ID   GAG_WMSV                Reviewed;         521 AA.
AC   P03330; A0A0U3TJX4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 4.
DT   27-MAR-2024, entry version 114.
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   Woolly monkey sarcoma virus (WMSV) (Simian sarcoma-associated virus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11970;
OH   NCBI_TaxID=9518; Lagothrix (woolly monkeys).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6298772; DOI=10.1073/pnas.80.3.731;
RA   Devare S.G., Reddy E.P., Law J.D., Robbins K.C., Aaronson S.A.;
RT   "Nucleotide sequence of the simian sarcoma virus genome: demonstration that
RT   its acquired cellular sequences encode the transforming gene product
RT   p28sis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:731-735(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSAV {ECO:0000312|EMBL:ALV83311.1};
RX   PubMed=26637454; DOI=10.1128/jvi.02745-15;
RA   Alfano N., Kolokotronis S.O., Tsangaras K., Roca A.L., Xu W., Eiden M.V.,
RA   Greenwood A.D.;
RT   "Episodic diversifying selection shaped the genomes of gibbon ape leukemia
RT   virus and related gammaretroviruses.";
RL   J. Virol. 90:1757-1772(2015).
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 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA24514.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR   EMBL; V01201; CAA24514.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; KT724051; ALV83311.1; -; Genomic_DNA.
DR   PIR; A03928; FOMVGS.
DR   RefSeq; YP_001165469.2; NC_009424.4.
DR   RefSeq; YP_003580184.1; NC_009424.4.
DR   SMR; P03330; -.
DR   GeneID; 5176148; -.
DR   KEGG; vg:5176148; -.
DR   Proteomes; UP000167400; Genome.
DR   Proteomes; UP000203831; 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; 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; IPR010999; Retrovr_matrix.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR33166:SF1; CORE SHELL PROTEIN GAG P30 DOMAIN-CONTAINING PROTEIN; 1.
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; Coiled coil; Host cell membrane; Host cytoplasm;
KW   Host endosome; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Metal-binding; Myristate; Phosphoprotein; RNA-binding;
KW   Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW   Virion; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..521
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000390820"
FT   CHAIN           2..128
FT                   /note="Matrix protein p15"
FT                   /id="PRO_0000040960"
FT   CHAIN           129..196
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /id="PRO_0000040961"
FT   CHAIN           197..455
FT                   /note="Capsid protein p30"
FT                   /id="PRO_0000040962"
FT   CHAIN           456..521
FT                   /note="Nucleocapsid protein p10-Gag"
FT                   /id="PRO_0000040963"
FT   ZN_FING         490..507
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          106..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          408..455
FT                   /evidence="ECO:0000255"
FT   MOTIF           119..122
FT                   /note="PTAP/PSAP motif"
FT                   /evidence="ECO:0000250|UniProtKB:P03332"
FT   MOTIF           140..143
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        141..160
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            128..129
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03332"
FT   SITE            196..197
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03332"
FT   SITE            455..456
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"
FT   CONFLICT        14
FT                   /note="D -> G (in Ref. 1; CAA24514)"
FT   CONFLICT        33
FT                   /note="G -> E (in Ref. 1; CAA24514)"
FT   CONFLICT        112
FT                   /note="R -> Q (in Ref. 1; CAA24514)"
FT   CONFLICT        317
FT                   /note="R -> L (in Ref. 1; CAA24514)"
FT   CONFLICT        383
FT                   /note="M -> T (in Ref. 1; CAA24514)"
FT   CONFLICT        386
FT                   /note="I -> T (in Ref. 1; CAA24514)"
FT   CONFLICT        462
FT                   /note="R -> G (in Ref. 1; CAA24514)"
FT   CONFLICT        465
FT                   /note="R -> G (in Ref. 1; CAA24514)"
FT   CONFLICT        468
FT                   /note="Q -> R (in Ref. 1; CAA24514)"
FT   CONFLICT        473
FT                   /note="S -> G (in Ref. 1; CAA24514)"
SQ   SEQUENCE   521 AA;  58316 MW;  471F0C4FF190FDD0 CRC64;
     MGQNNSTPLS LTLDHWKDVR TRAHNLSVKI RKGKWQTFCS SEWPTFGVGW PPEGTFNLSV
     IFAVKRIVFQ ETGGHPDQVP YIVVWQDLAQ SPPPWVPPSA KIAVVSSPEN TRGPSAGRPS
     APPRPPIYPA TDDLLLLSEP PPYPAALPPP LAPPAVGPAP GQAPDSSDPE GPAAGTRSRR
     ARSPADDSGP DSTVILPLRA IGPPAEPNGL VPLQYWPFSS ADLYNWKSNH PSFSENPAGL
     TGLLESLMFS HQPTWDDCQQ LLQILFTTEE RERILLEARK NVLGDNGAPT QLENLINEAF
     PLNRPQWDYN TAAGRERLLV YRRTLVAGLK GAARRPTNLA KVREVLQGPA EPPSVFLERL
     MEAYRRYTPF DPSEEGQQAA VAMAFIGQSA PDIKKKLQRL EGLQDYSLQD LVREAEKVYH
     KRETEEERQE REKKEAEERE RRRDRRQEKN LTRILAAVVS ERGSRDRQTG NLSNRARKTP
     RDGRPPLDKD QCAYCKEKGH WARECPQKKN VREAKVLALD D
//