GAG_BAEVM
ID GAG_BAEVM Reviewed; 537 AA.
AC P03341; P10268;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 02-JUN-2021, entry version 126.
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 Baboon endogenous virus (strain M7).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC unclassified Gammaretrovirus.
OX NCBI_TaxID=11764;
OH NCBI_TaxID=9554; Papio (baboons).
OH NCBI_TaxID=9565; Theropithecus gelada (Gelada baboon).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kato S., Matsuo K., Nishimura N., Takahashi N., Takano T.;
RT "The entire nucleotide sequence of baboon endogenous virus DNA: a chimeric
RT genome structure of murine type C and simian type D retroviruses.";
RL Jpn. J. Genet. 62:127-137(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6408267; DOI=10.1128/jvi.47.1.137-145.1983;
RA Tamura T.;
RT "Provirus of M7 baboon endogenous virus: nucleotide sequence of the gag-pol
RT region.";
RL J. Virol. 47:137-145(1983).
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. The virus core is composed of a lattice formed from
CC 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 two L domain: a PPXY motif which
CC potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase
CC and a PTAP/PSAP motif, which potentially interacts with the UEV domain
CC of TSG101 (By similarity). {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=J02034; Type=Miscellaneous discrepancy; Note=Several errors.; Evidence={ECO:0000305};
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DR EMBL; D10032; BAA00923.1; -; Genomic_DNA.
DR EMBL; X05470; CAA29027.1; -; Genomic_DNA.
DR EMBL; J02034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A03939; FOMVVB.
DR PIR; JT0260; FOMVM7.
DR RefSeq; YP_009109690.1; NC_022517.1.
DR SMR; P03341; -.
DR GeneID; 22318532; -.
DR KEGG; vg:22318532; -.
DR Proteomes; UP000007443; 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..537
FT /note="Gag polyprotein"
FT /id="PRO_0000390797"
FT CHAIN 2..145
FT /note="Matrix protein p15"
FT /id="PRO_0000040826"
FT CHAIN 146..226
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000040827"
FT CHAIN 227..477
FT /note="Capsid protein p30"
FT /id="PRO_0000040828"
FT CHAIN 478..537
FT /note="Nucleocapsid protein p10-Gag"
FT /id="PRO_0000040829"
FT ZN_FING 501..518
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 137..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 154..157
FT /note="PPXY motif"
FT /evidence="ECO:0000305"
FT MOTIF 173..176
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000305"
FT COMPBIAS 143..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 145..146
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 226..227
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 477..478
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 537 AA; 60624 MW; 5DEEE4437CFCFB79 CRC64;
MGQTLTTPLS LTLTHFSDVR ARAHNLSVGV RKGRWQTFCS SEWPTLHVGW PRDGTFDLSV
ILQVKTKVMD PGPHGHPDQV AYIITWEDLV RNPPPWVKPF LHTPSTSKST LLALEVPKNR
TLDPPKPVLP DESQQDLLFQ DPLPHPPHNP LLEPPPYNSP SPPVLSPVSP TTPSAPTPSS
LVSSSTPPSS PAPPELTPRT PPQTPRLRLR RAEGQDGPST WQSSLFPLRT VNRTIQYWPF
SASDLYNWKT HNPSFSQDPQ ALTSLIESIL LTHQPTWDDC QQLLQVLLTT EERQRVLLEA
RKNVPGPGGL PTQLPNEIDE GFPLTRPDWD YETAPGRESL RIYRQALLAG LKGAGKRPTN
LAKVRTITQG KDESPAAFME RLLEGFRMYT PFDPEAPEHK ATVAMSFIDQ AALDIKGKLQ
RLDGIQTHGL QELVREAEKV YNKRETPEER EARLIKEQEE REDRRDRKRD KHLTKILAAV
VTEKRAGKSG ETRRRPKVDK DQCAYCKERG HWIKDCPKRP RDQKKPAPVL TLGEDSE
