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Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag]

 GAG_HV1H2               Reviewed;         500 AA.
P04591;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 166.
RecName: Full=Gag polyprotein;
AltName: Full=Pr55Gag;
Contains:
RecName: Full=Matrix protein p17;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Spacer peptide 1 {ECO:0000250|UniProtKB:P12493};
Short=SP1;
AltName: Full=p2;
Contains:
RecName: Full=Nucleocapsid protein p7;
Short=NC;
Contains:
RecName: Full=Spacer peptide 2 {ECO:0000250|UniProtKB:P12493};
Short=SP2;
AltName: Full=p1;
Contains:
RecName: Full=p6-gag;
Name=gag;
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
(HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11706;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3040055; DOI=10.1089/aid.1987.3.57;
Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S.,
Gallo R.C., Wong-Staal F.;
"Complete nucleotide sequences of functional clones of the AIDS
virus.";
AIDS Res. Hum. Retroviruses 3:57-69(1987).
[2]
FUNCTION (CAPSID PROTEIN P24).
PubMed=8648689;
Braaten D., Franke E.K., Luban J.;
"Cyclophilin A is required for an early step in the life cycle of
human immunodeficiency virus type 1 before the initiation of reverse
transcription.";
J. Virol. 70:3551-3560(1996).
[3]
MUTAGENESIS OF PRO-217; VAL-218; HIS-219; ALA-220; GLY-221; PRO-222;
ILE-223; ALA-224 AND PRO-225, AND INTERACTION WITH HUMAN CYPA.
PubMed=9223641; DOI=10.1006/jmbi.1997.1051;
Yoo S., Myszka D.G., Yeh C., McMurray M., Hill C.P., Sundquist W.I.;
"Molecular recognition in the HIV-1 capsid/cyclophilin A complex.";
J. Mol. Biol. 269:780-795(1997).
[4]
MUTAGENESIS OF LYS-18; ARG-22 AND LYS-27.
PubMed=10604476; DOI=10.1038/45272;
Dupont S., Sharova N., DeHoratius C., Virbasius C.M., Zhu X.,
Bukrinskaya A.G., Stevenson M., Green M.R.;
"A novel nuclear export activity in HIV-1 matrix protein required for
viral replication.";
Nature 402:681-685(1999).
[5]
FUNCTION (NUCLEOCAPSID PROTEIN P7).
PubMed=9931246; DOI=10.1006/jmbi.1998.2460;
Negroni M., Buc H.;
"Recombination during reverse transcription: an evaluation of the role
of the nucleocapsid protein.";
J. Mol. Biol. 286:15-31(1999).
[6]
FUNCTION (NUCLEOCAPSID PROTEIN P7).
PubMed=11044125; DOI=10.1128/JVI.74.22.10796-10800.2000;
Cen S., Khorchid A., Gabor J., Rong L., Wainberg M.A., Kleiman L.;
"Roles of Pr55(gag) and NCp7 in tRNA(3)(Lys) genomic placement and the
initiation step of reverse transcription in human immunodeficiency
virus type 1.";
J. Virol. 74:10796-10800(2000).
[7]
GAG/GAG-POL RATIO.
PubMed=11160682; DOI=10.1128/JVI.75.4.1834-1841.2001;
Shehu-Xhilaga M., Crowe S.M., Mak J.;
"Maintenance of the Gag/Gag-Pol ratio is important for human
immunodeficiency virus type 1 RNA dimerization and viral
infectivity.";
J. Virol. 75:1834-1841(2001).
[8]
CIS/TRANS ISOMERIZATION (CAPSID PROTEIN P24).
PubMed=11929983; DOI=10.1073/pnas.082100499;
Bosco D.A., Eisenmesser E.Z., Pochapsky S., Sundquist W.I., Kern D.;
"Catalysis of cis/trans isomerization in native HIV-1 capsid by human
cyclophilin A.";
Proc. Natl. Acad. Sci. U.S.A. 99:5247-5252(2002).
