GAG_HV1N5
ID GAG_HV1N5 Reviewed; 500 AA.
AC P12493;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
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:0000303|PubMed:22334652};
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:0000303|PubMed:22334652};
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 NY5)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11698;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone pNL4-3;
RA Buckler C.E., Buckler-White A.J., Willey R.L., McCoy J.;
RL Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION OF MATRIX PROTEIN P17 WITH GP41.
RX PubMed=8918455; DOI=10.1002/j.1460-2075.1996.tb00964.x;
RA Cosson P.;
RT "Direct interaction between the envelope and matrix proteins of HIV-1.";
RL EMBO J. 15:5783-5788(1996).
RN [3]
RP INTERACTION OF CAPSID PROTEIN WITH HUMAN PPIA/CYPA.
RX PubMed=8980234; DOI=10.1016/s0092-8674(00)81823-1;
RA Gamble T.R., Vajdos F.F., Yoo S., Worthylake D.K., Houseweart M.,
RA Sundquist W.I., Hill C.P.;
RT "Crystal structure of human cyclophilin A bound to the amino-terminal
RT domain of HIV-1 capsid.";
RL Cell 87:1285-1294(1996).
RN [4]
RP INTERACTION OF P6-GAG WITH HUMAN TSG101, AND FUNCTION (P6-GAG).
RX PubMed=11427703; DOI=10.1073/pnas.131059198;
RA VerPlank L., Bouamr F., LaGrassa T.J., Agresta B., Kikonyogo A., Leis J.,
RA Carter C.A.;
RT "Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L
RT domain in HIV type 1 Pr55(Gag).";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7724-7729(2001).
RN [5]
RP INTERACTION OF P6-GAG WITH HUMAN TSG101, AND FUNCTION (P6-GAG).
RX PubMed=11595185; DOI=10.1016/s0092-8674(01)00506-2;
RA Garrus J.E., von Schwedler U.K., Pornillos O.W., Morham S.G., Zavitz K.H.,
RA Wang H.E., Wettstein D.A., Stray K.M., Cote M., Rich R.L., Myszka D.G.,
RA Sundquist W.I.;
RT "Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1
RT budding.";
RL Cell 107:55-65(2001).
RN [6]
RP SUBCELLULAR LOCATION OF GAG POLYPROTEIN.
RX PubMed=14722309; DOI=10.1128/jvi.78.3.1552-1563.2004;
RA Ono A., Freed E.O.;
RT "Cell-type-dependent targeting of human immunodeficiency virus type 1
RT assembly to the plasma membrane and the multivesicular body.";
RL J. Virol. 78:1552-1563(2004).
RN [7]
RP INTERACTION OF MATRIX PROTEIN P17 WITH HUMAN AP3D1.
RX PubMed=15766529; DOI=10.1016/j.cell.2004.12.023;
RA Dong X., Li H., Derdowski A., Ding L., Burnett A., Chen X., Peters T.R.,
RA Dermody T.S., Woodruff E., Wang J.J., Spearman P.;
RT "AP-3 directs the intracellular trafficking of HIV-1 Gag and plays a key
RT role in particle assembly.";
RL Cell 120:663-674(2005).
RN [8]
RP INTERACTION OF MATRIX PROTEIN P17 WITH PHOSPHATIDYLINOSITOL
RP 4,5-BISPHOSPHATE, AND FUNCTION (MATRIX PROTEIN P17).
RX PubMed=16840558; DOI=10.1073/pnas.0602818103;
RA Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., Summers M.F.;
RT "Structural basis for targeting HIV-1 Gag proteins to the plasma membrane
RT for virus assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11364-11369(2006).
RN [9]
RP MUTAGENESIS OF SER-9; SER-67; SER-72 AND SER-77.
RX PubMed=19059618; DOI=10.1016/j.virol.2008.10.047;
RA Bhatia A.K., Kaushik R., Campbell N.A., Pontow S.E., Ratner L.;
RT "Mutation of critical serine residues in HIV-1 matrix result in an envelope
RT incorporation defect which can be rescued by truncation of the gp41
RT cytoplasmic tail.";
RL Virology 384:233-241(2009).
RN [10]
RP LATE-BUDDING DOMAINS, INTERACTION OF P6-GAG WITH HOST TSG101, INTERACTION
RP OF P6-GAG WITH HOST PDCD6IP/AIP1, AND FUNCTION (P6-GAG).
