GAG_HV1H2
ID GAG_HV1H2 Reviewed; 500 AA.
AC P04591;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Pr55Gag;
DE Contains:
DE RecName: Full=Matrix protein p17;
DE Short=MA;
DE Contains:
DE RecName: Full=Capsid protein p24;
DE Short=CA;
DE Contains:
DE RecName: Full=Spacer peptide 1 {ECO:0000250|UniProtKB:P12493};
DE Short=SP1;
DE AltName: Full=p2;
DE Contains:
DE RecName: Full=Nucleocapsid protein p7;
DE Short=NC;
DE Contains:
DE RecName: Full=Spacer peptide 2 {ECO:0000250|UniProtKB:P12493};
DE Short=SP2;
DE AltName: Full=p1;
DE Contains:
DE RecName: Full=p6-gag;
GN Name=gag;
OS Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11706;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3040055; DOI=10.1089/aid.1987.3.57;
RA Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C.,
RA Wong-Staal F.;
RT "Complete nucleotide sequences of functional clones of the AIDS virus.";
RL AIDS Res. Hum. Retroviruses 3:57-69(1987).
RN [2]
RP FUNCTION (CAPSID PROTEIN P24).
RX PubMed=8648689; DOI=10.1128/jvi.70.6.3551-3560.1996;
RA Braaten D., Franke E.K., Luban J.;
RT "Cyclophilin A is required for an early step in the life cycle of human
RT immunodeficiency virus type 1 before the initiation of reverse
RT transcription.";
RL J. Virol. 70:3551-3560(1996).
RN [3]
RP MUTAGENESIS OF PRO-217; VAL-218; HIS-219; ALA-220; GLY-221; PRO-222;
RP ILE-223; ALA-224 AND PRO-225, AND INTERACTION WITH HUMAN CYPA.
RX PubMed=9223641; DOI=10.1006/jmbi.1997.1051;
RA Yoo S., Myszka D.G., Yeh C., McMurray M., Hill C.P., Sundquist W.I.;
RT "Molecular recognition in the HIV-1 capsid/cyclophilin A complex.";
RL J. Mol. Biol. 269:780-795(1997).
RN [4]
RP MUTAGENESIS OF LYS-18; ARG-22 AND LYS-27.
RX PubMed=10604476; DOI=10.1038/45272;
RA Dupont S., Sharova N., DeHoratius C., Virbasius C.M., Zhu X.,
RA Bukrinskaya A.G., Stevenson M., Green M.R.;
RT "A novel nuclear export activity in HIV-1 matrix protein required for viral
RT replication.";
RL Nature 402:681-685(1999).
RN [5]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=9931246; DOI=10.1006/jmbi.1998.2460;
RA Negroni M., Buc H.;
RT "Recombination during reverse transcription: an evaluation of the role of
RT the nucleocapsid protein.";
RL J. Mol. Biol. 286:15-31(1999).
RN [6]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=11044125; DOI=10.1128/jvi.74.22.10796-10800.2000;
RA Cen S., Khorchid A., Gabor J., Rong L., Wainberg M.A., Kleiman L.;
RT "Roles of Pr55(gag) and NCp7 in tRNA(3)(Lys) genomic placement and the
RT initiation step of reverse transcription in human immunodeficiency virus
RT type 1.";
RL J. Virol. 74:10796-10800(2000).
RN [7]
RP GAG/GAG-POL RATIO.
RX PubMed=11160682; DOI=10.1128/jvi.75.4.1834-1841.2001;
RA Shehu-Xhilaga M., Crowe S.M., Mak J.;
RT "Maintenance of the Gag/Gag-Pol ratio is important for human
RT immunodeficiency virus type 1 RNA dimerization and viral infectivity.";
RL J. Virol. 75:1834-1841(2001).
RN [8]
RP CIS/TRANS ISOMERIZATION (CAPSID PROTEIN P24).
RX PubMed=11929983; DOI=10.1073/pnas.082100499;
RA Bosco D.A., Eisenmesser E.Z., Pochapsky S., Sundquist W.I., Kern D.;
RT "Catalysis of cis/trans isomerization in native HIV-1 capsid by human
RT cyclophilin A.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5247-5252(2002).
RN [9]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7), AND MUTAGENESIS OF HIS-400; CYS-405;
RP HIS-421 AND CYS-426.
RX PubMed=11932404; DOI=10.1128/jvi.76.9.4370-4378.2002;
RA Guo J., Wu T., Kane B.F., Johnson D.G., Henderson L.E., Gorelick R.J.,
RA Levin J.G.;
RT "Subtle alterations of the native zinc finger structures have dramatic
RT effects on the nucleic acid chaperone activity of human immunodeficiency
RT virus type 1 nucleocapsid protein.";
RL J. Virol. 76:4370-4378(2002).
