ASAGRGRRGQ
RTQQQAGRQQ QQQTRRTNQG NQGQRDNNQR QSSGGNQGQR GQGGYDLRPR TYQPQRYGGG
RGRRWNDNQQ QQQAQPGRSS DQPRSQSQQP QPEARGDQSR TSGAGRGQQG RGNQNRNQRR
ADANNTRNVD TVTATTTSSS TASSGQNGSS TTPPASGSRN QGD