RX PubMed=19282983; DOI=10.1371/journal.ppat.1000339;
RA Dussupt V., Javid M.P., Abou-Jaoude G., Jadwin J.A., de La Cruz J.,
RA Nagashima K., Bouamr F.;
RT "The nucleocapsid region of HIV-1 Gag cooperates with the PTAP and LYPXnL
RT late domains to recruit the cellular machinery necessary for viral
RT budding.";
RL PLoS Pathog. 5:E1000339-E1000339(2009).
RN [11]
RP INTERACTION OF MATRIX PROTEIN P17 WITH RAT CALM1.
RX PubMed=21799007; DOI=10.1074/jbc.m111.273623;
RA Samal A.B., Ghanam R.H., Fernandez T.F., Monroe E.B., Saad J.S.;
RT "NMR, biophysical, and biochemical studies reveal the minimal Calmodulin
RT binding domain of the HIV-1 matrix protein.";
RL J. Biol. Chem. 286:33533-33543(2011).
RN [12]
RP PROTEOLYTIC PROCESSING OF GAG POLYPROTEIN.
RX PubMed=22334652; DOI=10.1074/jbc.m112.339374;
RA Lee S.K., Potempa M., Kolli M., Ozen A., Schiffer C.A., Swanstrom R.;
RT "Context surrounding processing sites is crucial in determining cleavage
RT rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol
RT polyprotein precursors by viral protease.";
RL J. Biol. Chem. 287:13279-13290(2012).
RN [13]
RP INTERACTION OF CAPSID WITH HUMAN NUP153 AND HUMAN CPSF6, AND MUTAGENESIS OF
RP ASN-189 AND ASN-206.
RC STRAIN=Clone pNL4-3;
RX PubMed=24130490; DOI=10.1371/journal.ppat.1003693;
RA Matreyek K.A., Yucel S.S., Li X., Engelman A.;
RT "Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding
RT pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.";
RL PLoS Pathog. 9:E1003693-E1003693(2013).
RN [14]
RP INTERACTION OF CAPSID WITH HUMAN NUP153 AND HUMAN NUP98, AND MUTAGENESIS OF
RP ASN-206.
RX PubMed=23523133; DOI=10.1016/j.virol.2013.02.008;
RA Di Nunzio F., Fricke T., Miccio A., Valle-Casuso J.C., Perez P., Souque P.,
RA Rizzi E., Severgnini M., Mavilio F., Charneau P., Diaz-Griffero F.;
RT "Nup153 and Nup98 bind the HIV-1 core and contribute to the early steps of
RT HIV-1 replication.";
RL Virology 440:8-18(2013).
RN [15]
RP SUBUNIT (CAPSID PROTEIN P24).
RX PubMed=24066695; DOI=10.1021/ja406246z;
RA Deshmukh L., Schwieters C.D., Grishaev A., Ghirlando R., Baber J.L.,
RA Clore G.M.;
RT "Structure and dynamics of full-length HIV-1 capsid protein in solution.";
RL J. Am. Chem. Soc. 135:16133-16147(2013).
RN [16]
RP INTERACTION OF MATRIX PROTEIN P17 WITH RNA, AND FUNCTION (MATRIX PROTEIN
RP P17).
RX PubMed=23552424; DOI=10.1128/jvi.00075-13;
RA Chukkapalli V., Inlora J., Todd G.C., Ono A.;
RT "Evidence in support of RNA-mediated inhibition of phosphatidylserine-
RT dependent HIV-1 Gag membrane binding in cells.";
RL J. Virol. 87:7155-7159(2013).
RN [17]
RP PHOSPHORYLATION AT SER-148 (CAPSID PROTEIN P24), AND FUNCTION (CAPSID
RP PROTEIN P24).
RX PubMed=24509437; DOI=10.1099/vir.0.060053-0;
RA Dochi T., Nakano T., Inoue M., Takamune N., Shoji S., Sano K., Misumi S.;
RT "Phosphorylation of human immunodeficiency virus type 1 capsid protein at
RT serine 16, required for peptidyl-prolyl isomerase-dependent uncoating, is
RT mediated by virion-incorporated extracellular signal-regulated kinase 2.";
RL J. Gen. Virol. 95:1156-1166(2014).
RN [18]
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 [19] {ECO:0007744|PDB:1GWP}
RP STRUCTURE BY NMR OF 133-283.
