GAG_RSVP
ID GAG_RSVP Reviewed; 701 AA.
AC P03322;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Gag polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p19;
DE Contains:
DE RecName: Full=p2A;
DE Contains:
DE RecName: Full=p2B;
DE Contains:
DE RecName: Full=p10;
DE Contains:
DE RecName: Full=Capsid protein p27, alternate cleaved 1;
DE Contains:
DE RecName: Full=Capsid protein p27, alternate cleaved 2;
DE Contains:
DE RecName: Full=Spacer peptide;
DE Short=SP;
DE AltName: Full=p3;
DE Contains:
DE RecName: Full=Nucleocapsid protein p12;
DE Contains:
DE RecName: Full=Protease p15;
DE EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
GN Name=gag;
OS Rous sarcoma virus (strain Prague C) (RSV-PrC).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX NCBI_TaxID=11888;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6299578; DOI=10.1016/0092-8674(83)90071-5;
RA Schwartz D., Tizard R., Gilbert W.;
RT "Nucleotide sequence of Rous sarcoma virus.";
RL Cell 32:853-869(1983).
RN [2]
RP PROTEIN SEQUENCE OF 489-577.
RA Misono K.S., Sharief F.S., Leis J.;
RT "Primary structure of Rous sarcoma virus RNA-associated polypeptide.";
RL Fed. Proc. 39:1611-1611(1980).
RN [3]
RP PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
RX PubMed=8636100; DOI=10.1074/jbc.271.12.6781;
RA Tozser J., Bagossi P., Weber I.T., Copeland T.D., Oroszlan S.;
RT "Comparative studies on the substrate specificity of avian myeloblastosis
RT virus proteinase and lentiviral proteinases.";
RL J. Biol. Chem. 271:6781-6788(1996).
RN [4]
RP PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
RX PubMed=8627817; DOI=10.1128/jvi.70.5.3313-3318.1996;
RA Pepinsky R.B., Papayannopoulos I.A., Campbell S., Vogt V.M.;
RT "Analysis of Rous sarcoma virus Gag protein by mass spectrometry indicates
RT trimming by host exopeptidase.";
RL J. Virol. 70:3313-3318(1996).
RN [5]
RP RIBOSOMAL FRAMESHIFTING (GAG POLYPROTEIN).
RX PubMed=9813113; DOI=10.1006/jmbi.1998.2186;
RA Marczinke B., Fisher R., Vidakovic M., Bloys A.J., Brierley I.;
RT "Secondary structure and mutational analysis of the ribosomal frameshift
RT signal of rous sarcoma virus.";
RL J. Mol. Biol. 284:205-225(1998).
RN [6]
RP DOMAIN (GAG POLYPROTEIN), AND MUTAGENESIS OF PRO-172 AND 180-LEU--LEU-184.
RX PubMed=20392845; DOI=10.1128/jvi.00238-10;
RA Dilley K.A., Gregory D., Johnson M.C., Vogt V.M.;
RT "An LYPSL late domain in the gag protein contributes to the efficient
RT release and replication of Rous sarcoma virus.";
RL J. Virol. 84:6276-6287(2010).
RN [7]
RP SUBCELLULAR LOCATION (GAG POLYPROTEIN), DOMAIN (GAG POLYPROTEIN), AND
RP MUTAGENESIS OF LEU-219; 524-LYS--LYS-527 AND 549-ARG--ARG-551.
RX PubMed=23036987; DOI=10.1016/j.virusres.2012.09.011;
RA Lochmann T.L., Bann D.V., Ryan E.P., Beyer A.R., Mao A., Cochrane A.,
RA Parent L.J.;
RT "NC-mediated nucleolar localization of retroviral gag proteins.";
RL Virus Res. 171:304-318(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 578-701, AND SUBUNIT (PROTEASE).
