GAG_HV2RO
ID GAG_HV2RO Reviewed; 522 AA.
AC P04590;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 148.
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 2 subtype A (isolate ROD) (HIV-2).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11720;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3031510; DOI=10.1038/326662a0;
RA Guyader M., Emerman M., Sonigo P., Clavel F., Montagnier L., Alizon M.;
RT "Genome organization and transactivation of the human immunodeficiency
RT virus type 2.";
RL Nature 326:662-669(1987).
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 (By
CC similarity). Most core are conical, with only 7% tubular (By
CC similarity). The core is constituted by capsid protein hexamer subunits
CC (By similarity). The core is disassembled soon after virion entry (By
CC similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp
CC bind retroviral capsids and cause premature capsid disassembly, leading
CC to blocks in reverse transcription (By similarity). Capsid restriction
CC by TRIM5 is one of the factors which restricts HIV-1 to the human
CC species (By similarity). Host PIN1 apparently facilitates the virion
CC uncoating (By similarity). On the other hand, interactions with PDZD8
CC or CYPA stabilize the capsid (By similarity). The capsid interacts with
CC high affinity with human NONO, promoting detection of viral DNA by
CC CGAS, leading to CGAS-mediated inmmune activation (By similarity).
CC {ECO:0000250|UniProtKB:P04591, ECO:0000250|UniProtKB:P12493,
CC ECO:0000250|UniProtKB:P18095}.
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:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: [Gag polyprotein]: Homotrimer; further assembles as hexamers
CC of trimers. Oligomerization possibly creates a central hole into which
CC the cytoplasmic tail of the gp41 envelope protein may be inserted.
CC Interacts with host TRIM22; this interaction seems to disrupt proper
CC trafficking of Gag polyprotein and may interfere with budding.
CC Interacts with host PDZD8. When ubiquitinated, interacts (via p6-gag
CC domain) with host PACSIN2; this interaction allows PACSIN2 recruitment
CC to viral assembly sites and its subsequent incorporation into virions
CC (By similarity). {ECO:0000250|UniProtKB:P03349,
CC ECO:0000250|UniProtKB:P04591}.
CC -!- SUBUNIT: [Matrix protein p17]: Homotrimer; further assembles as
CC hexamers of trimers. Interacts with gp41 (via C-terminus). Interacts
CC with host CALM1; this interaction induces a conformational change in
CC the Matrix protein, triggering exposure of the myristate group.
CC Interacts with host AP3D1; this interaction allows the polyprotein
CC trafficking to multivesicular bodies during virus assembly. Part of the
CC pre-integration complex (PIC) which is composed of viral genome, matrix
CC protein, Vpr and integrase. {ECO:0000250|UniProtKB:P04591,
CC 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 the interaction is strong and promotes CGAS-mediated immunity (By
CC similarity). {ECO:0000250|UniProtKB:P04591,
CC ECO:0000250|UniProtKB:P12493, ECO:0000250|UniProtKB:P18095}.
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. Interacts with host TSG101. p6-gag
CC interacts with host PDCD6IP/AIP1. {ECO:0000250|UniProtKB:P03348,
CC ECO:0000250|UniProtKB:P12493}.
CC -!- INTERACTION:
CC P04590; Q13523: PRPF4B; Xeno; NbExp=6; IntAct=EBI-780156, EBI-395940;
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=P04590-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P04584-1; 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 one L domains: a PTAP/PSAP
CC motif, which interacts with the UEV domain of TSG101 (By similarity).
CC {ECO:0000250}.
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. {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: [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; M15390; AAB00763.1; -; Genomic_DNA.
DR EMBL; X05291; CAA28909.1; -; Genomic_RNA.
DR PIR; A26262; FOLJG2.
DR PDB; 2WLV; X-ray; 1.25 A; A/B=136-279.
DR PDB; 4DGB; X-ray; 1.70 A; B=221-226.
DR PDBsum; 2WLV; -.
DR PDBsum; 4DGB; -.
DR BMRB; P04590; -.
DR SMR; P04590; -.
DR IntAct; P04590; 4.
DR EvolutionaryTrace; P04590; -.
DR PRO; PR:P04590; -.
DR Proteomes; UP000007426; Genome.
DR Proteomes; UP000246871; Genome.
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; 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; 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; Myristate; Phosphoprotein;
KW Reference proteome; 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..522
FT /note="Gag polyprotein"
FT /id="PRO_0000261248"
FT CHAIN 2..135
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038615"
FT CHAIN 136..365
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038616"
FT PEPTIDE 366..382
FT /note="Spacer peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042091"
FT CHAIN 383..431
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042092"
FT PEPTIDE 432..445
FT /note="Spacer peptide 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042093"
FT CHAIN 446..522
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042094"
FT ZN_FING 389..406
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 410..427
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: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 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..228
FT /note="Interaction with host PPIA/CYPA and NUP153"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT REGION 219..226
FT /note="PPIA/CYPA-binding loop"
FT /evidence="ECO:0000250|UniProtKB:P04591"
FT REGION 279..365
FT /note="Dimerization/Multimerization of capsid protein p24"
FT /evidence="ECO:0000250|UniProtKB:P04591"
FT REGION 473..522
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 456..459
FT /note="PTAP/PSAP motif"
FT COMPBIAS 115..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 135..136
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 365..366
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 382..383
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 431..432
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 445..446
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT MOD_RES 150
FT /note="Phosphoserine; by host MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:2WLV"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2WLV"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:2WLV"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:2WLV"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2WLV"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:2WLV"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:2WLV"
FT HELIX 197..216
FT /evidence="ECO:0007829|PDB:2WLV"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:2WLV"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:2WLV"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:2WLV"
FT HELIX 260..278
FT /evidence="ECO:0007829|PDB:2WLV"
SQ SEQUENCE 522 AA; 58374 MW; DC1FBA5280B577D9 CRC64;
MGARNSVLRG KKADELERIR LRPGGKKKYR LKHIVWAANK LDRFGLAESL LESKEGCQKI
LTVLDPMVPT GSENLKSLFN TVCVIWCIHA EEKVKDTEGA KQIVRRHLVA ETGTAEKMPS
TSRPTAPSSE KGGNYPVQHV GGNYTHIPLS PRTLNAWVKL VEEKKFGAEV VPGFQALSEG
CTPYDINQML NCVGDHQAAM QIIREIINEE AAEWDVQHPI PGPLPAGQLR EPRGSDIAGT
TSTVEEQIQW MFRPQNPVPV GNIYRRWIQI GLQKCVRMYN PTNILDIKQG PKEPFQSYVD
RFYKSLRAEQ TDPAVKNWMT QTLLVQNANP DCKLVLKGLG MNPTLEEMLT ACQGVGGPGQ
KARLMAEALK EVIGPAPIPF AAAQQRKAFK CWNCGKEGHS ARQCRAPRRQ GCWKCGKPGH
IMTNCPDRQA GFLGLGPWGK KPRNFPVAQV PQGLTPTAPP VDPAVDLLEK YMQQGKRQRE
QRERPYKEVT EDLLHLEQGE TPYREPPTED LLHLNSLFGK DQ
