GAG_WMSV
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 02-JUN-2021, entry version 109.
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) (Smian 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 PRIDE; 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; -; 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; 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