RX PubMed=2536902; DOI=10.1038/337576a0;
RA Miller M., Jaskolski M., Rao J.K.M., Leis J., Wlodawer A.;
RT "Crystal structure of a retroviral protease proves relationship to aspartic
RT protease family.";
RL Nature 337:576-579(1989).
RN [9] {ECO:0007744|PDB:2RSP}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 578-701, AND SUBUNIT (PROTEASE
RP P15).
RX PubMed=2166563; DOI=10.1021/bi00477a002;
RA Jaskolski M., Miller M., Rao J.K., Leis J., Wlodawer A.;
RT "Structure of the aspartic protease from Rous sarcoma retrovirus refined at
RT 2-A resolution.";
RL Biochemistry 29:5889-5898(1990).
RN [10] {ECO:0007744|PDB:1BAI}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 578-701 OF MUTANT SER-615;
RP ILE-619; ILE-621; MET-650; ALA-677; VAL-681; ARG-682; GLY-683; SER-684 WITH
RP INHIBITOR.
RC STRAIN=S9 variant;
RX PubMed=9521772; DOI=10.1021/bi972183g;
RA Wu J., Adomat J.M., Ridky T.W., Louis J.M., Leis J., Harrison R.W.,
RA Weber I.T.;
RT "Structural basis for specificity of retroviral proteases.";
RL Biochemistry 37:4518-4526(1998).
RN [11]
RP STRUCTURE BY NMR OF 1-87.
RX PubMed=9642071; DOI=10.1006/jmbi.1998.1788;
RA McDonnell J.M., Fushman D., Cahill S.M., Zhou W., Wolven A., Wilson C.B.,
RA Nelle T.D., Resh M.D., Wills J., Cowburn D.;
RT "Solution structure and dynamics of the bioactive retroviral M domain from
RT Rous sarcoma virus.";
RL J. Mol. Biol. 279:921-928(1998).
RN [12] {ECO:0007744|PDB:1EM9, ECO:0007744|PDB:1EOQ}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 240-393, FUNCTION (CAPSID PROTEIN
RP P27), AND SUBUNIT (CAPSID PROTEIN P27).
RX PubMed=10873863; DOI=10.1016/s0969-2126(00)00148-9;
RA Kingston R.L., Fitzon-Ostendorp T., Eisenmesser E.Z., Schatz G.W.,
RA Vogt V.M., Post C.B., Rossmann M.G.;
RT "Structure and self-association of the Rous sarcoma virus capsid protein.";
RL Structure 8:617-628(2000).
RN [13] {ECO:0007744|PDB:1P7N}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 215-386, AND SUBUNIT (CAPSID
RP PROTEIN P27).
RX PubMed=14659756; DOI=10.1016/j.jmb.2003.10.034;
RA Nandhagopal N., Simpson A.A., Johnson M.C., Francisco A.B., Schatz G.W.,
RA Rossmann M.G., Vogt V.M.;
RT "Dimeric rous sarcoma virus capsid protein structure relevant to immature
RT Gag assembly.";
RL J. Mol. Biol. 335:275-282(2004).
RN [14] {ECO:0007744|PDB:3G0V, ECO:0007744|PDB:3G1G, ECO:0007744|PDB:3G1I, ECO:0007744|PDB:3G21, ECO:0007744|PDB:3G26, ECO:0007744|PDB:3G28, ECO:0007744|PDB:3G29}
RP X-RAY CRYSTALLOGRAPHY (0.90 ANGSTROMS) OF 389-465, SUBUNIT (CAPSID PROTEIN
RP P27), AND DOMAIN (CAPSID PROTEIN P27).
RX PubMed=19446529; DOI=10.1016/j.str.2009.03.010;
RA Bailey G.D., Hyun J.K., Mitra A.K., Kingston R.L.;
RT "Proton-linked dimerization of a retroviral capsid protein initiates capsid
RT assembly.";
RL Structure 17:737-748(2009).