[9]
FUNCTION (NUCLEOCAPSID PROTEIN P7), AND MUTAGENESIS OF HIS-400;
CYS-405; HIS-421 AND CYS-426.
PubMed=11932404; DOI=10.1128/JVI.76.9.4370-4378.2002;
Guo J., Wu T., Kane B.F., Johnson D.G., Henderson L.E., Gorelick R.J.,
Levin J.G.;
"Subtle alterations of the native zinc finger structures have dramatic
effects on the nucleic acid chaperone activity of human
immunodeficiency virus type 1 nucleocapsid protein.";
J. Virol. 76:4370-4378(2002).
[10]
FUNCTION (CAPSID PROTEIN P24), AND QUARTERNARY STRUCTURE (CAPSID
PROTEIN P24).
PubMed=12660176; DOI=10.1093/emboj/cdg143;
Briggs J.A., Wilk T., Welker R., Krausslich H.G., Fuller S.D.;
"Structural organization of authentic, mature HIV-1 virions and
cores.";
EMBO J. 22:1707-1715(2003).
[11]
CLEAVAGE (NUCLEOCAPSID PROTEIN P7).
PubMed=15065874; DOI=10.1021/bi035625z;
Tozser J., Shulenin S., Louis J.M., Copeland T.D., Oroszlan S.;
"In vitro processing of HIV-1 nucleocapsid protein by the viral
proteinase: effects of amino acid substitutions at the scissile bond
in the proximal zinc finger sequence.";
Biochemistry 43:4304-4312(2004).
[12]
MUTAGENESIS OF ASN-394.
PubMed=16904152; DOI=10.1016/j.virol.2006.07.011;
Thomas J.A., Shulenin S., Coren L.V., Bosche W.J., Gagliardi T.D.,
Gorelick R.J., Oroszlan S.;
"Characterization of human immunodeficiency virus type 1 (HIV-1)
containing mutations in the nucleocapsid protein at a putative HIV-1
protease cleavage site.";
Virology 354:261-270(2006).
[13]
FUNCTION (NUCLEOCAPSID PROTEIN P7).
PubMed=17070549; DOI=10.1016/j.jmb.2006.09.081;
Hagan N.A., Fabris D.;
"Dissecting the protein-RNA and RNA-RNA interactions in the
nucleocapsid-mediated dimerization and isomerization of HIV-1 stemloop
1.";
J. Mol. Biol. 365:396-410(2007).
[14]
MUTAGENESIS OF SER-6; SER-9; SER-67 AND SER-72, AND PHOSPHORYLATION.
PubMed=17656588; DOI=10.1110/ps.072987607;
Saad J.S., Kim A., Ghanam R.H., Dalton A.K., Vogt V.M., Wu Z., Lu W.,
Summers M.F.;
"Mutations that mimic phosphorylation of the HIV-1 matrix protein do
not perturb the myristyl switch.";
Protein Sci. 16:1793-1797(2007).
[15]
SUBUNIT (MATRIX PROTEIN P17).
PubMed=17108052; DOI=10.1128/JVI.02122-06;
Alfadhli A., Huseby D., Kapit E., Colman D., Barklis E.;
"Human immunodeficiency virus type 1 matrix protein assembles on
membranes as a hexamer.";
J. Virol. 81:1472-1478(2007).
[16]
FUNCTION (NUCLEOCAPSID PROTEIN P7).
PubMed=18343475; DOI=10.1016/j.virol.2008.02.001;
Kafaie J., Song R., Abrahamyan L., Mouland A.J., Laughrea M.;
"Mapping of nucleocapsid residues important for HIV-1 genomic RNA
dimerization and packaging.";
Virology 375:592-610(2008).
[17]
INTERACTION WITH HUMAN TRIM22.
