ID   GAG_FRSF5               Reviewed;         187 AA.
AC   P03331;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2026, 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;
GN   Name=gag;
OS   Friend spleen focus-forming virus (isolate 502) (FSFFV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Spleen focus-forming virus.
OX   NCBI_TaxID=355329;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6576374; DOI=10.1073/pnas.80.16.5037;
RA   Clark S.P., Mak T.W.;
RT   "Complete nucleotide sequence of an infectious clone of Friend spleen
RT   focus-forming provirus: gp55 is an envelope fusion glycoprotein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:5037-5041(1983).
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 pre-integration complex (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   -!- 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. Matrix protein p15 contains one L domain: a
CC       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 contains one L domain: a LYPX(n)L motif which
CC       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   -!- CAUTION: This gag polyprotein does not encode any capsid and
CC       nucleoprotein. {ECO:0000305}.
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DR   EMBL; K00021; AAA46486.1; -; Genomic_RNA.
DR   PIR; A03929; FOVW5S.
DR   RefSeq; NP_041217.1; NC_001500.1.
DR   SMR; P03331; -.
DR   ELM; P03331; -.
DR   GeneID; 1491887; -.
DR   KEGG; vg:1491887; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
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; Gamma-retroviral matrix domain; 1.
DR   InterPro; IPR000840; G_retro_matrix.
DR   InterPro; IPR036946; G_retro_matrix_sf.
DR   InterPro; IPR050462; Retroviral_Gag-Pol_poly.
DR   InterPro; IPR010999; Retrovr_matrix.
DR   PANTHER; PTHR33166; GAG_P30 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01140; Gag_MA; 1.
DR   SUPFAM; SSF47836; Retroviral matrix proteins; 1.
PE   3: Inferred from homology;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   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..187
FT                   /note="Gag polyprotein"
FT                   /id="PRO_0000390799"
FT   CHAIN           2..129
FT                   /note="Matrix protein p15"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040841"
FT   CHAIN           130..187
FT                   /note="RNA-binding phosphoprotein p12"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000040842"
FT   REGION          107..187
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   COMPBIAS        157..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            129..130
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   187 AA;  20804 MW;  7B0774B671E31185 CRC64;
     MGQTVTTPLS LTLEHWEDVQ RTASNQSVDV KKRRWVTFCS AEWPTFGVGW PQDGTFNLDI
     ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF VSPKLSPSPT APILPSGPST
     QPPPRSALYP ALTPSIKPGP SPIMADLSLT FSQKTLRRTE DRDRPPLTEM ATEKRPPPLL
     RFLPPLP
//