RN [15] {ECO:0007744|PDB:2X8Q}
RP STRUCTURE BY ELECTRON MICROSCOPY (18.30 ANGSTROMS) OF 240-465, SUBUNIT
RP (CAPSID PROTEIN P27), AND DOMAIN (CAPSID PROTEIN P27).
RX PubMed=20228062; DOI=10.1074/jbc.m110.108209;
RA Hyun J.K., Radjainia M., Kingston R.L., Mitra A.K.;
RT "Proton-driven assembly of the Rous sarcoma virus capsid protein results in
RT the formation of icosahedral particles.";
RL J. Biol. Chem. 285:15056-15064(2010).
RN [16] {ECO:0007744|PDB:5A9E}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.70 ANGSTROMS) OF 84-577, FUNCTION (GAG
RP POLYPROTEIN), AND SUBUNIT (GAG POLYPROTEIN).
RX PubMed=26223638; DOI=10.1128/jvi.01502-15;
RA Schur F.K., Dick R.A., Hagen W.J., Vogt V.M., Briggs J.A.;
RT "The structure of immature virus-like Rous sarcoma virus gag particles
RT reveals a structural role for the p10 domain in assembly.";
RL J. Virol. 89:10294-10302(2015).
RN [17]
RP FUNCTION (SPACER PEPTIDE), FUNCTION (CAPSID PROTEIN P27), AND PROTEOLYTIC
RP CLEAVAGE (GAG POLYPROTEIN).
RX PubMed=28588198; DOI=10.1038/s41598-017-02060-0;
RA Jaballah S.A., Bailey G.D., Desfosses A., Hyun J., Mitra A.K.,
RA Kingston R.L.;
RT "In vitro assembly of the Rous sarcoma virus capsid protein into hexamer
RT tubes at physiological temperature.";
RL Sci. Rep. 7:2913-2913(2017).
CC -!- FUNCTION: [Gag polyprotein]: The p10 domain folds back and interacts
CC with the capsid protein domain during Gag polyprotein assembly in the
CC immature particle (before the maturation cleavage that splits the 2
CC domains). {ECO:0000269|PubMed:26223638}.
CC -!- FUNCTION: Capsid protein p27: Self-associates to form the irregular
CC polyhedron core composed of hexamers and pentamers, that encapsulates
CC the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro.
CC {ECO:0000269|PubMed:10873863, ECO:0000269|PubMed:28588198}.
CC -!- FUNCTION: [Nucleocapsid protein p12]: Binds strongly to viral nucleic
CC acids and promote their aggregation. Also destabilizes the nucleic
CC acids duplexes via highly structured zinc-binding motifs.
CC {ECO:0000305}.
CC -!- FUNCTION: [Spacer peptide]: Plays a role in the oligomerization of the
CC Gag polyprotein and in the stabilization of the immature particle.
CC Essential layering element during tube assembly.
CC {ECO:0000269|PubMed:28588198}.
CC -!- FUNCTION: [Protease p15]: Aspartyl protease that mediates proteolytic
CC cleavages of Gag and Gag-Pol polyproteins during or shortly after the
CC release of the virion from the plasma membrane. Cleavages take place as
CC an ordered, step-wise cascade to yield mature proteins. This process is
CC called maturation. Displays maximal activity during the budding process
CC just prior to particle release from the cell. {ECO:0000255|PROSITE-
CC ProRule:PRU00275}.
CC -!- SUBUNIT: [Protease p15]: Active as a homodimer (PubMed:2166563,
CC PubMed:2536902). {ECO:0000269|PubMed:2166563,
CC ECO:0000269|PubMed:2536902}.
CC -!- SUBUNIT: [Capsid protein p27, alternate cleaved 1]: Homodimer
CC (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062).
CC Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529,
CC PubMed:20228062). {ECO:0000269|PubMed:10873863,
CC ECO:0000269|PubMed:14659756, ECO:0000269|PubMed:19446529,
CC ECO:0000269|PubMed:20228062}.
