GAG_SIVCZ
ID GAG_SIVCZ Reviewed; 508 AA.
AC P17282;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 23-FEB-2022, entry version 119.
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 p2;
DE Contains:
DE RecName: Full=Nucleocapsid protein p7;
DE Short=NC;
DE Contains:
DE RecName: Full=Spacer peptide p1;
DE Contains:
DE RecName: Full=p6-gag;
GN Name=gag;
OS Simian immunodeficiency virus (isolate CPZ GAB1) (SIV-cpz) (Chimpanzee
OS immunodeficiency virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=402771;
OH NCBI_TaxID=9596; Pan (chimpanzees).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2188136; DOI=10.1038/345356a0;
RA Huet T., Cheynier R., Meyerhans A., Roelants G., Wain-Hobson S.;
RT "Genetic organization of a chimpanzee lentivirus related to HIV-1.";
RL Nature 345:356-359(1990).
CC -!- FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to
CC the plasma membrane via a multipartite membrane binding signal, that
CC includes its myristoylated N-terminus. Also mediates nuclear
CC localization of the preintegration complex. Implicated in the release
CC from host cell mediated by Vpu (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Capsid protein p24 forms the conical core of the virus that
CC encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC -!- FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral
CC dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc
CC fingers (By similarity). {ECO:0000250}.
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}.
CC -!- SUBUNIT: [Matrix protein p17]: Homotrimer. Interacts with gp41 (via C-
CC terminus). {ECO:0000250|UniProtKB:P04591,
CC ECO:0000250|UniProtKB:P12493}.
CC -!- SUBUNIT: [p6-gag]: Interacts with host TSG101 (By similarity).
CC {ECO:0000250|UniProtKB:P12493}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host
CC nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane
CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry,
CC the nuclear localization signal (NLS) of the matrix protein
CC participates with Vpr to the nuclear localization of the viral genome.
CC During virus production, the nuclear export activity of the matrix
CC protein counteracts the NLS to maintain the Gag and Gag-Pol
CC polyproteins in the cytoplasm, thereby directing unspliced RNA to the
CC plasma membrane (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000305}.
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=P17282-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P17283-1; 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 (By similarity). {ECO:0000250}.
CC -!- PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. The polyprotein is cleaved during and after budding, this
CC process is termed maturation (By similarity). {ECO:0000250}.
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; X52154; CAA36401.1; -; Genomic_RNA.
DR PIR; S09983; FOLJSI.
DR SMR; P17282; -.
DR ELM; P17282; -.
DR PRO; PR:P17282; -.
DR Proteomes; UP000009153; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
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; 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 3: Inferred from homology;
KW Capsid protein; Host cell membrane; Host cytoplasm; Host membrane;
KW Host nucleus; Host-virus interaction; Lipoprotein; Membrane; Metal-binding;
KW 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:0000250"
FT CHAIN 2..508
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316150"
FT CHAIN 2..140
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038644"
FT CHAIN 141..371
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038645"
FT PEPTIDE 372..387
FT /note="Spacer peptide p2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316151"
FT CHAIN 388..442
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038646"
FT PEPTIDE 443..458
FT /note="Spacer peptide p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316152"
FT CHAIN 459..508
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316153"
FT ZN_FING 400..417
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 421..438
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 104..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..508
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 465..468
FT /note="PTAP/PSAP motif"
FT MOTIF 491..500
FT /note="LYPX(n)L motif"
FT COMPBIAS 114..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 140..141
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 371..372
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 387..388
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 442..443
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 458..459
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 508 AA; 55963 MW; 6FC992B9EB4CBB5D CRC64;
MGARASVLTG GKLDRWEKVR LRPGGRKRYM MKHLVWASRE LERFACDPGL MESKEGCTKL
LQQLEPALKT GSEGLRSLFN TLAVLWCIHS DITVEDTQKA LEQLKRHHGE QQSKTESNSG
SREGGASQGA SASAGISGNY PLVQNAQGQM VHQAISPRTL NAWVKVVEEK AFSPEVIPMF
SALSEGALPQ DVNTMLNAVG GHQGAMQVLK EVINEEAAEW DRLHPTHAGP IAPGQLREPR
GSDIAGTTST LQEQIGWTTA NPPIPVGDVY RRWVILGLNK VVRMYCPVSI LDIRQGPKEP
FRDYVDRFYK TLRAEQASQE VKNWMTDTLL VQNANPDCKQ ILKALGPGAT LEEMMTACQG
VGGPSHKARV LAEAMSMVQN QGRADVFFQK GQGAGPKRKI KCFNCGKEGH LARNCKAPRR
KGCWRCGQEG HQMKDCTGRQ VNFLGKGWPS RSGRPGNFVQ NRTEPTAPPI ESYGYQEEEK
SQEKKEGESS LYPPTSLKSL FGSDPSSQ