RX PubMed=12032547; DOI=10.1038/nsb806;
RA Tang C., Ndassa Y., Summers M.F.;
RT "Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag
RT polyprotein.";
RL Nat. Struct. Biol. 9:537-543(2002).
RN [20] {ECO:0007744|PDB:2C55}
RP STRUCTURE BY NMR OF 449-500.
RX PubMed=16234236; DOI=10.1074/jbc.m507375200;
RA Fossen T., Wray V., Bruns K., Rachmat J., Henklein P., Tessmer U.,
RA Maczurek A., Klinger P., Schubert U.;
RT "Solution structure of the human immunodeficiency virus type 1 p6
RT protein.";
RL J. Biol. Chem. 280:42515-42527(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 133-363, INTERACTION WITH HUMAN
RP NUP153, AND MUTAGENESIS OF PRO-166; ILE-169; PRO-170; ASN-185; LEU-188;
RP ASN-189; VAL-191; ASN-206; VAL-274; ARG-305 AND GLN-308.
RX PubMed=29997211; DOI=10.1128/jvi.00648-18;
RA Buffone C., Martinez-Lopez A., Fricke T., Opp S., Severgnini M., Cifola I.,
RA Petiti L., Frabetti S., Skorupka K., Zadrozny K.K., Ganser-Pornillos B.K.,
RA Pornillos O., Di Nunzio F., Diaz-Griffero F.;
RT "Nup153 Unlocks the Nuclear Pore Complex for HIV-1 Nuclear Translocation in
RT Nondividing Cells.";
RL J. Virol. 92:0-0(2018).
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:0000250|UniProtKB:P04591}.
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 (PubMed:16840558). Matrix protein is part of
CC the pre-integration complex. Implicated in the release from host cell
CC mediated by Vpu. Binds to RNA (PubMed:23552424). {ECO:0000250,
CC ECO:0000269|PubMed:16840558, ECO:0000269|PubMed:23552424}.
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. The core is constituted by
CC capsid protein hexamer subunits. The core is disassembled soon after
CC virion entry (By similarity). The capsid promotes immune invasion by
CC cloaking viral DNA from CGAS detection (By similarity). Host
CC restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral
CC capsids and cause premature capsid disassembly, leading to blocks in
CC reverse transcription. Capsid restriction by TRIM5 is one of the
CC factors which restricts HIV-1 to the human species. Host PIN1
CC apparently facilitates the virion uncoating (PubMed:24509437). On the
CC other hand, interactions with PDZD8 or CYPA stabilize the capsid.
CC {ECO:0000250|UniProtKB:P04591, ECO:0000269|PubMed:24509437}.
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:0000250|UniProtKB:P04591}.
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:0000269|PubMed:11427703,
CC ECO:0000269|PubMed:11595185, ECO:0000269|PubMed:19282983}.
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 (By similarity). Interacts with host PDZD8 (By similarity).
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). When
CC ubiquitinated, interacts (via p6-gag domain) with host PACSIN2; this
CC interaction allows PACSIN2 recruitment to viral assembly sites and its
CC subsequent incorporation into virions. Interacts with MOV10 (By
CC similarity). {ECO:0000250|UniProtKB:P03349,
CC ECO:0000250|UniProtKB:P04591}.
CC -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC hexamers of trimers (By similarity). Interacts with gp41 (via C-
CC terminus) (PubMed:8918455). Interacts with host CALM1; this interaction
CC induces a conformational change in the Matrix protein, triggering
CC exposure of the myristate group (PubMed:21799007). Interacts with host
CC AP3D1; this interaction allows the polyprotein trafficking to
CC multivesicular bodies during virus assembly (PubMed:15766529). 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:P04591, ECO:0000269|PubMed:15766529,
CC ECO:0000269|PubMed:21799007, ECO:0000269|PubMed:8918455}.
CC -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC multimerizes as homohexamers or homopentamers (PubMed:24066695).
CC Interacts with host NUP98 (PubMed:23523133). Interacts with host
CC PPIA/CYPA; this interaction stabilizes the capsid (PubMed:8980234).
CC Interacts with host NUP153 (PubMed:24130490, PubMed:23523133,
CC PubMed:29997211). Interacts with host PDZD8; this interaction
CC stabilizes the capsid (By similarity). Interacts with host TRIM5; this
CC interaction destabilizes the capsid (By similarity). Interacts with
CC host CPSF6 (PubMed:24130490). Interacts with host NONO; the interaction
CC is weak (By similarity). {ECO:0000250|UniProtKB:P04591,
CC ECO:0000269|PubMed:23523133, ECO:0000269|PubMed:24066695,
CC ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:29997211,
CC ECO:0000269|PubMed:8980234}.
