GAG_SIVGB
ID GAG_SIVGB Reviewed; 502 AA.
AC P22381;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 23-FEB-2022, entry version 110.
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 GB1) (SIV-mnd) (Simian
OS immunodeficiency virus mandrill).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11732;
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2797181; DOI=10.1038/341539a0;
RA Tsujimoto H., Hasegawa A., Maki N., Fukasawa M., Miura T., Speidel S.,
RA Cooper R.W., Moriyama E.N., Gojobori T., Hayami M.;
RT "Sequence of a novel simian immunodeficiency virus from a wild-caught
RT African mandrill.";
RL Nature 341:539-541(1989).
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=P22381-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P22382-1; 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 mandrill 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; M27470; AAB49568.1; -; Genomic_RNA.
DR SMR; P22381; -.
DR PRO; PR:P22381; -.
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; 1.
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..502
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316121"
FT CHAIN 2..121
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038631"
FT CHAIN 122..353
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038632"
FT PEPTIDE 354..367
FT /note="Spacer peptide p2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316122"
FT CHAIN 368..432
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038633"
FT PEPTIDE 433..447
FT /note="Spacer peptide p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316123"
FT CHAIN 448..502
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316124"
FT ZN_FING 386..403
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 407..424
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 204..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..502
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 454..457
FT /note="PTAP/PSAP motif"
FT COMPBIAS 477..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 367..368
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 432..433
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 502 AA; 56481 MW; 1B2B12464BEE5E9F CRC64;
MGNGNSALLG TDLDKFEKIR LKRGGKKCYR LKHLCWCKGE LDRFGLSDKL LETQQGCEKI
LSVCWPLYDQ GSDNLKALVG TVCVVACIHA GIEIKSTQDA LKKLKVITRK EEKQEDESKN
FPVQRDAAGQ YQYTPISPRI IQTWVKTVEE KKWKPEVIPL FSALTEGAIS HDLNIMLNAV
GDHQGAMQVL KDVINEQAAE WDLTHPQQQP AQPGGGLRTP SGSDIAGTTS TVEEQLAWMN
MQQNAINVGT IYKSWIILGM NRLVKSHCPI SITDVRQGPK EAFKDYVDRF YNVMRAEQAS
GEVKMWMQQH LLIENANPEC KQILRSLGKG ATLEEMLEAC QGVGGPQHKA RLMAEMMRTV
VGQSQNFVQQ RGPQRGPVRQ PTGRKPICFN CNKEGHVARF FKAPRRKGCW NCGAMDHQKA
QCPKPAQQQR VNFLGYGPWG PSKPGNYPAQ EVTPTAPPLE EKPLQKTLST YQKLGRGLRQ
KMKEEKREED FHSLSTLFQE DQ