RN [10]
RP FUNCTION (CAPSID PROTEIN P24), AND QUATERNARY STRUCTURE (CAPSID PROTEIN
RP P24).
RX PubMed=12660176; DOI=10.1093/emboj/cdg143;
RA Briggs J.A., Wilk T., Welker R., Krausslich H.G., Fuller S.D.;
RT "Structural organization of authentic, mature HIV-1 virions and cores.";
RL EMBO J. 22:1707-1715(2003).
RN [11]
RP CLEAVAGE (NUCLEOCAPSID PROTEIN P7).
RX PubMed=15065874; DOI=10.1021/bi035625z;
RA Tozser J., Shulenin S., Louis J.M., Copeland T.D., Oroszlan S.;
RT "In vitro processing of HIV-1 nucleocapsid protein by the viral proteinase:
RT effects of amino acid substitutions at the scissile bond in the proximal
RT zinc finger sequence.";
RL Biochemistry 43:4304-4312(2004).
RN [12]
RP MUTAGENESIS OF ASN-394.
RX PubMed=16904152; DOI=10.1016/j.virol.2006.07.011;
RA Thomas J.A., Shulenin S., Coren L.V., Bosche W.J., Gagliardi T.D.,
RA Gorelick R.J., Oroszlan S.;
RT "Characterization of human immunodeficiency virus type 1 (HIV-1) containing
RT mutations in the nucleocapsid protein at a putative HIV-1 protease cleavage
RT site.";
RL Virology 354:261-270(2006).
RN [13]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=17070549; DOI=10.1016/j.jmb.2006.09.081;
RA Hagan N.A., Fabris D.;
RT "Dissecting the protein-RNA and RNA-RNA interactions in the nucleocapsid-
RT mediated dimerization and isomerization of HIV-1 stemloop 1.";
RL J. Mol. Biol. 365:396-410(2007).
RN [14]
RP MUTAGENESIS OF SER-6; SER-9; SER-67 AND SER-72, AND PHOSPHORYLATION.
RX PubMed=17656588; DOI=10.1110/ps.072987607;
RA Saad J.S., Kim A., Ghanam R.H., Dalton A.K., Vogt V.M., Wu Z., Lu W.,
RA Summers M.F.;
RT "Mutations that mimic phosphorylation of the HIV-1 matrix protein do not
RT perturb the myristyl switch.";
RL Protein Sci. 16:1793-1797(2007).
RN [15]
RP SUBUNIT (MATRIX PROTEIN P17).
RX PubMed=17108052; DOI=10.1128/jvi.02122-06;
RA Alfadhli A., Huseby D., Kapit E., Colman D., Barklis E.;
RT "Human immunodeficiency virus type 1 matrix protein assembles on membranes
RT as a hexamer.";
RL J. Virol. 81:1472-1478(2007).
RN [16]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7).
RX PubMed=18343475; DOI=10.1016/j.virol.2008.02.001;
RA Kafaie J., Song R., Abrahamyan L., Mouland A.J., Laughrea M.;
RT "Mapping of nucleocapsid residues important for HIV-1 genomic RNA
RT dimerization and packaging.";
RL Virology 375:592-610(2008).
RN [17]
RP INTERACTION WITH HUMAN TRIM22.
RX PubMed=18389079; DOI=10.1371/journal.ppat.1000007;
RA Barr S.D., Smiley J.R., Bushman F.D.;
RT "The interferon response inhibits HIV particle production by induction of
RT TRIM22.";
RL PLoS Pathog. 4:E1000007-E1000007(2008).
RN [18]
RP SUBUNIT (CAPSID PROTEIN P24), AND FUNCTION (CAPSID PROTEIN P24).
RX PubMed=19914170; DOI=10.1016/j.cell.2009.10.010;
RA Byeon I.J., Meng X., Jung J., Zhao G., Yang R., Ahn J., Shi J., Concel J.,
RA Aiken C., Zhang P., Gronenborn A.M.;
RT "Structural convergence between Cryo-EM and NMR reveals intersubunit
RT interactions critical for HIV-1 capsid function.";
RL Cell 139:780-790(2009).
RN [19]
RP SUBUNIT (MATRIX PROTEIN P17).
RX PubMed=19327811; DOI=10.1016/j.virol.2009.02.048;
RA Alfadhli A., Barklis R.L., Barklis E.;
RT "HIV-1 matrix organizes as a hexamer of trimers on membranes containing
RT phosphatidylinositol-(4,5)-bisphosphate.";
RL Virology 387:466-472(2009).