CC -!- SUBUNIT: [Nucleocapsid protein p7]: Interacts with host NUP98.
CC {ECO:0000269|PubMed:23523133}.
CC -!- SUBUNIT: [p6-gag]: Interacts with Vpr; this interaction allows Vpr
CC incorporation into the virion (By similarity). Interacts with host
CC TSG101 (PubMed:11427703, PubMed:11595185). Interacts with host
CC PDCD6IP/AIP1(PubMed:19282983). {ECO:0000250|UniProtKB:P03348,
CC ECO:0000269|PubMed:11427703, ECO:0000269|PubMed:19282983}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane; Lipid-
CC anchor {ECO:0000269|PubMed:14722309}. Host endosome, host
CC multivesicular body. Note=These locations are probably linked to virus
CC assembly sites. The main location is the cell membrane, but under some
CC circumstances, late endosomal compartments can serve as productive
CC sites for virion assembly. {ECO:0000269|PubMed:14722309}.
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=P12493-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P12497-1; 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. {ECO:0000269|PubMed:19282983}.
CC -!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. {ECO:0000269|PubMed:22334652}.
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. {ECO:0000250|UniProtKB:P04591}.
CC -!- PTM: [Capsid protein p24]: Phosphorylated possibly by host MAPK1; this
CC phosphorylation is necessary for Pin1-mediated virion uncoating.
CC {ECO:0000269|PubMed:24509437}.
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: The infectious clone pNL4-3 is a chimeric provirus that
CC consists of DNA from HIV isolates NY5 (5' half) and BRU (3' half).
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; M19921; AAA44987.1; -; Genomic_RNA.
DR PDB; 1GWP; NMR; -; A=133-283.
DR PDB; 2C55; NMR; -; A=449-500.
DR PDB; 2MGU; NMR; -; M=8-43.
DR PDB; 3GV2; X-ray; 7.00 A; A/B/C/D/E/F=133-351.
DR PDB; 4U0A; X-ray; 2.05 A; A=133-363.
DR PDB; 4U0B; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
DR PDB; 4U0C; X-ray; 1.77 A; A=133-363.
DR PDB; 4U0D; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
DR PDB; 4U0E; X-ray; 2.04 A; A=133-363.
DR PDB; 4U0F; X-ray; 2.22 A; A=133-363.
DR PDB; 4XFX; X-ray; 2.43 A; A=133-363.
DR PDB; 4XFY; X-ray; 2.80 A; A=133-363.
DR PDB; 4XFZ; X-ray; 2.70 A; A=133-363.
DR PDB; 4XRO; X-ray; 2.01 A; A=133-363.
DR PDB; 4XRQ; X-ray; 1.95 A; A=133-363.
DR PDB; 5HGL; X-ray; 3.10 A; A/B/C/D/E/F=133-363.
DR PDB; 5HGM; X-ray; 2.04 A; A=133-363.
DR PDB; 5HGN; X-ray; 1.90 A; A=133-363.
DR PDB; 5HGO; X-ray; 2.00 A; A=133-363.
DR PDB; 5HGP; X-ray; 1.95 A; A=133-363.
DR PDB; 5IRT; NMR; -; A/B=133-363.
DR PDB; 5JPA; X-ray; 1.70 A; A=133-363.
DR PDB; 5L93; EM; 3.90 A; A/B/C=148-371.
DR PDB; 5O2U; X-ray; 2.76 A; A/C=1-500.
DR PDB; 5TSV; X-ray; 2.50 A; A/B=133-363.
DR PDB; 5TSX; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
DR PDB; 5UPW; EM; 5.00 A; A/B/C/D/E/F=133-353.
DR PDB; 5W4O; X-ray; 2.09 A; A=133-363.
DR PDB; 5W4P; X-ray; 2.19 A; A=133-363.
DR PDB; 5W4Q; X-ray; 2.29 A; A=133-363.
DR PDB; 6AXR; X-ray; 2.30 A; A=133-363.
DR PDB; 6AXS; X-ray; 2.40 A; A=133-363.
DR PDB; 6AXT; X-ray; 2.40 A; A=133-363.