PubMed=18389079; DOI=10.1371/journal.ppat.1000007;
Barr S.D., Smiley J.R., Bushman F.D.;
"The interferon response inhibits HIV particle production by induction
of TRIM22.";
PLoS Pathog. 4:E1000007-E1000007(2008).
[18]
SUBUNIT (CAPSID PROTEIN P24), AND FUNCTION (CAPSID PROTEIN P24).
PubMed=19914170; DOI=10.1016/j.cell.2009.10.010;
Byeon I.J., Meng X., Jung J., Zhao G., Yang R., Ahn J., Shi J.,
Concel J., Aiken C., Zhang P., Gronenborn A.M.;
"Structural convergence between Cryo-EM and NMR reveals intersubunit
interactions critical for HIV-1 capsid function.";
Cell 139:780-790(2009).
[19]
SUBUNIT (MATRIX PROTEIN P17).
PubMed=19327811; DOI=10.1016/j.virol.2009.02.048;
Alfadhli A., Barklis R.L., Barklis E.;
"HIV-1 matrix organizes as a hexamer of trimers on membranes
containing phosphatidylinositol-(4,5)-bisphosphate.";
Virology 387:466-472(2009).
[20]
FUNCTION (NUCLEOCAPSID PROTEIN P7), AND FUNCTION (GAG POLYPROTEIN).
PubMed=20828778; DOI=10.1016/j.virol.2010.08.013;
Jalalirad M., Laughrea M.;
"Formation of immature and mature genomic RNA dimers in wild-type and
protease-inactive HIV-1: differential roles of the Gag polyprotein,
nucleocapsid proteins NCp15, NCp9, NCp7, and the dimerization
initiation site.";
Virology 407:225-236(2010).
[21]
INTERACTION OF GAG POLYPROTEIN WITH PDZD8.
PubMed=20573829; DOI=10.1128/JVI.00843-10;
Henning M.S., Morham S.G., Goff S.P., Naghavi M.H.;
"PDZD8 is a novel Gag-interacting factor that promotes retroviral
infection.";
J. Virol. 84:8990-8995(2010).
[22]
INTERACTION OF MATRIX PROTEIN P17 WITH RAT CALM1.
PubMed=24500712; DOI=10.1074/jbc.M113.543694;
Vlach J., Samal A.B., Saad J.S.;
"Solution structure of calmodulin bound to the binding domain of the
HIV-1 matrix protein.";
J. Biol. Chem. 289:8697-8705(2014).
[23]
INTERACTION WITH MONKEY TRIM5 (CAPSID PROTEIN P24).
PubMed=23785198; DOI=10.1128/JVI.00713-13;
Shi J., Friedman D.B., Aiken C.;
"Retrovirus restriction by TRIM5 proteins requires recognition of only
a small fraction of viral capsid subunits.";
J. Virol. 87:9271-9278(2013).
[24]
INTERACTION OF CAPSID-NUCLEOCAPSID COMPLEX WITH HUMAN PDZD8, AND
FUNCTION (CAPSID PROTEIN P24).
PubMed=24554657; DOI=10.1128/JVI.02945-13;
Guth C.A., Sodroski J.;
"Contribution of PDZD8 to stabilization of the human immunodeficiency
virus type 1 capsid.";
J. Virol. 88:4612-4623(2014).
[25]
REVIEW.
PubMed=9878383; DOI=10.1006/jmbi.1998.2354;
Turner B.G., Summers M.F.;
"Structural biology of HIV.";
J. Mol. Biol. 285:1-32(1999).
[26]
REVIEW.
PubMed=12873766; DOI=10.1016/S0005-2736(03)00163-9;
Scarlata S., Carter C.;
"Role of HIV-1 Gag domains in viral assembly.";
Biochim. Biophys. Acta 1614:62-72(2003).
[27]
REVIEW.
PubMed=16815734; DOI=10.1016/j.mib.2006.06.011;
Sokolskaja E., Luban J.;
"Cyclophilin, TRIM5, and innate immunity to HIV-1.";
Curr. Opin. Microbiol. 9:404-408(2006).
