GAG_MSVMT
ID GAG_MSVMT Reviewed; 468 AA.
AC P32594;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 94.
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 Moloney murine sarcoma virus (strain ts110) (MoMSV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=31691;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1501276; DOI=10.1128/jvi.66.9.5329-5337.1992;
RA Huai L., Chiocca S.M., Gilbreth M.A., Ainsworth J.R., Bishop L.A.,
RA Murphy E.C. Jr.;
RT "Moloney murine sarcoma virus MuSVts110 DNA: cloning, nucleotide sequence,
RT and gene expression.";
RL J. Virol. 66:5329-5337(1992).
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 -!- FUNCTION: Nucleocapsid protein p10 is 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 (By
CC similarity). {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 probably translated as a Gag-Mos
CC polyprotein.
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DR EMBL; M96854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A42745; FOMVMU.
DR BMRB; P32594; -.
DR SMR; P32594; -.
DR GO; GO:0020002; C:host cell plasma membrane; 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: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 nucleoprotein; Viral release from host cell; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..468
FT /note="Gag polyprotein"
FT /id="PRO_0000390819"
FT CHAIN 2..131
FT /note="Matrix protein p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040953"
FT CHAIN 132..215
FT /note="RNA-binding phosphoprotein p12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040954"
FT CHAIN 216..468
FT /note="Capsid protein p30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040955"
FT REGION 111..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 111..114
FT /note="PTAP/PSAP motif"
FT MOTIF 130..134
FT /note="LYPX(n)L motif"
FT MOTIF 162..165
FT /note="PPXY motif"
FT COMPBIAS 111..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 131..132
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT SITE 215..216
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 468 AA; 52681 MW; AF4F795F5D69824F CRC64;
MGQTVTTPLS LTLDHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLL PSAPSLPLEP
PLSTPPQSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGDSG
EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRTG GNGQLQYWPF SSSDLYNWKS
NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR
PTQLPNEVDA AFPLERPDWE YTTQAGRNHL VHYRQLLIAG LQNAGRSPTN LAKVKGITQG
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLRNKTL
GDLVREAERI FNKRETPEER EERIRREREE KEERHAPKLP WLFLIISP
