GAG_FOAMV
ID GAG_FOAMV Reviewed; 648 AA.
AC P14349; P89871;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 02-JUN-2021, entry version 109.
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 Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=11963;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2451755; DOI=10.1128/jvi.62.5.1590-1597.1988;
RA Maurer B., Bannert H., Darai G., Fluegel R.M.;
RT "Analysis of the primary structure of the long terminal repeat and the gag
RT and pol genes of the human spumaretrovirus.";
RL J. Virol. 62:1590-1597(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND SEQUENCE REVISION.
RA Fluegel R.M.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEAR LOCALIZATION SIGNAL, AND NUCLEIC ACID-BINDING.
RX PubMed=8970944; DOI=10.1128/jvi.70.12.8255-8262.1996;
RA Yu S.F., Edelmann K., Strong R.K., Moebes A., Rethwilm A., Linial M.L.;
RT "The carboxyl terminus of the human foamy virus Gag protein contains
RT separable nucleic acid binding and nuclear transport domains.";
RL J. Virol. 70:8255-8262(1996).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=8995637; DOI=10.1128/jvi.71.2.1155-1161.1997;
RA Saib A., Puvion-Dutilleul F., Schmid M., Peries J., de The H.;
RT "Nuclear targeting of incoming human foamy virus Gag proteins involves a
RT centriolar step.";
RL J. Virol. 71:1155-1161(1997).
RN [5]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=10438890; DOI=10.1128/jvi.73.9.7907-7911.1999;
RA Pfrepper K.-I., Loechelt M., Rackwitz H.R., Schnoelzer M., Heid H.,
RA Fluegel R.M.;
RT "Molecular characterization of proteolytic processing of the Gag proteins
RT of human spumavirus.";
RL J. Virol. 73:7907-7911(1999).
RN [6]
RP CHARACTERIZATION OF GAG PROTEIN.
RX PubMed=15308736; DOI=10.1128/jvi.78.17.9423-9430.2004;
RA Stenbak C.R., Linial M.L.;
RT "Role of the C terminus of foamy virus Gag in RNA packaging and Pol
RT expression.";
RL J. Virol. 78:9423-9430(2004).
RN [7]
RP LATE-BUDDING MOTIFS, AND INTERACTION WITH HUMAN TSG101.
RX PubMed=15858022; DOI=10.1128/jvi.79.10.6392-6399.2005;
RA Patton G.S., Morris S.A., Chung W., Bieniasz P.D., McClure M.O.;
RT "Identification of domains in gag important for prototypic foamy virus
RT egress.";
RL J. Virol. 79:6392-6399(2005).
RN [8]
RP FUNCTION OF N-TERMINUS, AND MUTAGENESIS OF LEU-17; TRP-44; TRP-45; ARG-50;
RP LEU-56; LEU-58 AND PRO-65.
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).
RN [9]
RP FUNCTION, INTERACTION OF GAG PROTEIN WITH HOST DYNLL1, AND MUTAGENESIS OF
RP LEU-171.
RX PubMed=12857789; DOI=10.1242/jcs.00613;
RA Petit C., Giron M.L., Tobaly-Tapiero J., Bittoun P., Real E., Jacob Y.,
RA Tordo N., De The H., Saib A.;
RT "Targeting of incoming retroviral Gag to the centrosome involves a direct
RT interaction with the dynein light chain 8.";
RL J. Cell Sci. 116:3433-3442(2003).
RN [10]
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 [11]
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. {ECO:0000269|PubMed:12857789,
CC ECO:0000269|PubMed:16160174}.
CC -!- SUBUNIT: Gag protein specifically interacts with the N-terminus of
CC leader peptide (By similarity). This specific interaction between Gag
CC protein and Env glycoprotein may compensate for the lack of a Gag
CC membrane targeting signal, and allow particle egress. The capsid is
CC composed of multimeric Gag protein. Interacts with human TSG101.
CC Interacts with host light chain cytoplasmic dynein DYNLL1; this
CC interaction is critical for intracellular microtubule-dependent viral
CC genome transport toward the centrosome. {ECO:0000250,
CC ECO:0000269|PubMed:12857789, ECO:0000269|PubMed:15858022}.
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.
CC -!- SUBCELLULAR LOCATION: [p3]: Virion.
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.
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.
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. {ECO:0000269|PubMed:10438890}.
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; M19427; AAA66555.1; ALT_TERM; Genomic_RNA.
DR EMBL; U21247; AAB48111.1; -; Genomic_RNA.
DR PDB; 4JMR; X-ray; 2.90 A; A/B/C/D=1-179.
DR PDB; 4JNH; X-ray; 2.40 A; A/B=1-179.
DR PDB; 5M1G; NMR; -; A/B=381-477.
DR PDB; 5M1H; NMR; -; A=300-477.
DR PDB; 5MLU; X-ray; 2.80 A; M=535-551.
DR PDBsum; 4JMR; -.
DR PDBsum; 4JNH; -.