CC -!- SUBUNIT: [Capsid protein p27, alternate cleaved 2]: Homodimer
CC (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062).
CC Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529,
CC PubMed:20228062). {ECO:0000269|PubMed:10873863,
CC ECO:0000269|PubMed:14659756, ECO:0000269|PubMed:19446529,
CC ECO:0000269|PubMed:20228062}.
CC -!- SUBUNIT: [Gag polyprotein]: Homohexamer (PubMed:26223638). Interacts
CC (via p2B domain) with host PACSIN2; this interaction probably allows
CC PACSIN2 recruitment to viral assembly sites (By similarity).
CC {ECO:0000250|UniProtKB:P0C776, ECO:0000269|PubMed:26223638}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Host nucleus, host nucleolus
CC {ECO:0000269|PubMed:23036987}. Host nucleus, host nucleoplasm
CC {ECO:0000269|PubMed:23036987}. Note=Shuttles between nucleoplasm and
CC nucleolus. {ECO:0000269|PubMed:23036987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Translation results in the formation of the Gag polyprotein.
CC Ribosomal frameshifting at the gag/pol genes boundary produces the
CC Gag-Pol polyprotein. {ECO:0000269|PubMed:9813113};
CC Name=Gag polyprotein;
CC IsoId=P03322-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P03354-1; Sequence=External;
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle release. They can occur
CC individually or in close proximity within structural proteins. They
CC interacts with sorting cellular proteins of the multivesicular body
CC (MVB) pathway. Most of these proteins are class E vacuolar protein
CC sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes.
CC P2B contains two L domains: a PPXY motif which probably binds to the WW
CC domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases
CC and a LYPX(n)L domain which is known to bind the Alix adaptator
CC protein. {ECO:0000269|PubMed:20392845}.
CC -!- DOMAIN: [Gag polyprotein]: Contains a nuclear export signal in p10 and
CC a nucleolar localization signal in nucleocapsid protein p12.
CC {ECO:0000269|PubMed:23036987}.
CC -!- DOMAIN: Capsid protein p27: Proton-driven dimerization of the C-
CC terminus facilitates capsid assembly. {ECO:0000269|PubMed:19446529,
CC ECO:0000269|PubMed:20228062}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield
CC mature proteins (PubMed:8636100, PubMed:8627817). The cleavage at the
CC C-terminus of the Capsid protein p27 is slowly trimmed by the viral
CC protease, sometimes being cut internally thereby generating the short
CC version of the capsid protein and a capsid protein C-terminally
CC extended by 3 amino acids in a ratio of 2:1 (PubMed:28588198).
CC {ECO:0000269|PubMed:28588198, ECO:0000269|PubMed:8627817,
CC ECO:0000269|PubMed:8636100}.
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation. {ECO:0000269|PubMed:9813113}.
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DR EMBL; J02342; AAB59932.1; -; Genomic_RNA.
DR EMBL; V01197; CAA24512.1; -; Genomic_DNA.
DR PIR; A90834; FOFV1R.
DR RefSeq; NP_056887.1; NC_001407.1.
DR PDB; 1A6S; NMR; -; A=2-87.
DR PDB; 1BAI; X-ray; 2.40 A; A/B=578-701.
DR PDB; 1EM9; X-ray; 2.05 A; A/B=240-393.
DR PDB; 1EOQ; NMR; -; A=394-488.
DR PDB; 1P7N; X-ray; 2.60 A; A=215-386.
DR PDB; 2IHX; NMR; -; A=503-563.
DR PDB; 2RSP; X-ray; 2.00 A; A/B=578-701.
DR PDB; 2X8Q; EM; 18.30 A; A=240-465.
DR PDB; 3G0V; X-ray; 2.00 A; A=389-465.
DR PDB; 3G1G; X-ray; 2.01 A; A/B=390-476.
