GAG_SIVEK
ID GAG_SIVEK Reviewed; 511 AA.
AC Q1A250;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 76.
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 EK505) (SIV-cpz) (Chimpanzee
OS immunodeficiency virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=388912;
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16728595; DOI=10.1126/science.1126531;
RA Keele B.F., Van Heuverswyn F., Li Y., Bailes E., Takehisa J.,
RA Santiago M.L., Bibollet-Ruche F., Chen Y., Wain L.V., Liegeois F., Loul S.,
RA Ngole E.M., Bienvenue Y., Delaporte E., Brookfield J.F., Sharp P.M.,
RA Shaw G.M., Peeters M., Hahn B.H.;
RT "Chimpanzee reservoirs of pandemic and nonpandemic HIV-1.";
RL Science 313:523-526(2006).
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=Q1A250-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=Q1A249-1; 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; DQ373065; ABD19492.1; -; Genomic_RNA.
DR SMR; Q1A250; -.
DR PRO; PR:Q1A250; -.
DR Proteomes; UP000008436; 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..511
FT /note="Gag polyprotein"
FT /id="PRO_0000261252"
FT CHAIN 2..135
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249357"
FT CHAIN 136..366
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249358"
FT PEPTIDE 367..380
FT /note="Spacer peptide p2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249359"
FT CHAIN 381..437
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249360"
FT PEPTIDE 438..453
FT /note="Spacer peptide p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249361"
FT CHAIN 454..511
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249362"
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 107..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..511
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 462..465
FT /note="PTAP/PSAP motif"
FT MOTIF 493..503
FT /note="LYPX(n)L motif"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..511
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 437..438
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 453..454
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 511 AA; 56750 MW; 5DEE460AA84CE2F6 CRC64;
MGARASVLTG GKLDQWEKIY LRPGGKKKYM MKHLVWASRE LERFACNPGL MDTAEGCAQL
LRQLEPALKT GSEGLRSLFN TLAVLYCVHN NIKVQNTQEA LEKLREKMKA EQKEPEPEQA
AGAAAAPESS ISRNYPLVQN AQGQMVHQPL SPRTLNAWVK VVEEKAFNPE VIPMFMALSE
GATPQDLNTM LNTVGGHQAA MQMLKEVINE EAAEWDRGHP VHMGPIPPGQ VREPRGSDIA
GTTSTLAEQV AWMTANPPVP VGDIYRRWIV LGLNKIVRMY SPASILDIKQ GPKETFRDYV
DRFYKTLRAE QATQEVKNWM TETLLVQNAN PDCKNILRAL GPGASLEEMM TACQGVGGPA
HKARVLAEAM TQAQTATSVF MQRGNFKGIR KTIKCFNCGK EGHLARNCKA PRKKGCWKCG
QEGHQMKDCR SGERQANFLG KVWPLSKGRP GNFPQTTTRK EPTAPPIESY GYQEEKTTQG
TEREEKEKTE SSLYPPLTSL KSLFGSDPSL Q
