GAG_FRSF5
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 29-SEP-2021, entry version 101.
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 unclassified Gammaretrovirus.
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 preintegration 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:0016020; C:membrane; 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 InterPro; IPR000840; G_retro_matrix.
DR InterPro; IPR036946; G_retro_matrix_sf.
DR InterPro; IPR010999; Retrovr_matrix.
DR Pfam; PF01140; Gag_MA; 1.
DR SUPFAM; SSF47836; SSF47836; 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 107..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
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