DR PDB; 3G1I; X-ray; 2.10 A; A/B=389-465.
DR PDB; 3G21; X-ray; 0.90 A; A=389-465.
DR PDB; 3G26; X-ray; 1.55 A; A=389-465.
DR PDB; 3G28; X-ray; 1.64 A; A=389-465.
DR PDB; 3G29; X-ray; 2.50 A; A/B=389-465.
DR PDB; 5A9E; EM; 7.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=84-577.
DR PDB; 7NO0; EM; 3.10 A; A=240-468.
DR PDB; 7NO1; EM; 7.60 A; A/B/C=240-468.
DR PDB; 7NO2; EM; 4.30 A; A/B/C=240-468.
DR PDB; 7NO3; EM; 5.80 A; A/B/C/D/E=240-468.
DR PDB; 7NO4; EM; 7.50 A; A/B/C/D/E/F=240-468.
DR PDB; 7NO5; EM; 7.40 A; A/B/C/D/E/F=240-468.
DR PDB; 7NO6; EM; 6.00 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NO7; EM; 7.50 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NO8; EM; 7.90 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NO9; EM; 7.60 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOA; EM; 6.40 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOB; EM; 6.70 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOC; EM; 7.80 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOD; EM; 7.80 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOE; EM; 7.50 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOF; EM; 7.60 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOG; EM; 7.80 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOH; EM; 7.10 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOI; EM; 7.20 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOJ; EM; 6.70 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOK; EM; 9.10 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOL; EM; 8.20 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOM; EM; 6.70 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NON; EM; 6.80 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOO; EM; 7.90 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOP; EM; 7.80 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDB; 7NOQ; EM; 6.50 A; A/B/C/D/E/F/G/H/I/J=240-468.
DR PDBsum; 1A6S; -.
DR PDBsum; 1BAI; -.
DR PDBsum; 1EM9; -.
DR PDBsum; 1EOQ; -.
DR PDBsum; 1P7N; -.
DR PDBsum; 2IHX; -.
DR PDBsum; 2RSP; -.
DR PDBsum; 2X8Q; -.
DR PDBsum; 3G0V; -.
DR PDBsum; 3G1G; -.
DR PDBsum; 3G1I; -.
DR PDBsum; 3G21; -.
DR PDBsum; 3G26; -.
DR PDBsum; 3G28; -.
DR PDBsum; 3G29; -.
DR PDBsum; 5A9E; -.
DR PDBsum; 7NO0; -.
DR PDBsum; 7NO1; -.
DR PDBsum; 7NO2; -.
DR PDBsum; 7NO3; -.
DR PDBsum; 7NO4; -.
DR PDBsum; 7NO5; -.
DR PDBsum; 7NO6; -.
DR PDBsum; 7NO7; -.
DR PDBsum; 7NO8; -.
DR PDBsum; 7NO9; -.
DR PDBsum; 7NOA; -.
DR PDBsum; 7NOB; -.
DR PDBsum; 7NOC; -.
DR PDBsum; 7NOD; -.
DR PDBsum; 7NOE; -.
DR PDBsum; 7NOF; -.
DR PDBsum; 7NOG; -.
DR PDBsum; 7NOH; -.
DR PDBsum; 7NOI; -.
DR PDBsum; 7NOJ; -.
DR PDBsum; 7NOK; -.
DR PDBsum; 7NOL; -.
DR PDBsum; 7NOM; -.
DR PDBsum; 7NON; -.
DR PDBsum; 7NOO; -.
DR PDBsum; 7NOP; -.
DR PDBsum; 7NOQ; -.
DR BMRB; P03322; -.
DR SMR; P03322; -.
DR ELM; P03322; -.
DR MINT; P03322; -.
DR MEROPS; A02.015; -.
DR GeneID; 1491923; -.
DR KEGG; vg:1491923; -.