[28]
REVIEW.
PubMed=21762797; DOI=10.1016/j.jmb.2011.04.015;
Chukkapalli V., Ono A.;
"Molecular determinants that regulate plasma membrane association of
HIV-1 Gag.";
J. Mol. Biol. 410:512-524(2011).
[29]
REVIEW.
PubMed=24907482; DOI=10.1016/j.virusres.2014.05.011;
Darlix J.L., de Rocquigny H., Mauffret O., Mely Y.;
"Retrospective on the all-in-one retroviral nucleocapsid protein.";
Virus Res. 193:2-15(2014).
[30]
REVIEW.
PubMed=24933691; DOI=10.1016/j.tim.2014.04.012;
Tedbury P.R., Freed E.O.;
"The role of matrix in HIV-1 envelope glycoprotein incorporation.";
Trends Microbiol. 22:372-378(2014).
-!- FUNCTION: Gag polyprotein: Mediates, with Gag-Pol polyprotein, the
essential events in virion assembly, including binding the plasma
membrane, making the protein-protein interactions necessary to
create spherical particles, recruiting the viral Env proteins, and
packaging the genomic RNA via direct interactions with the RNA
packaging sequence (Psi). {ECO:0000269|PubMed:20828778}.
-!- FUNCTION: Matrix protein p17: Targets the polyprotein to the
plasma membrane via a multipartite membrane-binding signal, that
includes its myristoylated N-terminus (By similarity). Matrix
protein is part of the pre-integration complex. Implicated in the
release from host cell mediated by Vpu. Binds to RNA (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12493}.
-!- FUNCTION: Capsid protein p24: Forms the conical core that
encapsulates the genomic RNA-nucleocapsid complex in the virion.
Most core are conical, with only 7% tubular. The core is
constituted by capsid protein hexamer subunits. The core is
disassembled soon after virion entry (PubMed:12660176). Host
restriction factors such as monkey TRIM5-alpha or TRIMCyp bind
retroviral capsids and cause premature capsid disassembly, leading
to blocks in reverse transcription. Capsid restriction by TRIM5 is
one of the factors which restricts HIV-1 to the human species
(PubMed:23785198). Host PIN1 apparently facilitates the virion
uncoating (By similarity). On the other hand, interactions with
PDZD8 or CYPA stabilize the capsid (PubMed:24554657).
{ECO:0000250|UniProtKB:P12493, ECO:0000269|PubMed:12660176,
ECO:0000269|PubMed:19914170, ECO:0000269|PubMed:23785198,
ECO:0000269|PubMed:24554657, ECO:0000269|PubMed:8648689}.
-!- FUNCTION: Nucleocapsid protein p7: Encapsulates and protects viral
dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its
zinc fingers. Acts as a nucleic acid chaperone which is involved
in rearangement of nucleic acid secondary structure during gRNA
retrotranscription. Also facilitates template switch leading to
recombination. As part of the polyprotein, participates in gRNA
dimerization, packaging, tRNA incorporation and virion assembly.
{ECO:0000269|PubMed:11044125, ECO:0000269|PubMed:11932404,
ECO:0000269|PubMed:17070549, ECO:0000269|PubMed:18343475,
ECO:0000269|PubMed:20828778, ECO:0000269|PubMed:9931246}.
-!- FUNCTION: p6-gag: Plays a role in budding of the assembled
particle by interacting with the host class E VPS proteins TSG101
and PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P12493}.
