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-SEP-2026, entry version 136.
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   Baboon endogenous virus.
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   PRO; PR:P03341; -.
DR   GO; GO:0030430; C:host cell cytoplasm; ISS:UniProtKB.
DR   GO; GO:0044185; C:host cell late endosome membrane; ISS:UniProtKB.
DR   GO; GO:0020002; C:host cell plasma membrane; ISS:UniProtKB.
DR   GO; GO:0072494; C:host multivesicular body; 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:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.180; Gamma-retroviral matrix domain; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 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; IPR050462; Retroviral_Gag-Pol_poly.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1.
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; Retroviral matrix proteins; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 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..165
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..187
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..204
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..525
FT                   /note="Basic and acidic 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
//