DR BRENDA; 3.4.23.B10; 5464.
DR EvolutionaryTrace; P03322; -.
DR Proteomes; UP000007183; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0044095; C:host cell nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR004028; Gag_M.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR012344; Matrix_HIV/RSV_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR008916; Retrov_capsid_C.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF02813; Retro_M; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Capsid protein; Direct protein sequencing;
KW Host nucleus; Hydrolase; Metal-binding; Protease; Repeat;
KW Ribosomal frameshifting; Viral capsid assembly; Viral capsid maturation;
KW Viral matrix protein; Viral release from host cell; Virion; Zinc;
KW Zinc-finger.
FT CHAIN 1..701
FT /note="Gag polyprotein"
FT /id="PRO_0000442114"
FT CHAIN 1..155
FT /note="Matrix protein p19"
FT /id="PRO_0000026113"
FT CHAIN 156..166
FT /note="p2A"
FT /id="PRO_0000026114"
FT CHAIN 167..177
FT /note="p2B"
FT /id="PRO_0000026115"
FT CHAIN 178..239
FT /note="p10"
FT /id="PRO_0000026116"
FT CHAIN 240..479
FT /note="Capsid protein p27, alternate cleaved 2"
FT /id="PRO_0000026117"
FT CHAIN 240..476
FT /note="Capsid protein p27, alternate cleaved 1"
FT /id="PRO_0000442115"
FT PEPTIDE 477..488
FT /note="Spacer peptide"
FT /id="PRO_0000026118"
FT CHAIN 489..577
FT /note="Nucleocapsid protein p12"
FT /id="PRO_0000026119"
FT CHAIN 578..701
FT /note="Protease p15"
FT /id="PRO_0000026120"
FT DOMAIN 609..690
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT ZN_FING 507..524
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 533..550
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 128..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..259
FT /note="Involved in capsid protein dimerization"
FT /evidence="ECO:0000269|PubMed:14659756"
FT REGION 290..298
FT /note="Involved in capsid protein dimerization"
FT /evidence="ECO:0000269|PubMed:14659756"
FT REGION 351..362
FT /note="Involved in capsid protein dimerization"
FT /evidence="ECO:0000269|PubMed:14659756"
FT REGION 543..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..175
FT /note="PPXY motif"
FT /evidence="ECO:0000269|PubMed:20392845"
FT MOTIF 180..184
FT /note="LYPX(n)L motif"
FT /evidence="ECO:0000269|PubMed:20392845"
FT MOTIF 219..229
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:23036987"
FT MOTIF 524..527
FT /note="Nuclear/nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:23036987"
FT ACT_SITE 614
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT SITE 155..156
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000269|PubMed:8627817,
FT ECO:0000269|PubMed:8636100"
FT SITE 166..167
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000269|PubMed:8627817,
FT ECO:0000269|PubMed:8636100"
FT SITE 177..178
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000269|PubMed:8627817,
FT ECO:0000269|PubMed:8636100"
FT SITE 239..240
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000269|PubMed:8627817,
FT ECO:0000269|PubMed:8636100"
FT SITE 418
FT /note="Involved in capsid protein dimerization upon
FT acidification"
FT /evidence="ECO:0000269|PubMed:19446529"
FT SITE 430
FT /note="Involved in capsid protein dimerization upon
FT acidification"
FT /evidence="ECO:0000269|PubMed:19446529"
FT SITE 476..477
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000269|PubMed:28588198,
FT ECO:0000269|PubMed:8627817, ECO:0000269|PubMed:8636100"
FT SITE 479..480
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000269|PubMed:28588198,
FT ECO:0000269|PubMed:8627817"
FT SITE 488..489
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000269|PubMed:8627817,
FT ECO:0000269|PubMed:8636100"
FT SITE 577..578
FT /note="Cleavage; by viral protease p15"
FT /evidence="ECO:0000269|PubMed:8627817,
FT ECO:0000269|PubMed:8636100"
FT MUTAGEN 172
FT /note="P->A: 75% loss of budding."
