GAG_GALV
ID GAG_GALV Reviewed; 520 AA.
AC P21416;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 112.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Short=MA;
DE Contains:
DE RecName: Full=RNA-binding phosphoprotein p12;
DE AltName: Full=pp12;
DE Contains:
DE RecName: Full=Capsid protein p30;
DE Short=CA;
DE Contains:
DE RecName: Full=Nucleocapsid protein p10-Gag;
DE Short=NC-gag;
GN Name=gag;
OS Gibbon ape leukemia virus (GALV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11840;
OH NCBI_TaxID=9577; Hylobatidae (gibbons).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2683360; DOI=10.1016/0042-6822(89)90236-5;
RA Delassus S., Sonigo P., Wain-Hobson S.;
RT "Genetic organization of gibbon ape leukemia virus.";
RL Virology 173:205-213(1989).
CC -!- FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed
CC by the viral protease during virion maturation outside the cell. During
CC budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
CC like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
CC Gag binding host factors. Interaction with HECT ubiquitin ligases
CC probably links the viral protein to the host ESCRT pathway and
CC facilitates release. {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [Matrix protein p15]: 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 pre-integration complex.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-
CC integration complex (PIC) which tethers the latter to mitotic
CC chromosomes. {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion
CC that encapsulates the genomic RNA-nucleocapsid complex.
CC {ECO:0000250|UniProtKB:P03336}.
CC -!- FUNCTION: [Nucleocapsid protein p10-Gag]: Involved in the packaging and
CC encapsidation of two copies of the genome. Binds with high affinity to
CC conserved elements within the packaging signal, located near the 5'-end
CC of the genome. This binding is dependent on genome dimerization.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBUNIT: [Capsid protein p30]: Homohexamer; further associates as
CC homomultimer (By similarity). The virus core is composed of a lattice
CC formed from hexagonal rings, each containing six capsid monomers.
CC {ECO:0000250|UniProtKB:P03332, ECO:0000250|UniProtKB:P03336}.
CC -!- SUBUNIT: [Gag polyprotein]: Interacts (via PPXY motif) with host NEDD4.
CC Interacts (via PSAP motif) with host TSG101.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion
CC {ECO:0000250|UniProtKB:P03332}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane
CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body
CC {ECO:0000250|UniProtKB:P26807}. Note=These locations are probably
CC linked to virus assembly sites. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10-Gag]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P03332}. Note=Localizes to the host cytoplasm
CC early in infection and binds to the mitotic chromosomes later on.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle budding. They recruit
CC proteins of the host ESCRT machinery (Endosomal Sorting Complex
CC Required for Transport) or ESCRT-associated proteins. RNA-binding
CC phosphoprotein p12 contains one L domain: a PPXY motif which
CC potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC ligase. Matrix protein p15 contains one L domain: a PTAP/PSAP motif,
CC which potentially interacts with the UEV domain of TSG101.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The protease is released by
CC autocatalytic cleavage. The polyprotein is cleaved during and after
CC budding, this process is termed maturation.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
CC residues. {ECO:0000250|UniProtKB:P03332}.
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DR EMBL; M26927; AAA46809.1; -; Genomic_RNA.
DR PIR; A32595; FOLJGL.
DR RefSeq; NP_056789.1; NC_001885.2.
DR SMR; P21416; -.
DR PRIDE; P21416; -.
DR GeneID; 1491894; -.
DR KEGG; vg:1491894; -.
DR Proteomes; UP000008231; Genome.
DR GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072494; C:host multivesicular body; 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:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
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; 1.10.150.180; -; 1.
DR Gene3D; 1.10.375.10; -; 1.
DR InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR003036; Gag_P30.
DR InterPro; IPR008919; Retrov_capsid_N.
DR InterPro; IPR010999; Retrovr_matrix.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
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 endosome;
KW Host membrane; Host-virus interaction; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Phosphoprotein; RNA-binding; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
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:0000255"
FT CHAIN 2..520
FT /note="Gag polyprotein"
FT /id="PRO_0000390804"
FT CHAIN 2..125
FT /note="Matrix protein p15"
FT /id="PRO_0000040863"
FT CHAIN 126..195
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000040864"
FT CHAIN 196..454
FT /note="Capsid protein p30"
FT /id="PRO_0000040865"
FT CHAIN 455..520
FT /note="Nucleocapsid protein p10-Gag"
FT /id="PRO_0000040866"
FT ZN_FING 489..506
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 110..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 116..119
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 139..142
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT COMPBIAS 136..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 125..126
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 195..196
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 454..455
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 520 AA; 58110 MW; 77FE4760E61D1E2D CRC64;
MGQDNSTPIS LTLNHWRDVR TRAHNLSVEI KKGKWQTFCS SEWPTFGVGW PPEGTFNLSV
IFAVKKIVFQ ENGGHPDQVP YIVVWQDLAQ NPPPWVPASA KVAVVSDTRR PVAGRPSAPP
RPPIYPATDD LLLLSEPTPP PYPAALPPPL APQAIGPPSG QMPDSSDPEG PAAGTRSRRA
RSPADNSGPD STVILPLRAI GPPAEPNGLV PLQYWPFSSA DLYNWKSNHP SFSENPAGLT
GLLESLMFSH QPTWDDCQQL LQILFTTEER ERILLEARKN VLGDNGAPTQ LENLINEAFP
LNRPHWDYNT AAGRERLLVY RRTLVAGLKG AARRPTNLAK VREVLQGPAE PPSVFLERLM
EAYRRYTPFD PSSEGQQAAV AMAFIGQSAP DIKKKLQRLE GLQDYSLQDL VKEAEKVYHK
RETEEERQER EKKEAEEKER RRDRPKKKNL TKILAAVVSR EGSTGRQTGN LSNQAKKTPR
DGRPPLDKDQ CAYCKEKGHW ARECPRKKHV REAKVLALDN