RN [20]
RP FUNCTION (NUCLEOCAPSID PROTEIN P7), AND FUNCTION (GAG POLYPROTEIN).
RX PubMed=20828778; DOI=10.1016/j.virol.2010.08.013;
RA Jalalirad M., Laughrea M.;
RT "Formation of immature and mature genomic RNA dimers in wild-type and
RT protease-inactive HIV-1: differential roles of the Gag polyprotein,
RT nucleocapsid proteins NCp15, NCp9, NCp7, and the dimerization initiation
RT site.";
RL Virology 407:225-236(2010).
RN [21]
RP INTERACTION WITH HOST MOV10 (GAG POLYPROTEIN).
RX PubMed=20215113; DOI=10.1074/jbc.m110.109314;
RA Wang X., Han Y., Dang Y., Fu W., Zhou T., Ptak R.G., Zheng Y.H.;
RT "Moloney leukemia virus 10 (MOV10) protein inhibits retrovirus
RT replication.";
RL J. Biol. Chem. 285:14346-14355(2010).
RN [22]
RP INTERACTION WITH HOST PDZD8 (GAG POLYPROTEIN).
RX PubMed=20573829; DOI=10.1128/jvi.00843-10;
RA Henning M.S., Morham S.G., Goff S.P., Naghavi M.H.;
RT "PDZD8 is a novel Gag-interacting factor that promotes retroviral
RT infection.";
RL J. Virol. 84:8990-8995(2010).
RN [23]
RP INTERACTION WITH RAT CALM1 (MATRIX PROTEIN P17).
RX PubMed=24500712; DOI=10.1074/jbc.m113.543694;
RA Vlach J., Samal A.B., Saad J.S.;
RT "Solution structure of calmodulin bound to the binding domain of the HIV-1
RT matrix protein.";
RL J. Biol. Chem. 289:8697-8705(2014).
RN [24]
RP INTERACTION WITH MONKEY TRIM5 (CAPSID PROTEIN P24).
RX PubMed=23785198; DOI=10.1128/jvi.00713-13;
RA Shi J., Friedman D.B., Aiken C.;
RT "Retrovirus restriction by TRIM5 proteins requires recognition of only a
RT small fraction of viral capsid subunits.";
RL J. Virol. 87:9271-9278(2013).
RN [25]
RP INTERACTION OF CAPSID-NUCLEOCAPSID COMPLEX WITH HUMAN PDZD8, AND FUNCTION
RP (CAPSID PROTEIN P24).
RX PubMed=24554657; DOI=10.1128/jvi.02945-13;
RA Guth C.A., Sodroski J.;
RT "Contribution of PDZD8 to stabilization of the human immunodeficiency virus
RT type 1 capsid.";
RL J. Virol. 88:4612-4623(2014).
RN [26]
RP FUNCTION (CAPSID PROTEIN P24), INTERACTION WITH HUMAN NONO (CAPSID PROTEIN
RP P24), AND MUTAGENESIS OF GLN-182 AND 235-ASP-ILE-236.
RX PubMed=30270045; DOI=10.1016/j.cell.2018.08.062;
RA Lahaye X., Gentili M., Silvin A., Conrad C., Picard L., Jouve M., Zueva E.,
RA Maurin M., Nadalin F., Knott G.J., Zhao B., Du F., Rio M., Amiel J.,
RA Fox A.H., Li P., Etienne L., Bond C.S., Colleaux L., Manel N.;
RT "NONO detects the nuclear HIV capsid to promote cGAS-mediated innate immune
RT activation.";
RL Cell 175:488-501(2018).
RN [27]
RP REVIEW.
RX PubMed=9878383; DOI=10.1006/jmbi.1998.2354;
RA Turner B.G., Summers M.F.;
RT "Structural biology of HIV.";
RL J. Mol. Biol. 285:1-32(1999).
RN [28]
RP REVIEW.
RX PubMed=12873766; DOI=10.1016/s0005-2736(03)00163-9;
RA Scarlata S., Carter C.;
RT "Role of HIV-1 Gag domains in viral assembly.";
RL Biochim. Biophys. Acta 1614:62-72(2003).
RN [29]
RP REVIEW.
RX PubMed=16815734; DOI=10.1016/j.mib.2006.06.011;
RA Sokolskaja E., Luban J.;
RT "Cyclophilin, TRIM5, and innate immunity to HIV-1.";
RL Curr. Opin. Microbiol. 9:404-408(2006).
RN [30]
RP REVIEW.