DR PDBsum; 5M1G; -.
DR PDBsum; 5M1H; -.
DR PDBsum; 5MLU; -.
DR SMR; P14349; -.
DR ELM; P14349; -.
DR MEROPS; A09.001; -.
DR BRENDA; 3.4.23.B11; 2705.
DR Proteomes; UP000138352; 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; IMP:CACAO.
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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Cytoplasmic inwards viral transport;
KW DNA-binding; 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..648
FT /note="Gag polyprotein"
FT /id="PRO_0000125475"
FT CHAIN 1..621
FT /note="Gag protein"
FT /id="PRO_0000245437"
FT CHAIN 622..648
FT /note="p3"
FT /id="PRO_0000245438"
FT REGION 37..60
FT /note="Involved in viral assembly and export"
FT /evidence="ECO:0000255"
FT REGION 175..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..510
FT /note="Nucleic acid-binding; GR-box 1"
FT REGION 535..556
FT /note="GR-box 2"
FT REGION 586..618
FT /note="GR-box 3"
FT MOTIF 284..287
FT /note="PTAP/PSAP motif"
FT MOTIF 535..556
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:8970944"
FT COMPBIAS 210..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 311..312
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 339..340
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 352..353
FT /note="Cleavage; by viral protease; low efficiency"
FT /evidence="ECO:0000255"
FT SITE 621..622
FT /note="Cleavage; by viral protease; partial"
FT MUTAGEN 17
FT /note="L->A: No effect on capsid export. Reduced virus
FT titer."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 17
FT /note="L->S: Complete loss of capsid egress from
FT transfected cells."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 44
FT /note="W->A: 75% loss of particle export. Reduced virus
FT titer."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 45
FT /note="W->A: Complete loss of capsid egress from
FT transfected cells."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 50
FT /note="R->A: Complete loss of capsid egress from
FT transfected cells."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 56
FT /note="L->A: Complete loss of capsid egress from
FT transfected cells."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 58
FT /note="L->A: Complete loss of capsid egress from
FT transfected cells."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 65
FT /note="P->A: 75% loss of particle export."
FT /evidence="ECO:0000269|PubMed:16160174"
FT MUTAGEN 171
FT /note="L->G: Drastically reduces infectivity."
FT /evidence="ECO:0000269|PubMed:12857789"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4JNH"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:4JNH"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4JNH"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4JNH"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:4JNH"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:4JNH"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:4JMR"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4JNH"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:4JNH"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4JNH"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:4JNH"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:4JNH"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4JNH"
FT HELIX 140..177
FT /evidence="ECO:0007829|PDB:4JNH"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:5M1H"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:5M1H"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:5M1H"
FT HELIX 344..355
FT /evidence="ECO:0007829|PDB:5M1H"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:5M1H"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:5M1H"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:5M1G"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:5M1H"
FT HELIX 393..401
FT /evidence="ECO:0007829|PDB:5M1G"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:5M1G"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:5M1G"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:5M1G"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5M1G"
FT HELIX 433..445
FT /evidence="ECO:0007829|PDB:5M1G"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:5M1H"
FT HELIX 450..454
FT /evidence="ECO:0007829|PDB:5M1G"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:5M1G"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:5M1H"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:5M1G"
SQ SEQUENCE 648 AA; 70591 MW; C7ECBC8B96E77109 CRC64;
MASGSNVEEY ELDVEALVVI LRDRNIPRNP LHGEVIGLRL TEGWWGQIER FQMVRLILQD
DDNEPLQRPR YEVIQRAVNP HTMFMISGPL AELQLAFQDL DLPEGPLRFG PLANGHYVQG
DPYSSSYRPV TMAETAQMTR DELEDVLNTQ SEIEIQMINL LELYEVETRA LRRQLAERSS
TGQGGISPGA PRSRPPVSSF SGLPSLPSIP GIHPRAPSPP RATSTPGNIP WSLGDDSPPS
SSFPGPSQPR VSFHPGNPFV EEEGHRPRSQ SRERRREILP APVPSAPPMI QYIPVPPPPP
IGTVIPIQHI RSVTGEPPRN PREIPIWLGR NAPAIDGVFP VTTPDLRCRI INAILGGNIG
LSLTPGDCLT WDSAVATLFI RTHGTFPMHQ LGNVIKGIVD QEGVATAYTL GMMLSGQNYQ
LVSGIIRGYL PGQAVVTALQ QRLDQEIDNQ TRAETFIQHL NAVYEILGLN ARGQSIRASV
TPQPRPSRGR GRGQNTSRPS QGPANSGRGR QRPASGQSNR GSSTQNQNQD NLNQGGYNLR
PRTYQPQRYG GGRGRRWNDN TNNQESRPSD QGSQTPRPNQ AGSGVRGNQS QTPRPAAGRG
GRGNHNRNQR SSGAGDSRAV NTVTQSATSS TDESSSAVTA ASGGDQRD
