GAG_HV1W2
ID GAG_HV1W2 Reviewed; 389 AA.
AC P05889;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 140.
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 {ECO:0000250|UniProtKB:P12493};
DE Short=NC;
DE Flags: Fragment;
GN Name=gag;
OS Human immunodeficiency virus type 1 group M subtype B (isolate WMJ22)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11705;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3012778; DOI=10.1126/science.3012778;
RA Hahn B.H., Shaw G.M., Taylor M.E., Redfield R.R., Markham P.D.,
RA Salahuddin S.Z., Wong-Staal F., Gallo R.C., Parks E.S., Parks W.P.;
RT "Genetic variation in HTLV-III/LAV over time in patients with AIDS or at
RT risk for AIDS.";
RL Science 232:1548-1553(1986).
RN [2]
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).
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 (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. 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 (By similarity). On the
CC other hand, interactions with PDZD8 or CYPA stabilize the capsid (By
CC similarity). {ECO:0000250|UniProtKB:P04591,
CC ECO:0000250|UniProtKB:P12493}.
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 by
CC interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1.
CC {ECO:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: Gag polyprotein: Homotrimer; further assembles as hexamers of
CC trimers. Oligomerization possibly creates a central hole into which the
CC cytoplasmic tail of the gp41 envelope protein may be inserted.Gag
CC polyprotein: Interacts with host TRIM22; this interaction seems to
CC disrupt proper trafficking of Gag polyprotein and may interfere with
CC budding. Gag polyprotein: Interacts with host PDZD8. Matrix protein
CC p17: Homotrimer; further assembles as hexamers of trimers. Matrix
CC protein p17: Interacts with gp41 (via C-terminus). Matrix protein p17:
CC Interacts with host CALM1; this interaction induces a conformational
CC change in the Matrix protein, triggering exposure of the myristate
CC group. Matrix protein p17: Interacts with host AP3D1; this interaction
CC allows the polyprotein trafficking to multivesicular bodies during
CC virus assembly. Matrix protein p17: Part of the pre-integration complex
CC (PIC) which is composed of viral genome, matrix protein, Vpr and
CC integrase. Capsid protein p24: Homodimer; the homodimer further
CC multimerizes as homohexamers or homopentamers. Capsid protein p24:
CC Interacts with human PPIA/CYPA. Capsid protein p24: Interacts with
CC human NUP153. Capsid protein p24: Interacts with host PDZD8; this
CC interaction stabilizes the capsid. Capsid protein p24: Interacts with
CC monkey TRIM5; this interaction destabilizes the capsid. p6-gag
CC interacts with Vpr; this interaction allows Vpr incorporation into the
CC virion. p6-gag interacts with host TSG101. p6-gag interacts with host
CC PDCD6IP/AIP1. Gag polyprotein: When ubiquitinated, interacts (via p6-
CC gag domain) with host PACSIN2; this interaction allows PACSIN2
CC recruitment to viral assembly sites and its subsequent incorporation
CC into virions (By similarity). {ECO:0000250|UniProtKB:P03347,
CC ECO:0000250|UniProtKB:P03348, ECO:0000250|UniProtKB:P03349,
CC ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: [Capsid protein p24]: Homodimer; the homodimer further
CC multimerizes as homohexamers or homopentamers (By similarity).
CC Interacts with host NUP98 (By similarity). Interacts with host
CC PPIA/CYPA; this interaction stabilizes the capsid (By similarity).
CC Interacts with host NUP153 (By similarity). Interacts with host PDZD8;
CC this interaction stabilizes the capsid. Interacts with host TRIM5; this
CC interaction destabilizes the capsid (By similarity). Interacts with
CC host CPSF6 (By similarity). Interacts with host NONO; the interaction
CC is weak (By similarity). {ECO:0000250|UniProtKB:P04591,
CC ECO:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: [Nucleocapsid protein p7]: Interacts with host NUP98.
CC {ECO:0000250|UniProtKB:P12493}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane
CC {ECO:0000250|UniProtKB:P12493}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P12493}. 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
CC {ECO:0000250|UniProtKB:P12493}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host
CC cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion
CC {ECO:0000250|UniProtKB:P12493}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion
CC {ECO:0000250|UniProtKB:P12493}.
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=P05889-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P05889-2; Sequence=Not described;
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: [Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages by the
CC viral 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. {ECO:0000250|UniProtKB:P04591}.
CC -!- PTM: Capsid protein p24 is 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 is 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: Isolates WMJ1, WMJ2, and WMJ3 were obtained from blood
CC samples sequentially taken from a two-year old Haitian who was
CC perinatally infected by her mother.
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 -!- MISCELLANEOUS: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal
CC frameshifting. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the primate lentivirus group gag polyprotein
CC family. {ECO:0000305}.
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DR EMBL; K03457; AAB12988.1; -; Genomic_RNA.
DR PDB; 1FGL; X-ray; 1.80 A; B=213-237.
DR PDBsum; 1FGL; -.
DR SMR; P05889; -.
DR EvolutionaryTrace; P05889; -.
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:0016032; P:viral process; IEA:InterPro.
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; 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 Pfam; PF00540; Gag_p17; 1.
DR Pfam; PF00607; Gag_p24; 1.
DR Pfam; PF19317; Gag_p24_C; 1.
DR PRINTS; PR00234; HIV1MATRIX.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; Capsid protein; Host cell membrane; Host cytoplasm;
KW Host endosome; Host membrane; Host nucleus; Lipoprotein; Membrane;
KW Methylation; Myristate; Phosphoprotein; Ribosomal frameshifting;
KW RNA-binding; Viral nucleoprotein; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..>389
FT /note="Gag polyprotein"
FT /id="PRO_0000261235"
FT CHAIN 2..132
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038589"
FT CHAIN 133..363
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038590"
FT PEPTIDE 364..377
FT /note="Spacer peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038591"
FT CHAIN 378..>389
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038592"
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:0000250|UniProtKB:P04591"
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 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 /evidence="ECO:0000250|UniProtKB:P04591"
FT REGION 277..363
FT /note="Dimerization/Multimerization of capsid protein p24"
FT /evidence="ECO:0000250|UniProtKB:P04591"
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 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 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 LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT NON_TER 389
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:1FGL"
SQ SEQUENCE 389 AA; 43446 MW; F965F184AD63ECCD CRC64;
MGARASVLSG GELDKWEKIR LRPGGKKKYR LKHIVWASRE LERFAVNPGL LETSEGCRQI
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEKKDTKEA LDKIEEEQNK CKKKAQQAAA
DTGNSSQVSQ NYPIVQNLQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRLHPVHA GPIAPGQMRE PRGSDIAGTT
STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF
YKTLRAEQAT QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA
RVLAEAMSQV TNPTTIMMQK GNFRNQRKT
