Gag polyprotein (Pr65gag) (Core polyprotein) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-gag)]

 GAG_XMRV4               Reviewed;         536 AA.
 Q2F7I9;
 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
 21-MAR-2006, sequence version 1.
 07-APR-2021, entry version 66.
 RecName: Full=Gag polyprotein;
          Short=Pr65gag;
 AltName: Full=Core polyprotein;
 Contains:
   RecName: Full=Matrix protein p15;
            Short=MA;
 Contains:
   RecName: Full=RNA-binding phosphoprotein p12;
   AltName: Full=pp12;
 Contains:
   RecName: Full=Capsid protein p30;
            Short=CA;
 Contains:
   RecName: Full=Nucleocapsid protein p10;
            Short=NC-gag;
 Name=gag;
 Xenotropic MuLV-related virus (isolate VP42) (XMRV).
 Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
 Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
 unclassified Gammaretrovirus.
 NCBI_TaxID=356664;
 NCBI_TaxID=9606; Homo sapiens (Human).
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC RNA].
 PubMed=16609730; DOI=10.1371/journal.ppat.0020025;
 Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A.,
 Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H.,
 DeRisi J.L.;
 "Identification of a novel Gammaretrovirus in prostate tumors of patients
 homozygous for R462Q RNASEL variant.";
 PLoS Pathog. 2:E25-E25(2006).
 -!- FUNCTION: Gag polyprotein plays a role in budding and is processed by
     the viral protease during virion maturation outside the cell. During
     budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-
     like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to
     Gag binding host factors. Interaction with HECT ubiquitin ligases
     probably link the viral protein to the host ESCRT pathway and
     facilitate release (By similarity). {ECO:0000250}.
 -!- FUNCTION: Matrix protein p15 targets Gag and gag-pol polyproteins to
     the plasma membrane via a multipartite membrane binding signal, that
     includes its myristoylated N-terminus. Also mediates nuclear
     localization of the preintegration complex (By similarity).
     {ECO:0000250}.
 -!- FUNCTION: Capsid protein p30 forms the spherical core of the virion
     that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
 -!- FUNCTION: Nucleocapsid protein p10 is involved in the packaging and
     encapsidation of two copies of the genome. Binds with high affinity to
     conserved elements within the packaging signal, located near the 5'-end
     of the genome. This binding is dependent on genome dimerization (By
     similarity). {ECO:0000250}.
 -!- SUBUNIT: Capsid protein p30 is a homohexamer, that further associates
     as homomultimer. The virus core is composed of a lattice formed from
     hexagonal rings, each containing six capsid monomers (By similarity).
     {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250}. Host
     cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Host late
     endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Host
     endosome, host multivesicular body {ECO:0000250}. Note=These locations
     are probably linked to virus assembly sites. {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
 -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.
 -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10]: Virion {ECO:0000305}.
 -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
     essential for viral particle budding. They recruit proteins of the host
     ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
     ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one
     L domain: a PPXY motif which potentially interacts with the WW domain 3
     of NEDD4 E3 ubiquitin ligase. Matrix protein p15 contains one L domain:
     a PTAP/PSAP motif, which potentially interacts with the UEV domain of
     TSG101. The junction between the matrix protein p15 and RNA-binding
     phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which
     potentially interacts with PDCD6IP (By similarity). {ECO:0000250}.
 -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
     proteins. The protease is released by autocatalytic cleavage. The
     polyprotein is cleaved during and after budding, this process is termed
     maturation (By similarity). {ECO:0000250}.
 -!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
     residues. {ECO:0000250}.
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 EMBL; DQ241302; ABB83227.1; -; Genomic_RNA.
 SMR; Q2F7I9; -.
 Proteomes; UP000008602; Genome.
 GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
 GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
 GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
 GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
 GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
 GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
 Gene3D; 1.10.150.180; -; 1.
 Gene3D; 1.10.375.10; -; 1.
 InterPro; IPR000840; G_retro_matrix.
 InterPro; IPR036946; G_retro_matrix_sf.