RX PubMed=21762797; DOI=10.1016/j.jmb.2011.04.015;
RA Chukkapalli V., Ono A.;
RT "Molecular determinants that regulate plasma membrane association of HIV-1
RT Gag.";
RL J. Mol. Biol. 410:512-524(2011).
RN [31]
RP REVIEW.
RX PubMed=24907482; DOI=10.1016/j.virusres.2014.05.011;
RA Darlix J.L., de Rocquigny H., Mauffret O., Mely Y.;
RT "Retrospective on the all-in-one retroviral nucleocapsid protein.";
RL Virus Res. 193:2-15(2014).
RN [32]
RP REVIEW.
RX PubMed=24933691; DOI=10.1016/j.tim.2014.04.012;
RA Tedbury P.R., Freed E.O.;
RT "The role of matrix in HIV-1 envelope glycoprotein incorporation.";
RL Trends Microbiol. 22:372-378(2014).
CC -!- FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the
CC essential events in virion assembly, including binding the plasma
CC membrane, making the protein-protein interactions necessary to create
CC spherical particles, recruiting the viral Env proteins, and packaging
CC the genomic RNA via direct interactions with the RNA packaging sequence
CC (Psi). {ECO:0000269|PubMed:20828778}.
CC -!- FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma
CC membrane via a multipartite membrane-binding signal, that includes its
CC myristoylated N-terminus (By similarity). Matrix protein is part of the
CC pre-integration complex. Implicated in the release from host cell
CC mediated by Vpu. Binds to RNA (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P12493}.
CC -!- FUNCTION: [Capsid protein p24]: Forms the conical core that
CC encapsulates the genomic RNA-nucleocapsid complex in the virion. Most
CC core are conical, with only 7% tubular (PubMed:8648689,
CC PubMed:19914170). The core is constituted by capsid protein hexamer
CC subunits (PubMed:8648689, PubMed:19914170). The core is disassembled
CC soon after virion entry (PubMed:12660176). The capsid promotes immune
CC invasion by cloaking viral DNA from CGAS detection (PubMed:30270045).
CC Host restriction factors such as host TRIM5-alpha or TRIMCyp bind
CC retroviral capsids and cause premature capsid disassembly, leading to
CC blocks in reverse transcription (PubMed:23785198). Capsid restriction
CC by TRIM5 is one of the factors which restricts HIV-1 to the human
CC species (PubMed:23785198). Host PIN1 apparently facilitates the virion
CC uncoating (By similarity). On the other hand, interactions with PDZD8
CC or CYPA stabilize the capsid (PubMed:24554657).
CC {ECO:0000250|UniProtKB:P12493, ECO:0000269|PubMed:12660176,
CC ECO:0000269|PubMed:19914170, ECO:0000269|PubMed:23785198,
CC ECO:0000269|PubMed:24554657, ECO:0000269|PubMed:30270045,
CC ECO:0000269|PubMed:8648689}.
CC -!- FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral
CC dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc
CC fingers. Acts as a nucleic acid chaperone which is involved in
CC rearangement of nucleic acid secondary structure during gRNA
CC retrotranscription. Also facilitates template switch leading to
CC recombination. As part of the polyprotein, participates in gRNA
CC dimerization, packaging, tRNA incorporation and virion assembly.
CC {ECO:0000269|PubMed:11044125, ECO:0000269|PubMed:11932404,
CC ECO:0000269|PubMed:17070549, ECO:0000269|PubMed:18343475,
CC ECO:0000269|PubMed:20828778, ECO:0000269|PubMed:9931246}.
CC -!- FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle
CC by interacting with the host class E VPS proteins TSG101 and
CC PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: [Gag polyprotein]: Homotrimer; further assembles as hexamers
CC of trimers (By similarity). Oligomerization possibly creates a central
CC hole into which the cytoplasmic tail of the gp41 envelope protein may
CC be inserted. Interacts with host TRIM22; this interaction seems to
CC disrupt proper trafficking of Gag polyprotein and may interfere with
CC budding (PubMed:18389079). Interacts with host PDZD8 (PubMed:20573829).
CC When ubiquitinated, interacts (via p6-gag domain) with host PACSIN2;
CC this interaction allows PACSIN2 recruitment to viral assembly sites and
CC its subsequent incorporation into virions (By similarity). Interacts
CC with MOV10 (PubMed:20215113). {ECO:0000250|UniProtKB:P03349,
CC ECO:0000269|PubMed:18389079, ECO:0000269|PubMed:20215113,
CC ECO:0000269|PubMed:20573829}.
