GAG_MSVMO
ID GAG_MSVMO Reviewed; 538 AA.
AC P03334;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 121.
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;
DE Contains:
DE RecName: Full=Nucleocapsid protein p10;
DE Short=NC-gag;
GN Name=gag;
OS Moloney murine sarcoma virus (MoMSV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11809;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (PROVIRUS).
RX PubMed=6170110; DOI=10.1126/science.6170110;
RA Reddy E.P., Smith M.J., Aaronson S.A.;
RT "Complete nucleotide sequence and organization of the Moloney murine
RT sarcoma virus genome.";
RL Science 214:445-450(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE 124 CIRCULAR).
RX PubMed=6173134; DOI=10.1016/0092-8674(81)90364-0;
RA van Beveren C., van Straaten F., Galleshaw J.A., Verma I.M.;
RT "Nucleotide sequence of the genome of a murine sarcoma virus.";
RL Cell 27:97-108(1981).
RN [3]
RP PROTEIN SEQUENCE OF 2-17, AND MYRISTOYLATION AT GLY-2.
RX PubMed=6340098; DOI=10.1073/pnas.80.2.339;
RA Henderson L.E., Krutzsch H.C., Oroszlan S.;
RT "Myristyl amino-terminal acylation of murine retrovirus proteins: an
RT unusual post-translational proteins modification.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:339-343(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 -!- 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 -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10]: 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}.
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DR EMBL; J02266; AAA46499.1; -; Genomic_RNA.
DR EMBL; V01185; CAA24507.1; -; Genomic_DNA.
DR PIR; A94261; FOMVM.
DR RefSeq; NP_057858.1; NC_001502.1.
DR BMRB; P03334; -.
DR SMR; P03334; -.
DR ELM; P03334; -.
DR iPTMnet; P03334; -.
DR GeneID; 1491884; -.
DR KEGG; vg:1491884; -.
DR Proteomes; UP000108184; Genome.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF01140; Gag_MA; 1.
DR Pfam; PF01141; Gag_p12; 1.
DR Pfam; PF02093; Gag_p30; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF47836; SSF47836; 1.
DR SUPFAM; SSF47943; SSF47943; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Direct protein sequencing; Host cell membrane;
KW Host membrane; Host-virus interaction; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..538
FT /note="Gag polyprotein"
FT /id="PRO_0000390818"
FT CHAIN 2..131
FT /note="Matrix protein p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040949"
FT CHAIN 132..215
FT /note="RNA-binding phosphoprotein p12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040950"
FT CHAIN 216..478
FT /note="Capsid protein p30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040951"
FT CHAIN 479..538
FT /note="Nucleocapsid protein p10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040952"
FT ZN_FING 502..519
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 111..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..538
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 COMPBIAS 435..476
FT /note="Basic and acidic 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 SITE 478..479
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:6340098"
FT VARIANT 519
FT /note="R -> K (in clone 124)"
SQ SEQUENCE 538 AA; 61209 MW; D78326F3B5701E56 CRC64;
MGQTVTTPLS LTLDHWKDVE RLAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLL PSAPSLPLEP
PLSTPPQSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGDSG
EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRTG GNGQLQYWPF SSSDLYNWKN
NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR
PTQLPNEVDA AFPLERPDWE YTTQAGRNHL VHYRQLLIAG LQNAGRSPTN LAKVKGITQG
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLRNKTL
GDLVREAERI FNKRETPEER EERIRREREE KEERRRTEDE QKEKERDRRR HREMSRLLAT
VVSGQRQDRQ EGERRRSQLD CDQCTYCEEQ GHWAKDCPRR PRGPRGPRPQ TSLLTLDD