 InterPro; IPR003036; Gag_P30.
 InterPro; IPR008919; Retrov_capsid_N.
 InterPro; IPR010999; Retrovr_matrix.
 InterPro; IPR001878; Znf_CCHC.
 InterPro; IPR036875; Znf_CCHC_sf.
 Pfam; PF01140; Gag_MA; 1.
 Pfam; PF02093; Gag_p30; 1.
 Pfam; PF00098; zf-CCHC; 1.
 SMART; SM00343; ZnF_C2HC; 1.
 SUPFAM; SSF47836; SSF47836; 1.
 SUPFAM; SSF47943; SSF47943; 1.
 SUPFAM; SSF57756; SSF57756; 1.
 PROSITE; PS50158; ZF_CCHC; 1.
 3: Inferred from homology;
 Capsid protein; Coiled coil; Host cell membrane; Host endosome;
 Host membrane; Host-virus interaction; Lipoprotein; Membrane;
 Metal-binding; Myristate; Phosphoprotein; RNA-binding; Viral budding;
 Viral budding via the host ESCRT complexes; Viral nucleoprotein;
 Viral release from host cell; Virion; Zinc; Zinc-finger.
 INIT_MET        1
                 /note="Removed; by host"
                 /evidence="ECO:0000250"
 CHAIN           2..536
                 /note="Gag polyprotein"
                 /evidence="ECO:0000250"
                 /id="PRO_0000390840"
 CHAIN           2..129
                 /note="Matrix protein p15"
                 /evidence="ECO:0000255"
                 /id="PRO_0000390841"
 CHAIN           130..213
                 /note="RNA-binding phosphoprotein p12"
                 /evidence="ECO:0000255"
                 /id="PRO_0000390842"
 CHAIN           214..476
                 /note="Capsid protein p30"
                 /evidence="ECO:0000255"
                 /id="PRO_0000390843"
 CHAIN           477..536
                 /note="Nucleocapsid protein p10"
                 /evidence="ECO:0000255"
                 /id="PRO_0000390844"
 ZN_FING         500..517
                 /note="CCHC-type"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
 COILED          436..476
                 /evidence="ECO:0000255"
 MOTIF           109..112
                 /note="PTAP/PSAP motif"
 MOTIF           128..132
                 /note="LYPX(n)L motif"
 MOTIF           161..164
                 /note="PPXY motif"
 SITE            129..130
                 /note="Cleavage; by viral protease p14"
                 /evidence="ECO:0000250"
 SITE            213..214
                 /note="Cleavage; by viral protease p14"
                 /evidence="ECO:0000250"
 SITE            476..477
                 /note="Cleavage; by viral protease p14"
                 /evidence="ECO:0000250"
 MOD_RES         190
                 /note="Phosphoserine; by host"
                 /evidence="ECO:0000250"
 LIPID           2
                 /note="N-myristoyl glycine; by host"
                 /evidence="ECO:0000250"
 SEQUENCE   536 AA;  60402 MW;  14E6C765479E3C24 CRC64;
 MGQTVTTPLS LTLQHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW PQDGTFNLGI
 ISQVKSRVFC PGPHGHPDQV PYIVTWEALA YDPPPWVKPF VSPKPPPLPT APVLPPGPSA
 QPPSRSALYP ALTPSIKSKP PKPQVLPDSG GPLIDLLTED PPPYGAQPSS SARENNEEEA
 ATTSEVSPPS PMVSRLRGRR DPPAADSTTS QAFPLRMGGD GQLQYWPFSS SDLYNWKNNN
 PSFSEDPGKL TALIESVLIT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGNDGRPT
 QLPNEVNAAF PLERPDWGYT TTEGRNHLVL YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN
 ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA PDIGRKLERL EDLKSKTLGD
 LVREAEKIFN KRETPEEREE RIRREIEEKE ERRRAEDEQR ERERDRRRHR EMSKLLATVV
 IGQRQDRQGG ERRRPQLDKD QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGD

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