ID   GAG_RSVP                Reviewed;         701 AA.
AC   P03322; Q77YH0;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   04-NOV-2026, entry version 167.
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     AltName: Full=NCp12 {ECO:0000250|UniProtKB:P0C776};
DE   Contains:
DE     RecName: Full=Protease p15;
DE              EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
GN   Name=gag;
OS   Rous sarcoma virus subgroup C (strain Prague) (RSV-Pr-C).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC   Alpharetrovirus avirousar; Rous sarcoma virus.
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Reipen I.G., Sahm H., Sprenger G.A.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEOLYTIC CLEAVAGE (GAG POLYPROTEIN).
RX   PubMed=7666544; DOI=10.1128/jvi.69.10.6430-6438.1995;
RA   Pepinsky R.B., Papayannopoulos I.A., Chow E.P., Krishna N.K., Craven R.C.,
RA   Vogt V.M.;
RT   "Differential proteolytic processing leads to multiple forms of the CA
RT   protein in avian sarcoma and leukemia viruses.";
RL   J. Virol. 69:6430-6438(1995).
RN   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
RP   FUNCTION (SPACER PEPTIDE), AND SUBCELLULAR LOCATION (GAG POLYPROTEIN).
RX   PubMed=26676779; DOI=10.1128/jvi.02733-15;
RA   Dick R.A., Barros M., Jin D., Loesche M., Vogt V.M.;
RT   "Membrane Binding of the Rous Sarcoma Virus Gag Protein Is Cooperative and
RT   Dependent on the Spacer Peptide Assembly Domain.";
RL   J. Virol. 90:2473-2485(2015).
RN   [11]
RP   FUNCTION (SPACER PEPTIDE), FUNCTION (CAPSID PROTEIN P27), AND SUBUNIT
RP   (CAPSID PROTEIN P27).
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).
RN   [12]
RP   FUNCTION (CAPSID PROTEIN P27).
RX   PubMed=34050170; DOI=10.1038/s41467-021-23506-0;
RA   Obr M., Ricana C.L., Nikulin N., Feathers J.R., Klanschnig M., Thader A.,
RA   Johnson M.C., Vogt V.M., Schur F.K.M., Dick R.A.;
RT   "Structure of the mature Rous sarcoma virus lattice reveals a role for IP6
RT   in the formation of the capsid hexamer.";
RL   Nat. Commun. 12:3226-3226(2021).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY, 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   [14] {ECO:0007744|PDB:2RSP}
RP   X-RAY CRYSTALLOGRAPHY, AND SUBUNIT (PROTEASE 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   [15] {ECO:0007744|PDB:1BAI}
RP   X-RAY CRYSTALLOGRAPHY OF MUTANT SER-615; ILE-619; ILE-621; MET-650;
RP   ALA-677; VAL-681; ARG-682; GLY-683; SER-684 WITH 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   [16]
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   [17] {ECO:0007744|PDB:1EM9, ECO:0007744|PDB:1EOQ}
RP   X-RAY CRYSTALLOGRAPHY, FUNCTION (CAPSID PROTEIN P27), AND SUBUNIT (CAPSID
RP   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   [18] {ECO:0007744|PDB:1P7N}
RP   X-RAY CRYSTALLOGRAPHY, AND SUBUNIT (CAPSID 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   [19] {ECO:0007829|PDB:2IHX}
RP   STRUCTURE BY NMR OF 503-563 IN COMPLEX WITH ZINC, AND FUNCTION
RP   (NUCLEOCAPSID PROTEIN P12).
RX   PubMed=17070546; DOI=10.1016/j.jmb.2006.10.013;
RA   Zhou J., Bean R.L., Vogt V.M., Summers M.;
RT   "Solution structure of the Rous sarcoma virus nucleocapsid protein: muPsi
RT   RNA packaging signal complex.";
RL   J. Mol. Biol. 365:453-467(2007).
RN   [20] {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, SUBUNIT (CAPSID PROTEIN P27), AND DOMAIN (CAPSID
RP   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   [21] {ECO:0007744|PDB:2X8Q}
RP   STRUCTURE BY ELECTRON MICROSCOPY, SUBUNIT (CAPSID PROTEIN P27), AND DOMAIN
RP   (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   [22] {ECO:0007744|PDB:5A9E}
RP   STRUCTURE BY ELECTRON MICROSCOPY, FUNCTION (GAG POLYPROTEIN), AND SUBUNIT
RP   (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).
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, alternate cleaved 1]: Self-associates to
CC       form the irregular polyhedron core composed of hexamers and pentamers,
CC       that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a
CC       tube in vitro (PubMed:10873863, PubMed:28588198). Binds to inositol
CC       hexakisphosphate (IP6), which allows the assembly of the polyhedral
CC       capsid (PubMed:34050170). {ECO:0000269|PubMed:10873863,
CC       ECO:0000269|PubMed:28588198, ECO:0000269|PubMed:34050170}.
CC   -!- FUNCTION: [Capsid protein p27, alternate cleaved 2]: Self-associates to
CC       form the irregular polyhedron core composed of hexamers and pentamers,
CC       that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a
CC       tube in vitro (PubMed:10873863, PubMed:28588198). Binds to inositol
CC       hexakisphosphate (IP6), which allows the assembly of the polyhedral
CC       capsid (PubMed:34050170). {ECO:0000269|PubMed:10873863,
CC       ECO:0000269|PubMed:28588198, ECO:0000269|PubMed:34050170}.