-!- SUBUNIT: Gag polyprotein: Homotrimer; further assembles as
hexamers of trimers (By similarity). Oligomerization possibly
creates a central hole into which the cytoplasmic tail of the gp41
envelope protein may be inserted.Gag polyprotein: Interacts with
host TRIM22; this interaction seems to disrupt proper trafficking
of Gag polyprotein and may interfere with budding
(PubMed:18389079). Gag polyprotein: Interacts with host PDZD8 (By
similarity). Matrix protein p17: Homotrimer; further assembles as
hexamers of trimers (PubMed:19327811). Matrix protein p17:
Interacts with gp41 (via C-terminus) (By similarity). Matrix
protein p17: Interacts with host CALM1; this interaction induces a
conformational change in the Matrix protein, triggering exposure
of the myristate group (PubMed:24500712). Matrix protein p17:
Interacts with host AP3D1; this interaction allows the polyprotein
trafficking to multivesicular bodies during virus assembly (By
similarity). Matrix protein p17: Part of the pre-integration
complex (PIC) which is composed of viral genome, matrix protein,
Vpr and integrase (By similarity). Capsid protein p24: Homodimer;
the homodimer further multimerizes as homohexamers or
homopentamers (PubMed:19914170). Capsid protein p24: Interacts
with human PPIA/CYPA;this interaction stabilizes the capsid
(PubMed:9223641). Capsid protein p24: Interacts with human NUP153
(By similarity). Capsid protein p24: Interacts with host PDZD8;
this interaction stabilizes the capsid (PubMed:20573829). Capsid
protein p24: Interacts with monkey TRIM5; this interaction
destabilizes the capsid (PubMed:23785198). p6-gag interacts with
Vpr; this interaction allows Vpr incorporation into the virion (By
similarity). p6-gag interacts with host TSG101 (By similarity).
p6-gag interacts with host PDCD6IP/AIP1 (By similarity).
{ECO:0000250|UniProtKB:P03347, ECO:0000250|UniProtKB:P03348,
ECO:0000250|UniProtKB:P12493, ECO:0000269|PubMed:18389079,
ECO:0000269|PubMed:19327811, ECO:0000269|PubMed:19914170,
ECO:0000269|PubMed:20573829, ECO:0000269|PubMed:23785198,
ECO:0000269|PubMed:24500712, ECO:0000269|PubMed:9223641}.
-!- INTERACTION:
Q12904:AIMP1 (xeno); NbExp=3; IntAct=EBI-6179719, EBI-1045802;
Q13155:AIMP2 (xeno); NbExp=3; IntAct=EBI-6179719, EBI-745226;
P80318:Cct3 (xeno); NbExp=3; IntAct=EBI-10634977, EBI-772361;
Q9UI47:CTNNA3 (xeno); NbExp=2; IntAct=EBI-6179727, EBI-3937546;
O43324:EEF1E1 (xeno); NbExp=4; IntAct=EBI-6179719, EBI-1048486;
Q8N1G4:LRRC47 (xeno); NbExp=2; IntAct=EBI-6179727, EBI-2509921;
Q9Y3B7:MRPL11 (xeno); NbExp=3; IntAct=EBI-6179727, EBI-5453723;
Q14978:NOLC1 (xeno); NbExp=2; IntAct=EBI-6179719, EBI-396155;
Q9NTK5:OLA1 (xeno); NbExp=4; IntAct=EBI-6179719, EBI-766468;
Q99873:PRMT1 (xeno); NbExp=2; IntAct=EBI-6179727, EBI-78738;
Q86SQ7:SDCCAG8 (xeno); NbExp=2; IntAct=EBI-6179719, EBI-1047850;
Q9HD40:SEPSECS (xeno); NbExp=3; IntAct=EBI-6163428, EBI-6163446;
P55769:SNU13 (xeno); NbExp=2; IntAct=EBI-6179727, EBI-712228;
O95793-2:STAU1 (xeno); NbExp=4; IntAct=EBI-6163428, EBI-358189;
Q99816-1:TSG101 (xeno); NbExp=3; IntAct=EBI-10634977, EBI-15891993;
Q7Z739:YTHDF3 (xeno); NbExp=2; IntAct=EBI-6179727, EBI-2849837;
-!- SUBCELLULAR LOCATION: Gag polyprotein: Host cell membrane; Lipid-
anchor. Host endosome, host multivesicular body
{ECO:0000250|UniProtKB:P12493}. Note=These locations are probably
linked to virus assembly sites. The main location is the cell
membrane, but under some circumstances, late endosomal
compartments can serve as productive sites for virion assembly.
