GAG_HV1MN
ID GAG_HV1MN Reviewed; 507 AA.
AC P05888;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
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 1 group M subtype B (isolate MN) (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11696;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3369091; DOI=10.1016/0042-6822(88)90568-5;
RA Gurgo C., Guo H.-G., Franchini G., Aldovini A., Collalti E., Farrell K.,
RA Wong-Staal F., Gallo R.C., Reitz M.S. Jr.;
RT "Envelope sequences of two new United States HIV-1 isolates.";
RL Virology 164:531-536(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-507, MYRISTOYLATION AT GLY-2, AND PROTEOLYTIC
RP PROCESSING OF POLYPROTEIN.
RX PubMed=1548743; DOI=10.1128/jvi.66.4.1856-1865.1992;
RA Henderson L.E., Bowers M.A., Sowder R.C. II, Serabyn S.A., Johnson D.G.,
RA Bess J.W. Jr., Arthur L.O., Bryant D.K., Fenselau C.;
RT "Gag proteins of the highly replicative MN strain of human immunodeficiency
RT virus type 1: posttranslational modifications, proteolytic processings, and
RT complete amino acid sequences.";
RL J. Virol. 66:1856-1865(1992).
RN [3]
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 [4]
RP STRUCTURE BY NMR OF 381-435.
RX PubMed=1304355; DOI=10.1002/pro.5560010502;
RA Summers M.F., Henderson L.E., Chance M.R., Bess J.W. Jr., South T.L.,
RA Blake P.R., Sagi I., Perez-Alvarado G., Sowder R.C. III, Hare D.R.,
RA Arthur L.O.;
RT "Nucleocapsid zinc fingers detected in retroviruses: EXAFS studies of
RT intact viruses and the solution-state structure of the nucleocapsid protein
RT from HIV-1.";
RL Protein Sci. 1:563-574(1992).
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.
CC {ECO:0000250|UniProtKB:P04591, 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
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 Interacts with MOV10 (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 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 -!- 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 -!- 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=P05888-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P05961-1; 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.
CC {ECO:0000250|UniProtKB:P12493}.
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]: 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]: 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 MN isolate was taken from a pediatric AIDS patient
CC in 1984.
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; M17449; AAA44853.1; -; Genomic_RNA.
DR PIR; A38068; A38068.
DR PDB; 1AAF; NMR; -; A=381-435.
DR PDBsum; 1AAF; -.
DR SMR; P05888; -.
DR IntAct; P05888; 4.
DR MINT; P05888; -.
DR BindingDB; P05888; -.
DR iPTMnet; P05888; -.
DR EvolutionaryTrace; P05888; -.
DR PRO; PR:P05888; -.
DR Proteomes; UP000007697; 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:0043565; F:sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
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; Direct protein sequencing;
KW Host cell membrane; Host cytoplasm; Host endosome; Host membrane;
KW Host nucleus; Host-virus interaction; Lipoprotein; Membrane; Metal-binding;
KW Methylation; Myristate; Phosphoprotein; Reference proteome; Repeat;
KW Ribosomal frameshifting; RNA-binding; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral nucleoprotein;
KW Viral release from host cell; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:1548743"
FT CHAIN 2..507
FT /note="Gag polyprotein"
FT /id="PRO_0000261221"
FT CHAIN 2..135
FT /note="Matrix protein p17"
FT /id="PRO_0000038547"
FT CHAIN 136..366
FT /note="Capsid protein p24"
FT /id="PRO_0000038548"
FT PEPTIDE 367..380
FT /note="Spacer peptide 1"
FT /id="PRO_0000038549"
FT CHAIN 381..435
FT /note="Nucleocapsid protein p7"
FT /id="PRO_0000038550"
FT PEPTIDE 436..451
FT /note="Spacer peptide 2"
FT /id="PRO_0000038551"
FT CHAIN 452..507
FT /note="p6-gag"
FT /id="PRO_0000038552"
FT ZN_FING 393..410
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 414..431
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 106..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..230
FT /note="Interaction with host PPIA/CYPA and NUP153"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT REGION 220..228
FT /note="PPIA/CYPA-binding loop"
FT /evidence="ECO:0000250|UniProtKB:P04591"
FT REGION 280..366
FT /note="Dimerization/Multimerization of capsid protein p24"
FT /evidence="ECO:0000250|UniProtKB:P04591"
FT REGION 445..487
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 458..461
FT /note="PTAP/PSAP motif"
FT MOTIF 490..499
FT /note="LYPX(n)L motif"
FT COMPBIAS 115..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 135..136
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 366..367
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 380..381
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 435..436
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 451..452
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT MOD_RES 151
FT /note="Phosphoserine; by host MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P12493"
FT MOD_RES 390
FT /note="Asymmetric dimethylarginine; in Nucleocapsid protein
FT p7; by host PRMT6"
FT /evidence="ECO:0000250"
FT MOD_RES 412
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:0000269|PubMed:1548743"
FT VARIANT 35
FT /note="V -> I"
FT VARIANT 46
FT /note="I -> V"
FT VARIANT 75
FT /note="R -> L"
FT VARIANT 75
FT /note="R -> N"
FT VARIANT 75
FT /note="R -> S"
FT VARIANT 93
FT /note="K -> E"
FT CONFLICT 18
FT /note="K -> N (in Ref. 1; AAA44853)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="Q -> E (in Ref. 1; AAA44853)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="A -> V (in Ref. 1; AAA44853)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="A -> T (in Ref. 1; AAA44853)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..320
FT /note="WM -> RT (in Ref. 1; AAA44853)"
FT /evidence="ECO:0000305"
FT CONFLICT 448..449
FT /note="PG -> R (in Ref. 1; AAA44853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 56761 MW; AC6F207EC41C4726 CRC64;
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHVVWASRE LERFAINPGL LETSEGCRQI
LGQLQPSLQT GSEERKSLYN TVATLYCVHQ KIKIKDTKEA LEKIEEEQNK SKKKAQQAAA
DTGNRGNSSQ VSQNYPIVQN IQGQMVHQAI SPRTLNAWVK VVEEKAFSPE VIPMFSALSE
GATPQDLNTM LNTVGGHQAA MQMLKETINE EAAEWDRLHP AHAGPIAPGQ MREPRGSDIA
GTTSTLQEQI GWMTNNPPIP VGEIYKRWII LGLNKIVRMY SPSSILDIRQ GPKEPFRDYV
DRFYKTLRAE QASQEVKNWM TETLLVQNAN PDCKTILKAL GPAATLEEMM TACQGVGGPG
HKARVLAEAM SQVTNSATIM MQRGNFRNQR KIIKCFNCGK EGHIAKNCRA PRKRGCWKCG
KEGHQMKDCT ERQANFLGKI WPSCKGRPGN FPQSRTEPTA PPEESFRFGE ETTTPYQKQE
KKQETIDKDL YPLASLKSLF GNDPLSQ