CC -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC hexamers of trimers (PubMed:19327811). Interacts with gp41 (via C-
CC terminus) (By similarity). Interacts with host CALM1; this interaction
CC induces a conformational change in the Matrix protein, triggering
CC exposure of the myristate group (PubMed:24500712). Interacts with host
CC AP3D1; this interaction allows the polyprotein trafficking to
CC multivesicular bodies during virus assembly (By similarity). Part of
CC the pre-integration complex (PIC) which is composed of viral genome,
CC matrix protein, Vpr and integrase (By similarity).
CC {ECO:0000250|UniProtKB:P12493, ECO:0000269|PubMed:19327811,
CC ECO:0000269|PubMed:24500712}.
CC -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC multimerizes as homohexamers or homopentamers (PubMed:19914170).
CC Interacts with host NUP98 (By similarity). Interacts with host
CC PPIA/CYPA; this interaction stabilizes the capsid (PubMed:9223641).
CC Interacts with host NUP153 (By similarity). Interacts with host PDZD8;
CC this interaction stabilizes the capsid (PubMed:20573829). Interacts
CC with host TRIM5; this interaction destabilizes the capsid
CC (PubMed:23785198). Interacts with host CPSF6 (By similarity). Interacts
CC with host NONO; the interaction is weak (PubMed:30270045).
CC {ECO:0000250|UniProtKB:P12493, ECO:0000269|PubMed:19914170,
CC ECO:0000269|PubMed:20573829, ECO:0000269|PubMed:23785198,
CC ECO:0000269|PubMed:30270045, ECO:0000269|PubMed:9223641}.
CC -!- SUBUNIT: [Nucleocapsid protein p7]: Interacts with host NUP98.
CC {ECO:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: [p6-gag]: Interacts with Vpr; this interaction allows Vpr
CC incorporation into the virion (By similarity). Interacts with host
CC TSG101 (By similarity). Interacts with host PDCD6IP/AIP1 (By
CC similarity). {ECO:0000250|UniProtKB:P03348,
CC ECO:0000250|UniProtKB:P12493}.
CC -!- INTERACTION:
CC P04591; Q9HD40: SEPSECS; Xeno; NbExp=3; IntAct=EBI-6163428, EBI-6163446;
CC P04591; O95793-2: STAU1; Xeno; NbExp=4; IntAct=EBI-6163428, EBI-358189;
CC PRO_0000038593; Q12904: AIMP1; Xeno; NbExp=3; IntAct=EBI-6179719, EBI-1045802;
CC PRO_0000038593; Q13155: AIMP2; Xeno; NbExp=3; IntAct=EBI-6179719, EBI-745226;
CC PRO_0000038593; O43324: EEF1E1; Xeno; NbExp=4; IntAct=EBI-6179719, EBI-1048486;
CC PRO_0000038593; Q14978: NOLC1; Xeno; NbExp=2; IntAct=EBI-6179719, EBI-396155;
CC PRO_0000038593; Q9NTK5: OLA1; Xeno; NbExp=4; IntAct=EBI-6179719, EBI-766468;
CC PRO_0000038593; Q86SQ7: SDCCAG8; Xeno; NbExp=2; IntAct=EBI-6179719, EBI-1047850;
CC PRO_0000038593; Q9HD40: SEPSECS; Xeno; NbExp=5; IntAct=EBI-6179719, EBI-6163446;
CC PRO_0000038594; O95793-2: STAU1; Xeno; NbExp=2; IntAct=EBI-9871255, EBI-358189;
CC PRO_0000038596; Q9UI47: CTNNA3; Xeno; NbExp=2; IntAct=EBI-6179727, EBI-3937546;
CC PRO_0000038596; Q8N1G4: LRRC47; Xeno; NbExp=2; IntAct=EBI-6179727, EBI-2509921;
CC PRO_0000038596; Q9Y3B7: MRPL11; Xeno; NbExp=3; IntAct=EBI-6179727, EBI-5453723;
CC PRO_0000038596; Q99873: PRMT1; Xeno; NbExp=2; IntAct=EBI-6179727, EBI-78738;
CC PRO_0000038596; P55769: SNU13; Xeno; NbExp=2; IntAct=EBI-6179727, EBI-712228;
CC PRO_0000038596; Q7Z739: YTHDF3; Xeno; NbExp=2; IntAct=EBI-6179727, EBI-2849837;
CC PRO_0000038598; P80318: Cct3; Xeno; NbExp=3; IntAct=EBI-10634977, EBI-772361;
CC PRO_0000038598; Q99816-1: TSG101; Xeno; NbExp=3; IntAct=EBI-10634977, EBI-15891993;
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane; Lipid-
CC anchor. Host endosome, host multivesicular body
CC {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably
CC linked to virus assembly sites. The main location is the cell membrane,
CC but under some circumstances, late endosomal compartments can serve as
CC productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-
CC anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=Translation results in the formation of the Gag polyprotein
CC most of the time. Ribosomal frameshifting at the gag-pol genes
CC boundary occurs at low frequency and produces the Gag-Pol
CC polyprotein. This strategy of translation probably allows the virus
CC to modulate the quantity of each viral protein. Maintenance of a
CC correct Gag to Gag-Pol ratio is essential for RNA dimerization and
CC viral infectivity.;
CC Name=Gag polyprotein;
CC IsoId=P04591-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P04585-1; Sequence=External;
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. p6-gag contains two L domains: a PTAP/PSAP
CC motif, which interacts with the UEV domain of TSG101 and a LYPX(n)L
CC motif which interacts with PDCD6IP/AIP1.
