GAG_FFV
ID GAG_FFV Reviewed; 514 AA.
AC O56860;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 02-JUN-2021, entry version 76.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Gag protein;
DE AltName: Full=p48Gag;
DE Contains:
DE RecName: Full=p3;
DE AltName: Full=p3Gag;
GN Name=gag;
OS Feline foamy virus (FFV) (Feline syncytial virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Felispumavirus.
OX NCBI_TaxID=53182;
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9261397; DOI=10.1128/jvi.71.9.6727-6741.1997;
RA Winkler I., Bodem J., Haas L., Zemba M., Delius H., Flower R.,
RA Fluegel R.M., Loechelt M.;
RT "Characterization of the genome of feline foamy virus and its proteins
RT shows distinct features different from those of primate Spumaviruses.";
RL J. Virol. 71:6727-6741(1997).
RN [2]
RP INTERACTION OF GAG PROTEIN N-TERMINUS WITH ENV LEADER PEPTIDE.
RX PubMed=11483744; DOI=10.1128/jvi.75.17.7995-8007.2001;
RA Wilk T., Geiselhart V., Frech M., Fuller S.D., Fluegel R.M., Loechelt M.;
RT "Specific interaction of a novel foamy virus Env leader protein with the N-
RT terminal Gag domain.";
RL J. Virol. 75:7995-8007(2001).
RN [3]
RP SUBCELLULAR LOCATION, INTERACTION OF GAG PROTEIN N-TERMINUS WITH ENV LEADER
RP PEPTIDE, AND MUTAGENESIS OF ARG-43.
RX PubMed=12781711; DOI=10.1016/s0042-6822(03)00125-9;
RA Geiselhart V., Schwantes A., Bastone P., Frech M., Loechelt M.;
RT "Features of the Env leader protein and the N-terminal Gag domain of feline
RT foamy virus important for virus morphogenesis.";
RL Virology 310:235-244(2003).
RN [4]
RP MUTAGENESIS OF TRP-38.
RX PubMed=16160174; DOI=10.1128/jvi.79.19.12464-12476.2005;
RA Cartellieri M., Herchenroeder O., Rudolph W., Heinkelein M., Lindemann D.,
RA Zentgraf H., Rethwilm A.;
RT "N-terminal Gag domain required for foamy virus particle assembly and
RT export.";
RL J. Virol. 79:12464-12476(2005).
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 light chain cytoplasmic dynein DYNLL1;
CC this interaction is critical for intracellular microtubule-dependent
CC viral genome transport toward the centrosome (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Gag protein]: Virion {ECO:0000250}. Host nucleus
CC {ECO:0000250}. Host cytoplasm {ECO:0000250}. Note=Nuclear at initial
CC phase, cytoplasmic at assembly. Shortly after infection, Gag protein is
CC targeted to centrosomes. It is then actively transported into the
CC nucleus thanks to its nuclear localization signal (By similarity). In
CC the late phases of infection, Gag proteins assemble in the cytoplasm to
CC form the virion's capsids. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [p3]: Virion. Host cytoplasm, host perinuclear
CC region. Note=Gag proteins assemble in the cytoplasm to form the
CC capsids. {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; Y08851; CAA70074.1; -; Genomic_DNA.
DR SMR; O56860; -.
DR Proteomes; UP000008763; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; 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: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; 2.
PE 1: Evidence at protein level;
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 nucleoprotein; Virion; Virus entry into host cell.
FT CHAIN 1..514
FT /note="Gag polyprotein"
FT /id="PRO_0000244977"
FT CHAIN 1..488
FT /note="Gag protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000244978"
FT CHAIN 489..514
FT /note="p3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000244979"
FT REGION 352..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 182..183
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 210..211
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 223..224
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 488..489
FT /note="Cleavage; by viral protease; partial"
FT MUTAGEN 38
FT /note="W->A: Loss of capsid export."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 43
FT /note="R->A: Induces deficiency in replication; Gag is
FT mislocalized to the nucleus."
FT /evidence="ECO:0000269|PubMed:12781711"
SQ SEQUENCE 514 AA; 55534 MW; 66A97BAA9A76519E CRC64;
MARELNPLQL QQLYINNGLQ PNPGHGDIIA VRFTGGPWGP GDRWARVTIR LQDNTGQPLQ
VPGYDLEPGI INLREDILIA GPYNLIRTAF LDLEPARGPE RHGPFGDGRL QPGDGLSEGF
QPITDEEIQA EVGTIGAARN EIRLLREALQ RLQAGGVGRP IPGAVLQPQP VIGPVIPINH
LRSVIGNTPP NPRDVALWLG RSTAAIEGVF PIVDQVTRMR VVNALVASHP GLTLTENEAG
SWNAAISALW RKAHGAAAQH ELAGVLSDIN KKEGIQTAFN LGMQFTDGNW SLVWGIIRTL
LPGQALVTNA QSQFDLMGDD IQRAENFPRV INNLYTMLGL NIHGQSIRPR VQTQPLQTRP
RNPGRSQQGQ LNQPRPQNRA NQSYRPPRQQ QQHSDVPEQR DQRGPSQPPR GSGGGYNFRR
NPQQPQRYGQ GPPGPNPYRR FGDGGNPQQQ GPPPNRGPDQ GPRPGGNPRG GGRGQGPRNG
GGSAAAVHTV KASENETKNG SAEAVDGGKK GGKD