{ECO:0000250|UniProtKB:P12493}.
-!- SUBCELLULAR LOCATION: Matrix protein p17: Virion membrane; Lipid-
anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p7: Virion
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=Translation results in the formation of the Gag
polyprotein most of the time. Ribosomal frameshifting at the
gag-pol genes boundary occurs at low frequency and produces the
Gag-Pol polyprotein. This strategy of translation probably
allows the virus to modulate the quantity of each viral protein.
Maintenance of a correct Gag to Gag-Pol ratio is essential for
RNA dimerization and viral infectivity.;
Name=Gag polyprotein;
IsoId=P04591-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Gag-Pol polyprotein;
IsoId=P04585-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting.;
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle budding. They recruit proteins of the
host ESCRT machinery (Endosomal Sorting Complex Required for
Transport) or ESCRT-associated proteins. p6-gag contains two L
domains: a PTAP/PSAP motif, which interacts with the UEV domain of
TSG101 and a LYPX(n)L motif which interacts with PDCD6IP/AIP1.
{ECO:0000250|UniProtKB:P12493}.
-!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the
viral protease yield mature proteins.
{ECO:0000250|UniProtKB:P12493}.
-!- PTM: Matrix protein p17: Tyrosine phosphorylated presumably in the
virion by a host kinase. Phosphorylation is apparently not a major
regulator of membrane association (PubMed:17656588).
{ECO:0000269|PubMed:17656588}.
-!- PTM: Capsid protein p24: Phosphorylated possibly by host MAPK1;
this phosphorylation is necessary for Pin1-mediated virion
uncoating. {ECO:0000250|UniProtKB:P12493}.
-!- PTM: Nucleocapsid protein p7: Methylated by host PRMT6, impairing
its function by reducing RNA annealing and the initiation of
reverse transcription. {ECO:0000250|UniProtKB:P03347}.
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
(for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
The vast majority of strains found worldwide belong to the group
M. Group O seems to be endemic to and largely confined to Cameroon
and neighboring countries in West Central Africa, where these
viruses represent a small minority of HIV-1 strains. The group N
is represented by a limited number of isolates from Cameroonian
persons. The group M is further subdivided in 9 clades or subtypes
(A to D, F to H, J and K).
-!- SIMILARITY: Belongs to the primate lentivirus group gag
polyprotein family. {ECO:0000305}.
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=Gag
entry;
URL="http://www.bioafrica.net/proteomics/GAGprot.html";
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=MA
(p17) entry;
URL="http://www.bioafrica.net/proteomics/GAG-MAprot.html";
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=CA
(p24) entry;
URL="http://www.bioafrica.net/proteomics/GAG-CAprot.html";
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=p2
entry;
URL="http://www.bioafrica.net/proteomics/GAG-p2prot.html";
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=NC (p7)
entry;
URL="http://www.bioafrica.net/proteomics/GAG-NCprot.html";
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=p1
entry;
URL="http://www.bioafrica.net/proteomics/GAG-p1prot.html";
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=p6
entry;
URL="http://www.bioafrica.net/proteomics/GAG-p6prot.html";
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EMBL; K03455; AAB50258.1; -; Genomic_RNA.
RefSeq; NP_057850.1; NC_001802.1.
PDB; 1TSQ; X-ray; 2.00 A; P=429-438.
PDB; 1TSU; X-ray; 2.10 A; P=429-436.
PDB; 5FJB; EM; 9.00 A; A/B=133-350.
PDB; 5I1R; Other; -; A=378-432.
PDB; 5INC; X-ray; 2.88 A; E/F=308-316.
