GAG_SFVCP
ID GAG_SFVCP Reviewed; 653 AA.
AC Q87039;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 70.
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 (isolate chimpanzee) (SFVcpz).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=298339;
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8184531; DOI=10.1006/viro.1994.1285;
RA Herchenroder O., Renne R., Loncar D., Cobb E.K., Murthy K.K., Schneider J.,
RA Mergia A., Luciw P.A.;
RT "Isolation, cloning, and sequencing of simian foamy viruses from
RT chimpanzees (SFVcpz): high homology to human foamy virus (HFV).";
RL Virology 201:187-199(1994).
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. Host nucleus. Host
CC cytoplasm. Note=Nuclear at initial phase, cytoplasmic at assembly.
CC Shortly after infection, Gag protein is targeted to centrosomes. It is
CC then actively transported into the nucleus thanks to its nuclear
CC localization signal. In the late phases of infection, Gag proteins
CC assemble in the cytoplasm to form the virion's capsids (By similarity).
CC {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. Nucleocapsid protein p14 contains one L
CC domain: a PTAP/PSAP motif, which interacts with the UEV domain of
CC TSG101 (By similarity). {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; U04327; AAA19977.1; -; Genomic_DNA.
DR RefSeq; NP_056802.1; NC_001364.1.
DR SMR; Q87039; -.
DR GeneID; 1489964; -.
DR KEGG; vg:1489964; -.
DR Proteomes; UP000001063; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IDA:CACAO.
DR GO; GO:0044383; C:host chromosome; IDA:CACAO.
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..653
FT /note="Gag polyprotein"
FT /id="PRO_0000378591"
FT CHAIN 1..626
FT /note="Gag protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000378592"
FT CHAIN 627..653
FT /note="p3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000378593"
FT REGION 37..60
FT /note="Involved in viral assembly and export"
FT /evidence="ECO:0000255"
FT REGION 179..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..515
FT /note="Nucleic acid-binding; GR-box 1"
FT /evidence="ECO:0000250"
FT REGION 540..561
FT /note="GR-box 2"
FT /evidence="ECO:0000250"
FT REGION 591..623
FT /note="GR-box 3"
FT /evidence="ECO:0000250"
FT MOTIF 289..292
FT /note="PTAP/PSAP motif"
FT MOTIF 540..561
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 180..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 316..317
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 344..345
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 357..358
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 626..627
FT /note="Cleavage; by viral protease; partial"
FT /evidence="ECO:0000250"
SQ SEQUENCE 653 AA; 70762 MW; 6D9FFD24EACEBA96 CRC64;
MASGSNVEEY ELDVEALVVI LRDRNIGRNP LHGEIIGLRL TEGWWGQLER FQMVRLILQD
EDNEPLQRPR HEIIPRAVNP HTMFVLSGPL AELQLAFQDL DLPEGPLRFG PLANGHYVEG
DPYSRSYRPV TMAETAQMTR DELEDTLNTQ SEIEIQMINL LELYEVETRA LRRQLAERSS
IGQGGISPGA SHSRPPVSSF SGLPSLPAIP GIHTRAPSPP RATSTPGNIP RSLGDDNMPS
SSFAGPSQPR VSFHPGNPFA EAEGHRPRSQ SRERRRDIPS APVISAPVPS APPMIQYIPV
PPPPPVGAVI PIQHIRSVTG EPPRNPREIP IWLGRNAPAI DGVFPTTTPD LRCRIINALL
GGNLGLSLTP GDCITWDSAV ATLFIRTYGQ YPLHQLGNVL KGIADQEGVA TAYTLGMMLS
GQNYQLVSGI IRGYLPGQAV VTAMQQRLDQ EIDDQTRAET FIQHLNAVYE ILGLNARGQS
IRASVTPQPR PSRGRGRGQS APEPSQGPVN SGRGRQCPAP GQNDRGSNIQ NQGQENSSQG
GYNLRSRTYQ PQRYGGGRGR RWNENTNNSE TRPTEQSPQT PRPIQAGSGV RGNQSQTYKP
AAGRGGRGNQ NRNQRSSGAG DSRAVNTVTQ SATSSTDESS STTTAAPSGG QGN