DR PDB; 6AXV; X-ray; 2.77 A; A=133-363.
DR PDB; 6AXW; X-ray; 2.40 A; A=133-362.
DR PDB; 6AXX; X-ray; 2.60 A; A=133-363.
DR PDB; 6AXY; X-ray; 2.78 A; A=133-363.
DR PDB; 6AY9; X-ray; 2.50 A; A=133-363.
DR PDB; 6AYA; X-ray; 2.40 A; A=133-363.
DR PDB; 6B2G; X-ray; 2.41 A; A=133-363.
DR PDB; 6B2H; X-ray; 2.60 A; A=133-363.
DR PDB; 6B2I; X-ray; 2.50 A; A=133-363.
DR PDB; 6B2J; X-ray; 2.21 A; A=133-363.
DR PDB; 6B2K; X-ray; 2.00 A; A=133-363.
DR PDB; 6BHS; X-ray; 1.98 A; A=133-363.
DR PDB; 6BHT; X-ray; 2.69 A; A/B/C/D/E/F/G/H/I/J/K/L=133-363.
DR PDB; 6ECN; X-ray; 3.40 A; A/B/D/E=133-363, C/F=133-278.
DR PDB; 6H09; X-ray; 2.00 A; A=133-351.
DR PDB; 6MQA; X-ray; 3.20 A; A=132-363.
DR PDB; 6MQO; X-ray; 3.20 A; A=132-363.
DR PDB; 6MQP; X-ray; 3.30 A; A=132-363.
DR PDB; 6OBH; X-ray; 2.96 A; A/B/C/D/E/F=132-363.
DR PDB; 6OMT; X-ray; 2.05 A; A=132-363.
DR PDB; 6PU1; X-ray; 2.28 A; A=133-363.
DR PDB; 6R6Q; X-ray; 2.73 A; A=133-351.
DR PDB; 6RWG; NMR; -; A=276-432.
DR PDB; 6V2F; X-ray; 2.00 A; A/B/C/D/E/F=132-363.
DR PDB; 6VKV; X-ray; 2.22 A; A/B/C=133-363.
DR PDB; 6VWS; EM; 6.08 A; A/B/C/D/M/N=133-352.
DR PDB; 6WAP; NMR; -; A=133-363.
DR PDB; 6X63; NMR; -; 0/0A/0B/0C/0D/0E/1/1A/1B/1C/1D/1E/2/2A/2B/2C/2D/2E/3/3A/3B/3C/3D/3E/4/4A/4B/4C/4D/4E=133-363.
DR PDB; 7E1J; X-ray; 2.72 A; A/B/C/D/E/F=1-116.
DR PDB; 7JXR; X-ray; 2.04 A; A/B/C/D/E/F=2-132.
DR PDB; 7JXS; X-ray; 2.35 A; A/B/C/D/E/F=2-132.
DR PDB; 7M9F; X-ray; 2.70 A; A=133-363.
DR PDB; 7OVQ; EM; 7.20 A; A/B/C/D/E/F/I/K/M/O/P/Q/R/S/X/Y/Z/b/c/d/f/h/l/m=2-116.
DR PDB; 7OVR; EM; 7.00 A; A/B/C/D/E/F/H/I/J/O/P/Q/R/S/U/W/Y/b/c/d/e/f/j/l=2-116.
DR PDBsum; 1GWP; -.
DR PDBsum; 2C55; -.
DR PDBsum; 2MGU; -.
DR PDBsum; 3GV2; -.
DR PDBsum; 4U0A; -.
DR PDBsum; 4U0B; -.
DR PDBsum; 4U0C; -.
DR PDBsum; 4U0D; -.
DR PDBsum; 4U0E; -.
DR PDBsum; 4U0F; -.
DR PDBsum; 4XFX; -.
DR PDBsum; 4XFY; -.
DR PDBsum; 4XFZ; -.
DR PDBsum; 4XRO; -.
DR PDBsum; 4XRQ; -.
DR PDBsum; 5HGL; -.
DR PDBsum; 5HGM; -.
DR PDBsum; 5HGN; -.
DR PDBsum; 5HGO; -.
DR PDBsum; 5HGP; -.
DR PDBsum; 5IRT; -.
DR PDBsum; 5JPA; -.
DR PDBsum; 5L93; -.
DR PDBsum; 5O2U; -.
DR PDBsum; 5TSV; -.