CC {ECO:0000250|UniProtKB:P12493}.
CC -!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.
CC -!- PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the
CC virion by a host kinase. Phosphorylation is apparently not a major
CC regulator of membrane association (PubMed:17656588).
CC {ECO:0000269|PubMed:17656588}.
CC -!- PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this
CC phosphorylation is necessary for Pin1-mediated virion uncoating.
CC {ECO:0000250|UniProtKB:P12493}.
CC -!- PTM: [Nucleocapsid protein p7]: Methylated by host PRMT6, impairing its
CC function by reducing RNA annealing and the initiation of reverse
CC transcription. {ECO:0000250|UniProtKB:P03347}.
CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC majority of strains found worldwide belong to the group M. Group O
CC seems to be endemic to and largely confined to Cameroon and neighboring
CC countries in West Central Africa, where these viruses represent a small
CC minority of HIV-1 strains. The group N is represented by a limited
CC number of isolates from Cameroonian persons. The group M is further
CC subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC -!- MISCELLANEOUS: [Isoform Gag polyprotein]: Produced by conventional
CC translation.
CC -!- SIMILARITY: Belongs to the primate lentivirus group gag polyprotein
CC family. {ECO:0000305}.
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DR EMBL; K03455; AAB50258.1; -; Genomic_RNA.
DR RefSeq; NP_057850.1; NC_001802.1.
DR PDB; 1TSQ; X-ray; 2.00 A; P=429-438.
DR PDB; 1TSU; X-ray; 2.10 A; P=429-436.
DR PDB; 5FJB; EM; 9.00 A; A/B=133-350.
DR PDB; 5I1R; Other; -; A=378-432.
DR PDB; 5INC; X-ray; 2.88 A; E/F=308-316.
DR PDB; 5IND; X-ray; 2.13 A; E/F=308-316.
DR PDB; 5NME; X-ray; 2.94 A; C/H=77-85.
DR PDB; 5NMF; X-ray; 2.89 A; C/H=77-85.
DR PDB; 5NMG; X-ray; 2.75 A; C/H=77-85.
DR PDB; 5NMH; X-ray; 1.55 A; C=77-85.
DR PDB; 5NMK; X-ray; 1.66 A; C=77-85.
DR PDB; 6CPL; X-ray; 2.45 A; C=293-312.
DR PDB; 6CPN; X-ray; 2.00 A; C=299-311.
DR PDB; 6CPO; X-ray; 2.40 A; C/F=299-311.
DR PDB; 6CQJ; X-ray; 2.75 A; C/F/I=299-311.
DR PDB; 6CQL; X-ray; 2.40 A; C=299-311.
DR PDB; 6CQN; X-ray; 2.50 A; C=299-311.
DR PDB; 6CQQ; X-ray; 2.80 A; C/H=299-311.
DR PDB; 6CQR; X-ray; 3.04 A; C/H=299-311.
DR PDB; 6EC2; X-ray; 3.40 A; A/C/F/G=133-363.
DR PDB; 6ECN; X-ray; 3.40 A; A/B/D/E=133-363.
DR PDB; 6ECO; X-ray; 4.20 A; A=133-358, D=133-353.
DR PDB; 6N3J; EM; 3.00 A; A/B/C/D/E/F=278-377.
DR PDB; 6N3U; EM; 2.90 A; A/B/C/D/E/F=278-377.
DR PDB; 6ZDJ; EM; 5.80 A; A/B/C/D/G/H/N/Y/d/e/j/k=133-352.
DR PDBsum; 1TSQ; -.
DR PDBsum; 1TSU; -.
DR PDBsum; 5FJB; -.
DR PDBsum; 5I1R; -.
DR PDBsum; 5INC; -.
DR PDBsum; 5IND; -.
