GAG_SIVV1
ID GAG_SIVV1 Reviewed; 520 AA.
AC P27972;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 23-FEB-2022, entry version 113.
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 AGM155) (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=11727;
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2304139; DOI=10.1128/jvi.64.3.1086-1092.1990;
RA Johnson P.R., Fomsgaard A., Allan J.S., Gravell M., London W.T.,
RA Olmstead R.A., Hirsch V.M.;
RT "Simian immunodeficiency viruses from African green monkeys display unusual
RT genetic diversity.";
RL J. Virol. 64:1086-1092(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=P27972-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P27973-1; 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; M29975; AAA91905.1; -; Genomic_RNA.
DR SMR; P27972; -.
DR PRO; PR:P27972; -.
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..520
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316105"
FT CHAIN 2..141
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038619"
FT CHAIN 142..372
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038620"
FT PEPTIDE 373..386
FT /note="Spacer peptide p2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316106"
FT CHAIN 387..439
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038621"
FT PEPTIDE 440..454
FT /note="Spacer peptide p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316107"
FT CHAIN 482..520
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316108"
FT ZN_FING 398..415
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 419..436
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 117..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..520
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 463..466
FT /note="PTAP/PSAP motif"
FT COMPBIAS 120..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 439..440
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 520 AA; 57735 MW; 2FE1B7D0E484D414 CRC64;
MGAATSALNR RQLDEFEHIR LRPNGKKKYQ IKHLIWAGKK MDRFGLHEKL LETEEGCKKI
IEVLSPLEPT GSEGMKSLYN LVCVLLCVHQ EKKVKDTEEA LAIVRQCCHL VDKEKTAVTP
PGGQQKNNTG GTATPGGSQN FPAQQQGNAW VHVPLSPRTL NAWVKAVEEK KFGAEIVPMF
QALSEGCTPY DINQMLNVLG DHQGALQIVK EIINEEAAQW DVTHPPPAGP LPAGQLRDPG
GSDIAGTTST VQEQLEWIYT ANPRVDVGAI YRRWIILGLQ KCVKMYNPVS VLDIRQGPKE
PFKDYVDRFY KAIRAEQASG EVKQWMTESL LIQNANPDCK VILKGLGMHP TLEEMLTACQ
GVGGPSYKAK VMAEMMQNLQ SQNMVQQGGG RGRPRPPPKC YNCGKFGHMQ RQCPEPRKIK
CLKCGKPGHL AKDCRGQVNF LGYGRWMGTK PRNFPAATLG AEPSAPPPPN NSTPYDPAKK
LLQQYAEKGK QMRNQNRNPP ANNPDWNEGY SLNSLFGEDQ
