GAG_SIVTN
ID GAG_SIVTN Reviewed; 524 AA.
AC Q8AII2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 96.
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 TAN1) (SIV-cpz) (Chimpanzee
OS immunodeficiency virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=388910;
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12525658; DOI=10.1128/jvi.77.3.2233-2242.2003;
RA Santiago M.L., Bibollet-Ruche F., Bailes E., Kamenya S., Muller M.N.,
RA Lukasik M., Pusey A.E., Collins D.A., Wrangham R.W., Goodall J., Shaw G.M.,
RA Sharp P.M., Hahn B.H.;
RT "Amplification of a complete simian immunodeficiency virus genome from
RT fecal RNA of a wild chimpanzee.";
RL J. Virol. 77:2233-2242(2003).
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=Q8AII2-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=Q8AII1-1; 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 domain: a PTAP/PSAP
CC motif, which interacts with the UEV domain of TSG101 (By similarity).
CC {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; AF447763; AAO13959.1; -; Genomic_RNA.
DR SMR; Q8AII2; -.
DR PRO; PR:Q8AII2; -.
DR Proteomes; UP000007222; 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; 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 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; 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..524
FT /note="Gag polyprotein"
FT /id="PRO_0000261254"
FT CHAIN 2..155
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249368"
FT CHAIN 156..389
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249369"
FT PEPTIDE 390..403
FT /note="Spacer peptide p2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249370"
FT CHAIN 404..463
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249371"
FT PEPTIDE 464..479
FT /note="Spacer peptide p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249372"
FT CHAIN 480..524
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000249373"
FT ZN_FING 417..434
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 438..455
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 113..153
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 501..504
FT /note="PTAP/PSAP motif"
FT SITE 155..156
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 389..390
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 403..404
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 463..464
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 479..480
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 524 AA; 57324 MW; 5A2476B6D7C68425 CRC64;
MGARASVLRG DKLDTWESIR LKSRGRKKYL IKHLVWAGSE LQRFAMNPGL MENVEGCWKI
ILQLQPSVDI GSPEIISLFN TICVLYCVHA GERVQDTEEA VKIVKMKLTV QKNNSTATSS
GQRQNAGEKE ETVPPSGNTG NTGRATETPS GSRLYPVITD AQGVARHQPI SPRTLNAWVR
VIEEKGFNPE VIPMFSALSE GATPYDLNSM LNAVGEHQAA MQMLKEVINE EAAEWDRAHP
AHAGPQQAGM LREPTGADIA GTTSTLQEQV LWMTTPQAQG GVPVGDIYKR WIILGLNKLV
RMYSPVSILD IKQGPKEPFR DYVDRFYKTI RAEQASQPVK TWMTETLLVQ NANPDCKHIL
KALGQGATLE EMLTACQGVG GPSHKAKILA EAMASATAGG VNMLQGGKRP PLKKGQLQCF
NCGKVGHTAR NCRAPRKKGC WRCGQEGHQM KDCTTRNNST GVNFLGKRTP LWGCRPGNFV
QNTPEKGKAQ EQETAQTPVV PTAPPLEMTM KGGFSLKSIF GSDQ