PDB; 5IND; X-ray; 2.13 A; E/F=308-316.
PDBsum; 1TSQ; -.
PDBsum; 1TSU; -.
PDBsum; 5FJB; -.
PDBsum; 5I1R; -.
PDBsum; 5INC; -.
PDBsum; 5IND; -.
ProteinModelPortal; P04591; -.
SMR; P04591; -.
BioGrid; 1205537; 188.
ELM; P04591; -.
IntAct; P04591; 48.
GeneID; 155030; -.
KEGG; vg:155030; -.
OrthoDB; VOG09000135; -.
Reactome; R-HSA-162585; Uncoating of the HIV Virion.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-162592; Integration of provirus.
Reactome; R-HSA-162594; Early Phase of HIV Life Cycle.
Reactome; R-HSA-164516; Minus-strand DNA synthesis.
Reactome; R-HSA-164525; Plus-strand DNA synthesis.
Reactome; R-HSA-164843; 2-LTR circle formation.
Reactome; R-HSA-173107; Binding and entry of HIV virion.
Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
Reactome; R-HSA-174495; Synthesis And Processing Of GAG, GAGPOL Polyproteins.
Reactome; R-HSA-175474; Assembly Of The HIV Virion.
Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
EvolutionaryTrace; P04591; -.
PRO; PR:P04591; -.
Proteomes; UP000002241; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030260; P:entry into host cell; TAS:Reactome.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0051169; P:nuclear transport; TAS:Reactome.
GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; TAS:Reactome.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0019082; P:viral protein processing; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 4.10.60.10; -; 3.
InterPro; IPR000721; Gag_p24.
InterPro; IPR014817; Gag_p6.
InterPro; IPR000071; Lentvrl_matrix_N.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00540; Gag_p17; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF08705; Gag_p6; 1.
Pfam; PF00098; zf-CCHC; 2.
PRINTS; PR00234; HIV1MATRIX.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 2.
1: Evidence at protein level;
3D-structure; AIDS; Capsid protein; Complete proteome;
Host cell membrane; Host cytoplasm; Host endosome; Host membrane;
Host nucleus; Host-virus interaction; Lipoprotein; Membrane;
Metal-binding; Methylation; Myristate; Phosphoprotein;
Reference proteome; Repeat; Ribosomal frameshifting; RNA-binding;
Viral budding; Viral budding via the host ESCRT complexes;
Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 500 Gag polyprotein.
/FTId=PRO_0000261216.
CHAIN 2 132 Matrix protein p17. {ECO:0000250}.
/FTId=PRO_0000038593.
CHAIN 133 363 Capsid protein p24. {ECO:0000250}.
/FTId=PRO_0000038594.
PEPTIDE 364 377 Spacer peptide 1. {ECO:0000250}.
/FTId=PRO_0000038595.
CHAIN 378 432 Nucleocapsid protein p7. {ECO:0000250}.
/FTId=PRO_0000038596.
PEPTIDE 433 448 Spacer peptide 2. {ECO:0000250}.
/FTId=PRO_0000038597.
CHAIN 449 500 p6-gag. {ECO:0000250}.
/FTId=PRO_0000038598.
ZN_FING 390 407 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 411 428 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 7 31 Interaction with Gp41.
{ECO:0000250|UniProtKB:P12493}.
REGION 8 43 Interaction with host CALM1.
{ECO:0000269|PubMed:24500712}.
REGION 12 19 Interaction with host AP3D1.
{ECO:0000250|UniProtKB:P12497}.
REGION 14 33 Interaction with membrane
phosphatidylinositol 4,5-bisphosphate and
RNA. {ECO:0000250|UniProtKB:P12493}.
REGION 73 77 Interaction with membrane
phosphatidylinositol 4,5-bisphosphate.
{ECO:0000250|UniProtKB:P12493}.