DR PDBsum; 5TSX; -.
DR PDBsum; 5UPW; -.
DR PDBsum; 5W4O; -.
DR PDBsum; 5W4P; -.
DR PDBsum; 5W4Q; -.
DR PDBsum; 6AXR; -.
DR PDBsum; 6AXS; -.
DR PDBsum; 6AXT; -.
DR PDBsum; 6AXV; -.
DR PDBsum; 6AXW; -.
DR PDBsum; 6AXX; -.
DR PDBsum; 6AXY; -.
DR PDBsum; 6AY9; -.
DR PDBsum; 6AYA; -.
DR PDBsum; 6B2G; -.
DR PDBsum; 6B2H; -.
DR PDBsum; 6B2I; -.
DR PDBsum; 6B2J; -.
DR PDBsum; 6B2K; -.
DR PDBsum; 6BHS; -.
DR PDBsum; 6BHT; -.
DR PDBsum; 6ECN; -.
DR PDBsum; 6H09; -.
DR PDBsum; 6MQA; -.
DR PDBsum; 6MQO; -.
DR PDBsum; 6MQP; -.
DR PDBsum; 6OBH; -.
DR PDBsum; 6OMT; -.
DR PDBsum; 6PU1; -.
DR PDBsum; 6R6Q; -.
DR PDBsum; 6RWG; -.
DR PDBsum; 6V2F; -.
DR PDBsum; 6VKV; -.
DR PDBsum; 6VWS; -.
DR PDBsum; 6WAP; -.
DR PDBsum; 6X63; -.
DR PDBsum; 7E1J; -.
DR PDBsum; 7JXR; -.
DR PDBsum; 7JXS; -.
DR PDBsum; 7M9F; -.
DR PDBsum; 7OVQ; -.
DR PDBsum; 7OVR; -.
DR BMRB; P12493; -.
DR SMR; P12493; -.
DR iPTMnet; P12493; -.
DR ABCD; P12493; 1 sequenced antibody.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR EvolutionaryTrace; P12493; -.
DR PRO; PR:P12493; -.
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:0016020; C:membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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; Repeat; Ribosomal frameshifting; RNA-binding;
KW 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_0000261226"
FT CHAIN 2..132
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038559"
FT CHAIN 133..363
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038560"
FT PEPTIDE 364..377
FT /note="Spacer peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038561"
FT CHAIN 378..432
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038562"
FT PEPTIDE 433..448
FT /note="Spacer peptide 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038563"
FT CHAIN 449..500
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038564"
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:0000269|PubMed:8918455"
FT REGION 8..43
FT /note="Interaction with host CALM1"
FT /evidence="ECO:0000250|UniProtKB:P04591"
FT REGION 12..19
FT /note="Interaction with host AP3D1"
FT /evidence="ECO:0000269|PubMed:15766529"
FT REGION 14..33
FT /note="Interaction with membrane phosphatidylinositol 4,5-
FT bisphosphate and RNA"
FT /evidence="ECO:0000269|PubMed:16840558"
FT REGION 73..77
FT /note="Interaction with membrane phosphatidylinositol 4,5-
FT bisphosphate"
FT /evidence="ECO:0000269|PubMed:16840558"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..227
FT /note="Interaction with human PPIA/CYPA and NUP153"
FT /evidence="ECO:0000269|PubMed:24130490,
FT ECO:0000269|PubMed:8980234"
FT REGION 217..225
FT /note="PPIA/CYPA-binding loop"
FT /evidence="ECO:0000250|UniProtKB:P04591"
FT REGION 277..363
FT /note="Dimerization/Multimerization of capsid protein p24"
FT /evidence="ECO:0000250|UniProtKB:P04591"
FT REGION 438..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 16..22
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 26..32
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
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:0000269|PubMed:24509437"
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 9
FT /note="S->A: Loss of ability to fuse with target cell
FT membranes and infect host cell."
FT /evidence="ECO:0000269|PubMed:19059618"
FT MUTAGEN 67
FT /note="S->A: Loss of ability to fuse with target cell
FT membranes and infect host cell."
FT /evidence="ECO:0000269|PubMed:19059618"
FT MUTAGEN 72
FT /note="S->A: Loss of ability to fuse with target cell
FT membranes and infect host cell."
FT /evidence="ECO:0000269|PubMed:19059618"
FT MUTAGEN 77
FT /note="S->A: Loss of ability to fuse with target cell
FT membranes and infect host cell."