CC   -!- FUNCTION: [Nucleocapsid protein p12]: Binds strongly to viral nucleic
CC       acids and promotes their packaging (PubMed:17070546). Plays a role in
CC       the maturation-stabilization of the viral dimeric RNA via highly
CC       structured zinc-binding motifs (By similarity).
CC       {ECO:0000250|UniProtKB:P0C776, ECO:0000269|PubMed:17070546}.
CC   -!- FUNCTION: [Spacer peptide]: Plays a role in the oligomerization of the
CC       Gag polyprotein and in the stabilization of the immature particle
CC       (PubMed:28588198). Essential layering element during tube assembly that
CC       is progressively removed as capsid assembly proceeds (PubMed:28588198).
CC       Allows the cooperative binging of Gag to the host plasma membrane
CC       (PubMed:26676779). {ECO:0000269|PubMed:26676779,
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). Homohexamer (PubMed:28588198).
CC       {ECO:0000269|PubMed:10873863, ECO:0000269|PubMed:14659756,
CC       ECO:0000269|PubMed:19446529, ECO:0000269|PubMed:20228062,
CC       ECO:0000269|PubMed:28588198}.
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). Homohexamer (PubMed:28588198).
CC       {ECO:0000269|PubMed:10873863, ECO:0000269|PubMed:14659756,
CC       ECO:0000269|PubMed:19446529, ECO:0000269|PubMed:20228062,
CC       ECO:0000269|PubMed:28588198}.
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}. Host cell membrane
CC       {ECO:0000269|PubMed:26676779}. 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:8627817, PubMed:8636100). 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:7666544).
CC       {ECO:0000269|PubMed:7666544, 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; AF033808; AAC82560.1; -; Genomic_RNA.
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   BMRB; P03322; -.
DR   SMR; P03322; -.
DR   ELM; P03322; -.
DR   MEROPS; A02.015; -.
DR   GeneID; 1491923; -.
DR   KEGG; vg:1491923; -.
DR   BRENDA; 3.4.23.B10; 5464.
DR   EvolutionaryTrace; P03322; -.
DR   CDD; cd05482; HIV_retropepsin_like; 1.
DR   FunFam; 1.10.375.10:FF:000003; Gag polyprotein; 1.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 1.10.150.90; Immunodeficiency lentiviruses, gag gene matrix protein p17; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR004028; Gag_M.
DR   InterPro; IPR012344; Matrix_HIV/RSV_N.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR050195; Primate_lentivir_Gag_pol-like.
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   PANTHER; PTHR40389; ENDOGENOUS RETROVIRUS GROUP K MEMBER 24 GAG POLYPROTEIN-RELATED; 1.
DR   PANTHER; PTHR40389:SF3; IGE-BINDING PROTEIN; 1.
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; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
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:0020002; C:host cell plasma membrane; EXP:UniProtKB.
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:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046797; P:viral procapsid maturation; IEA:UniProtKB-KW.
DR   GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW.
DR   Proteomes; UP000137552; Segment.
DR   AlphaFoldDB; P03322; -.
DR   EMDB; EMD-12485; -.
DR   EMDB; EMD-12486; -.
DR   EMDB; EMD-12487; -.
DR   EMDB; EMD-12488; -.
DR   EMDB; EMD-12489; -.
DR   EMDB; EMD-12490; -.
DR   EMDB; EMD-12491; -.
DR   EMDB; EMD-12492; -.
DR   EMDB; EMD-12493; -.
DR   EMDB; EMD-12494; -.
DR   EMDB; EMD-12495; -.
DR   EMDB; EMD-12496; -.
DR   EMDB; EMD-12497; -.
DR   EMDB; EMD-12498; -.
DR   EMDB; EMD-12499; -.
DR   EMDB; EMD-12500; -.
DR   EMDB; EMD-12501; -.
DR   EMDB; EMD-12502; -.
DR   EMDB; EMD-12503; -.
DR   EMDB; EMD-12504; -.
DR   EMDB; EMD-12505; -.
DR   EMDB; EMD-12506; -.
DR   EMDB; EMD-12507; -.
DR   EMDB; EMD-12508; -.
DR   EMDB; EMD-12509; -.
DR   EMDB; EMD-12510; -.
DR   EMDB; EMD-12511; -.
DR   EMDB; EMD-12774; -.
DR   EMDB; EMD-1710; -.
DR   EMDB; EMD-3101; -.
DR   EMDB; EMD-3102; -.
DR   MDposit; P03322; -.
DR   MDRepo; P03322; -.
PE   1: Evidence at protein level;
KW   3D-structure; Aspartyl protease; Capsid protein; Direct protein sequencing;
KW   Host cell membrane; Host membrane; Host nucleus; Hydrolase; Membrane;
KW   Metal-binding; Protease; Reference proteome; 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   COMPBIAS        128..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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..6
FT                   /evidence="ECO:0007829|PDB:1A6S"
FT   HELIX           7..15
FT                   /evidence="ECO:0007829|PDB:1A6S"
FT   HELIX           28..32
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..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          510..512
FT                   /evidence="ECO:0007829|PDB:2IHX"
FT   HELIX           519..521
FT                   /evidence="ECO:0007829|PDB:2IHX"
FT   STRAND          527..529
FT                   /evidence="ECO:0007829|PDB:2IHX"
FT   TURN            536..538
FT                   /evidence="ECO:0007829|PDB:2IHX"
FT   STRAND          541..543
FT                   /evidence="ECO:0007829|PDB:2IHX"
FT   HELIX           545..547
FT                   /evidence="ECO:0007829|PDB:2IHX"
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
//