REGION 189 227 Interaction with host PPIA/CYPA and
NUP153. {ECO:0000250|UniProtKB:P12493}.
REGION 217 225 PPIA/CYPA-binding loop.
REGION 277 363 Dimerization/Multimerization of capsid
protein p24.
MOTIF 16 22 Nuclear export signal.
MOTIF 26 32 Nuclear localization signal.
MOTIF 455 458 PTAP/PSAP motif.
MOTIF 483 492 LYPX(n)L motif.
SITE 132 133 Cleavage; by viral protease.
{ECO:0000250}.
SITE 363 364 Cleavage; by viral protease.
{ECO:0000250}.
SITE 377 378 Cleavage; by viral protease.
{ECO:0000250}.
SITE 432 433 Cleavage; by viral protease.
{ECO:0000250}.
SITE 448 449 Cleavage; by viral protease.
{ECO:0000250}.
MOD_RES 148 148 Phosphoserine; by host MAPK1.
{ECO:0000250|UniProtKB:P12493}.
MOD_RES 387 387 Asymmetric dimethylarginine; in
Nucleocapsid protein p7; by host PRMT6.
{ECO:0000250}.
MOD_RES 409 409 Asymmetric dimethylarginine; in
Nucleocapsid protein p7; by host PRMT6.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
MUTAGEN 6 6 S->D: No influence on the PIP2- or
concentration-dependent myristyl switch
mechanism. {ECO:0000269|PubMed:17656588}.
MUTAGEN 9 9 S->D: No influence on the PIP2- or
concentration-dependent myristyl switch
mechanism. {ECO:0000269|PubMed:17656588}.
MUTAGEN 18 18 K->A: Replication-defective, induces
nuclear mislocalization of matrix
protein; when associated with G-22.
{ECO:0000269|PubMed:10604476}.
MUTAGEN 22 22 R->G: Replication-defective, induces
nuclear mislocalization of matrix
protein; when associated with A-18.
{ECO:0000269|PubMed:10604476}.
MUTAGEN 27 27 K->A: No effect on subcellular
localization of matrix protein; when
associated with A-18 and G-22.
{ECO:0000269|PubMed:10604476}.
MUTAGEN 67 67 S->D: No influence on the PIP2- or
concentration-dependent myristyl switch
mechanism. {ECO:0000269|PubMed:17656588}.
MUTAGEN 72 72 S->D: No influence on the PIP2- or
concentration-dependent myristyl switch
mechanism. {ECO:0000269|PubMed:17656588}.
MUTAGEN 217 217 P->A: 3-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 218 218 V->A: 2.7-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 219 219 H->A,Q: 8-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 220 220 A->G: 44-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 220 220 A->V: 3.4-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 221 221 G->A: 31-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 221 221 G->V: 154-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 222 222 P->A: 36-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 222 222 P->V: More than 150-fold decrease of
PPIA-binding affinity.
{ECO:0000269|PubMed:9223641}.
MUTAGEN 223 223 I->A: 1.2-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 223 223 I->V: 1.0-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 224 224 A->G: 2.3-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 224 224 A->V: 1.7-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 225 225 P->A: 1.6-fold decrease of PPIA-binding
affinity. {ECO:0000269|PubMed:9223641}.
MUTAGEN 394 394 N->F,G: Decreases infectivity and
replication.
{ECO:0000269|PubMed:16904152}.
MUTAGEN 400 400 H->C: Complete loss of infectivity and in
vitro chaperone activity.
{ECO:0000269|PubMed:11932404}.
MUTAGEN 405 405 C->H: Complete loss of infectivity and
DNA synthesis.
{ECO:0000269|PubMed:11932404}.
MUTAGEN 421 421 H->C: Partial loss of infectivity.
Complete loss of in vitro chaperone
activity. {ECO:0000269|PubMed:11932404}.
MUTAGEN 426 426 C->H: Partial loss of infectivity.
{ECO:0000269|PubMed:11932404}.
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


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