FT /evidence="ECO:0000269|PubMed:19059618"
FT MUTAGEN 166
FT /note="P->A: Loss of infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 169
FT /note="I->S: Loss of infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 170
FT /note="P->A: Retains infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 185
FT /note="N->L: Loss of infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 188
FT /note="L->S: Loss of infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 189
FT /note="N->A: Reduces binding to human NUP153 and CPSF6.
FT Reduces infectivity to non-dividing cells. Retains
FT infectivity to dividing cells."
FT /evidence="ECO:0000269|PubMed:24130490,
FT ECO:0000269|PubMed:29997211"
FT MUTAGEN 189
FT /note="N->D: Reduces binding to human NUP153. Does not
FT affect binding to CPSF6. Reduces infectivity to non-
FT dividing cells. Retains infectivity to dividing cells."
FT /evidence="ECO:0000269|PubMed:24130490,
FT ECO:0000269|PubMed:29997211"
FT MUTAGEN 189
FT /note="N->S: Reduces protein stability. Loss of binding to
FT FG repeats of human NUP153. Loss of binding to CPSF6.
FT Decreases virus ability to integrate in intrafenic regions
FT compared to wild-type virus. Reduces infectivity to non-
FT dividing cells; virus undergo reverse transcription but not
FT nuclear translocation. Retains infectivity to dividing
FT cells."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 191
FT /note="V->A: Loss of infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 206
FT /note="N->A: Loss of binding to NUP153 and CPSF6."
FT /evidence="ECO:0000269|PubMed:24130490"
FT MUTAGEN 206
FT /note="N->D: Loss of binding to CPSF6. Does not affect
FT binding to NUP153. Retains infectivity to non-dividing
FT cells."
FT /evidence="ECO:0000269|PubMed:23523133,
FT ECO:0000269|PubMed:24130490, ECO:0000269|PubMed:29997211"
FT MUTAGEN 274
FT /note="V->T: Loss of infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 305
FT /note="R->A: Does not bind FG repeats of human NUP153. Loss
FT of infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 305
FT /note="R->K: Retains binding to FG repeats of human
FT NUP153."
FT /evidence="ECO:0000269|PubMed:29997211"
FT MUTAGEN 308
FT /note="Q->A: Retains infectivity."
FT /evidence="ECO:0000269|PubMed:29997211"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:7JXR"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:7JXR"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:7JXR"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:7JXR"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:7JXR"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:7JXR"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:7JXS"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:7JXR"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:7JXR"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:7JXR"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5JPA"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:5JPA"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 195..215
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6WAP"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4XFY"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:5JPA"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:5JPA"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 258..277
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:5JPA"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:6OBH"
FT HELIX 293..307
FT /evidence="ECO:0007829|PDB:5JPA"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:4XRQ"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:4U0C"
FT HELIX 319..324
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:5JPA"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:6RWG"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:5JPA"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:6B2J"
FT TURN 353..357
FT /evidence="ECO:0007829|PDB:6WAP"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:6RWG"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:6RWG"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:6RWG"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:6RWG"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:6RWG"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:6RWG"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6RWG"
FT TURN 414..417
FT /evidence="ECO:0007829|PDB:6RWG"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:6RWG"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:6RWG"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:2C55"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:2C55"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:2C55"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:2C55"
FT HELIX 487..490
FT /evidence="ECO:0007829|PDB:2C55"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:2C55"
SQ SEQUENCE 500 AA; 55819 MW; 08ECC125834088C6 CRC64;
MGARASVLSG GELDKWEKIR LRPGGKKQYK LKHIVWASRE LERFAVNPGL LETSEGCRQI
LGQLQPSLQT GSEELRSLYN TIAVLYCVHQ RIDVKDTKEA LDKIEEEQNK SKKKAQQAAA
DTGNNSQVSQ NYPIVQNLQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRLHPVHA GPIAPGQMRE PRGSDIAGTT
STLQEQIGWM THNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPG ATLEEMMTAC QGVGGPGHKA
RVLAEAMSQV TNPATIMIQK GNFRNQRKTV KCFNCGKEGH IAKNCRAPRK KGCWKCGKEG
HQMKDCTERQ ANFLGKIWPS HKGRPGNFLQ SRPEPTAPPE ESFRFGEETT TPSQKQEPID
KELYPLASLR SLFGSDPSSQ
