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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_HV1VI               Reviewed;         491 AA.
Q9QSR4;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 92.
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 F1 (isolate VI850)
(HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=388813;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10725202; DOI=10.1006/viro.2000.0214;
Laukkanen T., Carr J.K., Janssens W., Liitsola K., Gotte D.,
McCutchan F.E., Op de Coul E., Cornelissen M., Heyndrickx L.,
van der Groen G., Salminen M.O.;
"Virtually full-length subtype F and F/D recombinant HIV-1 from Africa
and South America.";
Virology 269:95-104(2000).
-!- 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:0000250|UniProtKB:P04591}.
-!- 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 (By similarity). Host
restriction factors such as 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. Host PIN1
apparently facilitates the virion uncoating (By similarity). On
the other hand, interactions with PDZD8 or CYPA stabilize the
capsid (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.
-!- 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:0000250|UniProtKB:P04591}.
-!- 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. 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. Gag polyprotein: Interacts with
host PDZD8. Matrix protein p17: Homotrimer; further assembles as
hexamers of trimers. Matrix protein p17: Interacts with gp41 (via
C-terminus). Matrix protein p17: Interacts with host CALM1; this
interaction induces a conformational change in the Matrix protein,
triggering exposure of the myristate group. Matrix protein p17:
Interacts with host AP3D1; this interaction allows the polyprotein
trafficking to multivesicular bodies during virus assembly. Matrix
protein p17: Part of the pre-integration complex (PIC) which is
composed of viral genome, matrix protein, Vpr and integrase.
Capsid protein p24: Homodimer; the homodimer further multimerizes
as homohexamers or homopentamers. Capsid protein p24: Interacts
with human PPIA/CYPA. Capsid protein p24: Interacts with human
NUP153. Capsid protein p24: Interacts with host PDZD8; this
interaction stabilizes the capsid. Capsid protein p24: Interacts
with monkey TRIM5; this interaction destabilizes the capsid. p6-
gag interacts with Vpr; this interaction allows Vpr incorporation
into the virion. p6-gag interacts with host TSG101. p6-gag
interacts with host PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P03347,
ECO:0000250|UniProtKB:P03348, ECO:0000250|UniProtKB:P04591,
ECO:0000250|UniProtKB:P12493}.
-!- SUBCELLULAR LOCATION: Gag polyprotein: Host cell membrane
{ECO:0000250|UniProtKB:P12493}; Lipid-anchor
{ECO:0000250|UniProtKB:P12493}. 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
{ECO:0000250|UniProtKB:P12493}; Lipid-anchor
{ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host
cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion
{ECO:0000250|UniProtKB:P12493}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p7: Virion
{ECO:0000250|UniProtKB:P12493}.
-!- 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=Q9QSR4-1; Sequence=Displayed;
Note=Produced by conventional translation.;
Name=Gag-Pol polyprotein;
IsoId=Q9QSR3-1; 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. {ECO:0000250|UniProtKB:P04591}.
-!- PTM: Capsid protein p24 is phosphorylated possibly by host MAPK1;
this phosphorylation is necessary for Pin1-mediated virion
uncoating. {ECO:0000250|UniProtKB:P12493}.
-!- PTM: Nucleocapsid protein p7 is 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}.
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EMBL; AF077336; AAD46087.1; -; Genomic_DNA.
ProteinModelPortal; Q9QSR4; -.
SMR; Q9QSR4; -.
OrthoDB; VOG09000135; -.
PRO; PR:Q9QSR4; -.
Proteomes; UP000007418; Genome.
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: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:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.150.90; -; 1.
Gene3D; 1.10.375.10; -; 1.
InterPro; IPR000721; Gag_p24.
InterPro; IPR014817; Gag_p6.
InterPro; IPR000071; Lentvrl_matrix_N.
InterPro; IPR012344; Matrix_HIV/RSV_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; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 2.
3: Inferred from homology;
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 2 491 Gag polyprotein.
/FTId=PRO_0000261233.
CHAIN 2 128 Matrix protein p17. {ECO:0000250}.
/FTId=PRO_0000246410.
CHAIN 129 359 Capsid protein p24. {ECO:0000250}.
/FTId=PRO_0000246411.
PEPTIDE 360 371 Spacer peptide 1. {ECO:0000250}.
/FTId=PRO_0000246412.
CHAIN 372 426 Nucleocapsid protein p7. {ECO:0000250}.
/FTId=PRO_0000246413.
PEPTIDE 427 442 Spacer peptide 2. {ECO:0000250}.
/FTId=PRO_0000246414.
CHAIN 443 491 p6-gag. {ECO:0000250}.
/FTId=PRO_0000246415.
ZN_FING 384 401 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 405 422 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:0000250|UniProtKB:P04591}.
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 185 223 Interaction with host PPIA/CYPA and
NUP153. {ECO:0000250|UniProtKB:P12493}.
REGION 213 221 PPIA/CYPA-binding loop.
{ECO:0000250|UniProtKB:P04591}.
REGION 273 359 Dimerization/Multimerization of capsid
protein p24.
{ECO:0000250|UniProtKB:P04591}.
MOTIF 16 22 Nuclear export signal. {ECO:0000250}.
MOTIF 26 32 Nuclear localization signal.
{ECO:0000250}.
MOTIF 449 452 PTAP/PSAP motif.
MOTIF 476 486 LYPX(n)L motif.
SITE 128 129 Cleavage; by viral protease.
{ECO:0000250}.
SITE 359 360 Cleavage; by viral protease.
{ECO:0000250}.
SITE 371 372 Cleavage; by viral protease.
{ECO:0000250}.
SITE 426 427 Cleavage; by viral protease.
{ECO:0000250}.
SITE 442 443 Cleavage; by viral protease.
{ECO:0000250}.
MOD_RES 144 144 Phosphoserine; by host MAPK1.
{ECO:0000250|UniProtKB:P12493}.
MOD_RES 381 381 Asymmetric dimethylarginine; in
Nucleocapsid protein p7; by host PRMT6.
{ECO:0000250}.
MOD_RES 403 403 Asymmetric dimethylarginine; in
Nucleocapsid protein p7; by host PRMT6.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
SEQUENCE 491 AA; 54649 MW; BCCF6102798E6994 CRC64;
MGARASILSG GKLDEWEKIQ LRPGGKKRYK MKHLIWASRE LERFALDPGL LETSEGCQKI
IRQLQPSLQT GSEELKSLFN TVAVLYYVHQ RAGVTDTKEA LDKLEEEQNK SQQKTQQAAA
DKGVSQNYPI VQNLQGQMVH QSLSPRTLNA WVKVIEEKAF SPEVIPMFSA LSEGATPTDL
NTMLNTVGGH QAAMQMLKDT INEEAAEWDR LHPVHAGPAP PGQMREPRGS DIAGTTSTLQ
EQIQWMTGNP PVPVGDIYKR WIILGLNKIV RMYSPVSILD IKQGPKEPFR DYVDRFFKVL
RAEQASQDVK GWMTDTLLVQ NANPDCKTIL KALGTGATLE EMMTACQGVG GPSHKARVLA
EAMSQANSAI MMQKSNFKGQ RRVVKCFNCG KEGHIARNCR APRKKGCWKC GREGHQMKDC
TERQANFLGK IWPSNKGRPG NFLQSRPEPT APPAESFGFR EEITPSPKQE QKDGELYPPL
ASLKSLFGND P


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