GAG_SIVMK
ID GAG_SIVMK Reviewed; 506 AA.
AC P05893;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 23-FEB-2022, entry version 125.
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 K6W) (SIV-mac) (Simian
OS immunodeficiency virus rhesus monkey).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11735;
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3497350; DOI=10.1038/328539a0;
RA Franchini G., Gallo R.C., Guo H.-G., Gurgo C., Callatti E., Fargnoli K.,
RA Hall L., Wong-Staal F., Reitz M.S. Jr.;
RT "Sequence of simian immunodeficiency virus and its relationship to the
RT human immunodeficiency viruses.";
RL Nature 328:539-543(1987).
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=P05893-1; Sequence=Displayed;
CC Name=Gag-Pol polyprotein;
CC IsoId=P05897-1; 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 probably a macaque 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; M19499; AAB59905.1; ALT_SEQ; Genomic_RNA.
DR PDB; 2XS1; X-ray; 2.30 A; B=483-502.
DR PDBsum; 2XS1; -.
DR SMR; P05893; -.
DR PRO; PR:P05893; -.
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; 1.
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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Host cell membrane; Host cytoplasm;
KW Host membrane; Host nucleus; Host-virus interaction; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Phosphoprotein; Repeat; Ribosomal frameshifting;
KW RNA-binding; 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..506
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316130"
FT CHAIN 2..135
FT /note="Matrix protein p17"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038636"
FT CHAIN 136..364
FT /note="Capsid protein p24"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038637"
FT PEPTIDE 365..379
FT /note="Spacer peptide p2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316131"
FT CHAIN 380..433
FT /note="Nucleocapsid protein p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316132"
FT PEPTIDE 434..447
FT /note="Spacer peptide p1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316133"
FT CHAIN 448..506
FT /note="p6-gag"
FT /evidence="ECO:0000250"
FT /id="PRO_0000316134"
FT ZN_FING 391..408
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 412..429
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 114..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..239
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 458..461
FT /note="PTAP/PSAP motif"
FT COMPBIAS 115..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..239
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 447..448
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT HELIX 489..498
FT /evidence="ECO:0007829|PDB:2XS1"
SQ SEQUENCE 506 AA; 56725 MW; E0790BD20E2157C0 CRC64;
MGARNAVLSG KKADELEKIR LRPGGKKKYM LKHVVWAANE LDRFGLAESL LENKEGCQKI
LSVLAPLVPT GSENLKSLYN TVCVIWCIHA EEKVKHTEEA KQIVQRHLVV ETGTAETMPK
TSRPTAPSSG RGGNYPVQQI GGNYVHLPLS PRTLNAWVKL IEEKKFGAEV VPGFQALSEG
CTPYDINQML NCVGDHQAAM QIIRDIINEE AADWDLQHPQ PAPQQGQLRE PSGSDIAGTT
SSVDEQIQWM YRQQNPIPVG NIYRRWIQLR LQKCVRMYNP INILDVKQRP KEPFQSYVDR
FYKSLRAEQT DAAVKNWMTQ TLLIQNANPD CKLVLKGLGV NPTLEEMLTA CQGVGGPGQK
ARLMAEALKE ALRPVPTPFA AAQQRGPRKP IKCWNCGKEG HSARQCRAPR RQRCWKCGKM
DHVMAKCPDR QAGFLGLGPW GKKPRNFPMA QVHQGLTPTA PPEDPAVDLL KNYMQLGKQQ
RESREKPYKE VTEDLLHLNS LFGGDQ
