GAG_SIVVG
ID GAG_SIVVG Reviewed; 521 AA.
AC P27978;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 23-FEB-2022, entry version 111.
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 agm.vervet (isolate AGM3) (SIV-agm.ver)
OS (Simian immunodeficiency virus African green monkey vervet).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11730;
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2158689; DOI=10.1016/0042-6822(90)90246-n;
RA Baier M., Garber C., Mueller C., Cichutek K., Kurth R.;
RT "Complete nucleotide sequence of a simian immunodeficiency virus from
RT African green monkeys: a novel type of intragroup divergence.";
RL Virology 176:216-221(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}. Note=Following
CC virus entry, the nuclear localization signal (NLS) of the matrix
CC protein participates with Vpr to the nuclear localization of the viral
CC genome. During virus production, the nuclear export activity of the
CC matrix 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=P27978-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P27980-1; 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: This is an African green monkey isolate.
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; M30931; AAA91913.1; -; Genomic_RNA.
DR SMR; P27978; -.
DR PRO; PR:P27978; -.
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: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 cytoplasm; Host nucleus; Host-virus interaction;
KW Lipoprotein; Metal-binding; Myristate; Phosphoprotein; 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..521
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316109"
FT CHAIN 2..145
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038622"
FT CHAIN 146..376
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038623"
FT PEPTIDE 377..390
FT /note="Spacer peptide p2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316110"
FT CHAIN 391..443
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038624"
FT PEPTIDE 444..458
FT /note="Spacer peptide p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316111"
FT CHAIN 483..521
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316112"
FT ZN_FING 402..419
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 423..440
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 116..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..521
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 467..470
FT /note="PTAP/PSAP motif"
FT COMPBIAS 121..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 443..444
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 521 AA; 58409 MW; 1F111BD2F2EDF4F5 CRC64;
MGAATSALNR RQLDKFEHIR LRPTGKKKYQ IKHLIWAGKE MERFGLHERL LESEEGCKKI
IEVLYPLEPT GSEGLKSLFN LVCVLFCVHK DKEVKDTEEA VAIVRQCCHL VEKERNAERN
TTETSSGQKK NDKGVTVPPG GSQNFPAQQQ GNAWIHVPLS PRTLNAWVKA VEEKKFGAEI
VPMFQALSEG CTPYDINQML NVLGDHQGAL QIVKEIINEE AAQWDIAHPP PAGPLPAGQL
RDPRGSDIAG TTSTVQEQLE WIYTANPRVD VGAIYRRWII LGLQKCVKMY NPVSVLDIRQ
GPKEAFKDYV DRFYKAIRAE QASGEVKQWM TESLLIQNAN PDCKVILKGL GMHPTLEEML
TACQGVGGPS YKAKVMAEMM QNMQSQNMMQ QGGQRGRPRP PVKCYNCGKF GHMQRQCPEP
RKMRCLKCGK PGHLAKDCRG QVNFLGYGRW MGAKPRNFPA ATLGVEPTAP PPPSPYDPAK
KLLQQYADKG KQLREQRKKP PAVNPDWTEG YSLNSLFGED Q