DR PDBsum; 5NME; -.
DR PDBsum; 5NMF; -.
DR PDBsum; 5NMG; -.
DR PDBsum; 5NMH; -.
DR PDBsum; 5NMK; -.
DR PDBsum; 6CPL; -.
DR PDBsum; 6CPN; -.
DR PDBsum; 6CPO; -.
DR PDBsum; 6CQJ; -.
DR PDBsum; 6CQL; -.
DR PDBsum; 6CQN; -.
DR PDBsum; 6CQQ; -.
DR PDBsum; 6CQR; -.
DR PDBsum; 6EC2; -.
DR PDBsum; 6ECN; -.
DR PDBsum; 6ECO; -.
DR PDBsum; 6N3J; -.
DR PDBsum; 6N3U; -.
DR PDBsum; 6ZDJ; -.
DR BMRB; P04591; -.
DR SMR; P04591; -.
DR BioGRID; 1205537; 195.
DR ELM; P04591; -.
DR IntAct; P04591; 48.
DR MEROPS; A02.001; -.
DR PRIDE; P04591; -.
DR GeneID; 155030; -.
DR KEGG; vg:155030; -.
DR Reactome; R-HSA-162585; Uncoating of the HIV Virion.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-162592; Integration of provirus.
DR Reactome; R-HSA-162594; Early Phase of HIV Life Cycle.
DR Reactome; R-HSA-164516; Minus-strand DNA synthesis.
DR Reactome; R-HSA-164525; Plus-strand DNA synthesis.
DR Reactome; R-HSA-164843; 2-LTR circle formation.
DR Reactome; R-HSA-173107; Binding and entry of HIV virion.
DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR Reactome; R-HSA-174495; Synthesis And Processing Of GAG, GAGPOL Polyproteins.
DR Reactome; R-HSA-175474; Assembly Of The HIV Virion.
DR Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
DR Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
DR Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR EvolutionaryTrace; P04591; -.
DR PRO; PR:P04591; -.
DR Proteomes; UP000002241; Genome.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:CACAO.
DR GO; GO:0005730; C:nucleolus; IDA:CACAO.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
DR Gene3D; 1.10.1200.30; -; 1.
DR Gene3D; 1.10.150.90; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR045345; Gag_p24_C.
DR InterPro; IPR000721; Gag_p24_N.
DR InterPro; IPR014817; Gag_p6.
DR InterPro; IPR000071; Lentvrl_matrix_N.
DR InterPro; IPR012344; Matrix_HIV/RSV_N.
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; PF00540; Gag_p17; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR Pfam; PF08705; Gag_p6; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR PRINTS; PR00234; HIV1MATRIX.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; Capsid protein; Host cell membrane; Host cytoplasm;
KW Host endosome; Host membrane; Host nucleus; Host-virus interaction;
KW Lipoprotein; Membrane; Metal-binding; Methylation; Myristate;
KW Phosphoprotein; Reference proteome; Repeat; Ribosomal frameshifting;
KW RNA-binding; Viral budding; Viral budding via the host ESCRT complexes;
KW Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..500
FT /note="Gag polyprotein"
FT /id="PRO_0000261216"
FT CHAIN 2..132
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038593"
FT CHAIN 133..363
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038594"
FT PEPTIDE 364..377
FT /note="Spacer peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038595"
FT CHAIN 378..432
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038596"
FT PEPTIDE 433..448
FT /note="Spacer peptide 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038597"
FT CHAIN 449..500
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038598"
FT ZN_FING 390..407
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 411..428
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 7..31
FT /note="Interaction with Gp41"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT REGION 8..43
FT /note="Interaction with host CALM1"
FT /evidence="ECO:0000269|PubMed:24500712"
FT REGION 12..19
FT /note="Interaction with host AP3D1"
FT /evidence="ECO:0000250|UniProtKB:P12497"
FT REGION 14..33
FT /note="Interaction with membrane phosphatidylinositol 4,5-
FT bisphosphate and RNA"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT REGION 73..77
FT /note="Interaction with membrane phosphatidylinositol 4,5-
FT bisphosphate"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..227
FT /note="Interaction with host PPIA/CYPA and NUP153"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT REGION 217..225
FT /note="PPIA/CYPA-binding loop"
FT REGION 277..363
FT /note="Dimerization/Multimerization of capsid protein p24"
FT REGION 444..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..22
FT /note="Nuclear export signal"
FT MOTIF 26..32
FT /note="Nuclear localization signal"
FT MOTIF 455..458
FT /note="PTAP/PSAP motif"
FT MOTIF 483..492
FT /note="LYPX(n)L motif"
FT SITE 132..133
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 363..364
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 377..378
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 432..433
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 448..449
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT MOD_RES 148
FT /note="Phosphoserine; by host MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT MOD_RES 387
FT /note="Asymmetric dimethylarginine; in Nucleocapsid protein
FT p7; by host PRMT6"
FT /evidence="ECO:0000250"
FT MOD_RES 409
FT /note="Asymmetric dimethylarginine; in Nucleocapsid protein
FT p7; by host PRMT6"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT MUTAGEN 6
FT /note="S->D: No influence on the PIP2- or concentration-
FT dependent myristyl switch mechanism."
