ID   GAG_MSVFR               Reviewed;         310 AA.
AC   P29175;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-JUN-2021, entry version 97.
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;
GN   Name=gag;
OS   FBR murine osteosarcoma virus (FBR-MSV) (Finkel-Biskis-Reilly murine
OS   osteosarcoma virus).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=353765;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6203215; DOI=10.1016/0042-6822(84)90133-8;
RA   van Beveren C., Enami S., Curran T., Verma I.M.;
RT   "FBR murine osteosarcoma virus. II. Nucleotide sequence of the provirus
RT   reveals that the genome contains sequences acquired from two cellular
RT   genes.";
RL   Virology 135:229-243(1984).
CC   -!- FUNCTION: Gag polyprotein plays a role in budding and is processed by
CC       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 link the viral protein to the host ESCRT pathway and
CC       facilitate release (By similarity). {ECO:0000250}.
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 preintegration complex (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Capsid protein p30 forms the spherical core of the virion
CC       that encapsulates the genomic RNA-nucleocapsid complex. {ECO:0000250}.
CC   -!- SUBUNIT: Capsid protein p30 is a homohexamer, that further associates
CC       as homomultimer. The virus core is composed of a lattice formed from
CC       hexagonal rings, each containing six capsid monomers (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250}. Host
CC       cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.
CC   -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC       essential for viral particle budding. They recruit proteins of the host
CC       ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC       ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one
CC       L domain: a PPXY motif which potentially interacts with the WW domain 3
CC       of NEDD4 E3 ubiquitin ligase. Matrix protein p15 contains one L domain:
CC       a PTAP/PSAP motif, which potentially interacts with the UEV domain of
CC       TSG101. The junction between the matrix protein p15 and RNA-binding
CC       phosphoprotein p12 also contains one L domain: a LYPX(n)L which
CC       potentially interacts with PDCD6IP (By similarity). {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC       proteins. The protease is released by autocatalytic cleavage. The
CC       polyprotein is cleaved during and after budding, this process is termed
CC       maturation (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Fos-Fox
CC       polyprotein.
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DR   EMBL; K02712; AAA46573.1; ALT_TERM; Genomic_DNA.
DR   PIR; A23244; FOMVFB.
DR   SMR; P29175; -.
DR   ELM; P29175; -.
DR   Proteomes; UP000237129; Chromosome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019028; C:viral capsid; 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: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; IPR002079; Gag_p12.
DR   InterPro; IPR003036; Gag_P30.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   Pfam; PF01140; Gag_MA; 1.
DR   Pfam; PF01141; Gag_p12; 1.
DR   Pfam; PF02093; Gag_p30; 1.
DR   SUPFAM; SSF47836; SSF47836; 1.
DR   SUPFAM; SSF47943; SSF47943; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host cell membrane; Host membrane; Host-virus interaction;
KW   Lipoprotein; Membrane; Myristate; RNA-binding; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral matrix protein;
KW   Viral release from host cell; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..310
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000390817"
FT   CHAIN           2..129
FT                   /note="Matrix protein p15"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040946"
FT   CHAIN           130..214
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040947"
FT   CHAIN           215..310
FT                   /note="Capsid protein p30"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040948"
FT   REGION          107..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           109..112
FT                   /note="PTAP/PSAP motif"
FT   MOTIF           128..132
FT                   /note="LYPX(n)L motif"
FT   MOTIF           161..164
FT                   /note="PPXY motif"
FT   COMPBIAS        107..129
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            129..130
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   SITE            214..215
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  33849 MW;  F5713E16959C5F8C CRC64;
     MGQTVTTPLS LTLEHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFDVGW PQDGTFNLDI
     ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF VSPKLSPSPT APILPSGPST
     QPPPRSALYP ALTPSIKPRP SKPQVLSDDG GPLIDLLTED PPPYGEQGPS SSDGDGDREE
     ATSTSEIPAP SPMVSRLRGK RDPPAADSTT SRAFPLRLGG NGQKNNNPSF SEDPGKLTAL
     IESVLTTHQP TWDDCQQLLG TLLTGEEKQR VLLEARKAVR GNDGRPTQMP NEVNAAFPLE
     RPDWDYTTPE