FT /evidence="ECO:0000269|PubMed:20392845"
FT MUTAGEN 180..184
FT /note="LYPSL->AAASA: 40% loss of budding."
FT /evidence="ECO:0000269|PubMed:20392845"
FT MUTAGEN 219
FT /note="L->A: Reduced nucleolar localization of Gag
FT polyprotein."
FT /evidence="ECO:0000269|PubMed:23036987"
FT MUTAGEN 524..527
FT /note="KKRK->AAAA: Complete loss of nuclear and nucleolar
FT localization."
FT /evidence="ECO:0000269|PubMed:23036987"
FT MUTAGEN 549..551
FT /note="RKR->AAA: Reduced localization in nucleolus; no
FT effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:23036987"
FT CONFLICT 505
FT /note="A -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 2..16
FT /evidence="ECO:0007829|PDB:1A6S"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:1A6S"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1A6S"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1A6S"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:1A6S"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:1A6S"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:1A6S"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1A6S"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1A6S"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:1A6S"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:1P7N"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1P7N"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1EM9"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:1EM9"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:1EM9"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:1EM9"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:1EM9"
FT HELIX 302..325
FT /evidence="ECO:0007829|PDB:1EM9"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:1P7N"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:1EM9"
FT TURN 350..354
FT /evidence="ECO:0007829|PDB:1EM9"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:1EM9"
FT HELIX 365..385
FT /evidence="ECO:0007829|PDB:1EM9"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3G21"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:3G21"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3G21"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:3G21"
FT HELIX 424..435
FT /evidence="ECO:0007829|PDB:3G21"
FT HELIX 438..444
FT /evidence="ECO:0007829|PDB:3G21"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:3G21"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 589..596
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 605..613
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:2RSP"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 650..655
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 677..680
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 682..686
FT /evidence="ECO:0007829|PDB:2RSP"
FT HELIX 688..693
FT /evidence="ECO:0007829|PDB:2RSP"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:2RSP"
SQ SEQUENCE 701 AA; 74527 MW; 5FD365D9CFEF37F1 CRC64;
MEAVIKVISS ACKTYCGKTS PSKKEIGAML SLLQKEGLLM SPSDLYSPGS WDPITAALSQ
RAMILGKSGE LKTWGLVLGA LKAAREEQVT SEQAKFWLGL GGGRVSPPGP ECIEKPATER
RIDKGEEVGE TTVQRDAKMA PEETATPKTV GTSCYHCGTA IGCNCATASA PPPPYVGSGL
YPSLAGVGEQ QGQGGDTPPG AEQSRAEPGH AGQAPGPALT DWARVREELA STGPPVVAMP
VVIKTEGPAW TPLEPKLITR LADTVRTKGL RSPITMAEVE ALMSSPLLPH DVTNLMRVIL
GPAPYALWMD AWGVQLQTVI AAATRDPRHP ANGQGRGERT NLNRLKGLAD GMVGNPQGQA
ALLRPGELVA ITASALQAFR EVARLAEPAG PWADIMQGPS ESFVDFANRL IKAVEGSDLP
PSARAPVIID CFRQKSQPDI QQLIRTAPST LTTPGEIIKY VLDRQKTAPL TDQGIAAAMS
SAIQPLIMAV VNRERDGQTG SGGRARGLCY TCGSPGHYQA QCPKKRKSGN SRERCQLCNG
MGHNAKQCRK RDGNQGQRPG KGLSSGPWPG PEPPAVSLAM TMEHKDRPLV RVILTNTGSH
PVKQRSVYIT ALLDSGADIT IISEEDWPTD WPVMEAANPQ IHGIGGGIPM RKSRDMIELG
VINRDGSLER PLLLFPAVAM VRGSILGRDC LQGLGLRLTN L