FT /evidence="ECO:0000269|PubMed:17656588"
FT MUTAGEN 9
FT /note="S->D: No influence on the PIP2- or concentration-
FT dependent myristyl switch mechanism."
FT /evidence="ECO:0000269|PubMed:17656588"
FT MUTAGEN 18
FT /note="K->A: Replication-defective, induces nuclear
FT mislocalization of matrix protein; when associated with G-
FT 22."
FT /evidence="ECO:0000269|PubMed:10604476"
FT MUTAGEN 22
FT /note="R->G: Replication-defective, induces nuclear
FT mislocalization of matrix protein; when associated with A-
FT 18."
FT /evidence="ECO:0000269|PubMed:10604476"
FT MUTAGEN 27
FT /note="K->A: No effect on subcellular localization of
FT matrix protein; when associated with A-18 and G-22."
FT /evidence="ECO:0000269|PubMed:10604476"
FT MUTAGEN 67
FT /note="S->D: No influence on the PIP2- or concentration-
FT dependent myristyl switch mechanism."
FT /evidence="ECO:0000269|PubMed:17656588"
FT MUTAGEN 72
FT /note="S->D: No influence on the PIP2- or concentration-
FT dependent myristyl switch mechanism."
FT /evidence="ECO:0000269|PubMed:17656588"
FT MUTAGEN 182
FT /note="Q->Y: Increased interaction with human NONO."
FT /evidence="ECO:0000269|PubMed:30270045"
FT MUTAGEN 217
FT /note="P->A: 3-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 218
FT /note="V->A: 2.7-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 219
FT /note="H->A,Q: 8-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 220
FT /note="A->G: 44-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 220
FT /note="A->V: 3.4-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 221
FT /note="G->A: 31-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 221
FT /note="G->V: 154-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 222
FT /note="P->A: 36-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 222
FT /note="P->V: More than 150-fold decrease of PPIA-binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 223
FT /note="I->A: 1.2-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 223
FT /note="I->V: 1.0-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 224
FT /note="A->G: 2.3-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 224
FT /note="A->V: 1.7-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 225
FT /note="P->A: 1.6-fold decrease of PPIA-binding affinity."
FT /evidence="ECO:0000269|PubMed:9223641"
FT MUTAGEN 235..236
FT /note="DI->AA: Strongly decreased interaction with human
FT NONO."
FT /evidence="ECO:0000269|PubMed:30270045"
FT MUTAGEN 394
FT /note="N->F,G: Decreases infectivity and replication."
FT /evidence="ECO:0000269|PubMed:16904152"
FT MUTAGEN 400
FT /note="H->C: Complete loss of infectivity and in vitro
FT chaperone activity."
FT /evidence="ECO:0000269|PubMed:11932404"
FT MUTAGEN 405
FT /note="C->H: Complete loss of infectivity and DNA
FT synthesis."
FT /evidence="ECO:0000269|PubMed:11932404"
FT MUTAGEN 421
FT /note="H->C: Partial loss of infectivity. Complete loss of
FT in vitro chaperone activity."
FT /evidence="ECO:0000269|PubMed:11932404"
FT MUTAGEN 426
FT /note="C->H: Partial loss of infectivity."
FT /evidence="ECO:0000269|PubMed:11932404"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6N3U"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:6N3U"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:6N3U"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:6N3U"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:6N3U"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:6N3U"
FT HELIX 356..369
FT /evidence="ECO:0007829|PDB:6N3U"
SQ SEQUENCE 500 AA; 55930 MW; B74C3858C20EF82C CRC64;
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA LDKIEEEQNK SKKKAQQAAA
DTGHSNQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT
STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA
RVLAEAMSQV TNSATIMMQR GNFRNQRKIV KCFNCGKEGH TARNCRAPRK KGCWKCGKEG
HQMKDCTERQ ANFLGKIWPS YKGRPGNFLQ SRPEPTAPPE ESFRSGVETT TPPQKQEPID
KELYPLTSLR SLFGNDPSSQ
