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Gag polyprotein (Core polyprotein) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-gag)]

 GAG_MLVRD               Reviewed;         537 AA.
P11269;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 110.
RecName: Full=Gag polyprotein;
AltName: Full=Core polyprotein;
Contains:
RecName: Full=Matrix protein p15;
Short=MA;
Contains:
RecName: Full=RNA-binding phosphoprotein p12;
AltName: Full=pp12;
Contains:
RecName: Full=Capsid protein p30;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p10-Gag;
Short=NC-gag;
Name=gag;
Radiation murine leukemia virus.
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Gammaretrovirus; Murine leukemia virus.
NCBI_TaxID=11787;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3033897; DOI=10.1016/0042-6822(87)90241-8;
Merregaert J., Janowski M., Reddy E.P.;
"Nucleotide sequence of a radiation leukemia virus genome.";
Virology 158:88-102(1987).
[2]
PROTEIN SEQUENCE OF 478-505.
PubMed=6267042;
Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W.,
Oroszlan S.;
"Primary structure of the low molecular weight nucleic acid-binding
proteins of murine leukemia viruses.";
J. Biol. Chem. 256:8400-8406(1981).
-!- FUNCTION: Gag polyprotein: Plays a role in budding and is
processed by the viral protease during virion maturation outside
the cell. During budding, it recruits, in a PPXY-dependent or
independent manner, Nedd4-like ubiquitin ligases that conjugate
ubiquitin molecules to Gag, or to Gag binding host factors.
Interaction with HECT ubiquitin ligases probably links the viral
protein to the host ESCRT pathway and facilitates release.
{ECO:0000250|UniProtKB:P03332}.
-!- FUNCTION: Matrix protein p15: Targets Gag and gag-pol polyproteins
to the plasma membrane via a multipartite membrane binding signal,
that includes its myristoylated N-terminus. Also mediates nuclear
localization of the pre-integration complex.
{ECO:0000250|UniProtKB:P03332}.
-!- FUNCTION: RNA-binding phosphoprotein p12: Constituent of the pre-
integration complex (PIC) which tethers the latter to mitotic
chromosomes. {ECO:0000250|UniProtKB:P03332}.
-!- FUNCTION: Capsid protein p30: Forms the spherical core of the
virion that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250|UniProtKB:P03336}.
-!- FUNCTION: Nucleocapsid protein p10-Gag: Involved in the packaging
and encapsidation of two copies of the genome. Binds with high
affinity to conserved UCUG elements within the packaging signal,
located near the 5'-end of the genome. This binding is dependent
on genome dimerization. {ECO:0000250|UniProtKB:P03332}.
-!- SUBUNIT: Capsid protein p30: Homohexamer; further associates as
homomultimer (By similarity). Capsid protein p30: The virus core
is composed of a lattice formed from hexagonal rings, each
containing six capsid monomers. Capsid protein p30: Interacts with
mouse UBE2I and mouse PIAS4. Gag polyprotein: Interacts (via PPXY
motif) with host NEDD4. Gag polyprotein: Interacts (via PSAP
motif) with host TSG101. Gag polyprotein: Interacts (via LYPX(n)L
motif) with host PDCD6IP (By similarity).
{ECO:0000250|UniProtKB:P03332, ECO:0000250|UniProtKB:P03336}.
-!- SUBCELLULAR LOCATION: Gag polyprotein: Virion
{ECO:0000250|UniProtKB:P03332}. Host cell membrane
{ECO:0000250|UniProtKB:P03332}; Lipid-anchor
{ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular
body {ECO:0000250|UniProtKB:P26807}.
-!- SUBCELLULAR LOCATION: Matrix protein p15: Virion
{ECO:0000250|UniProtKB:P03332}.
-!- SUBCELLULAR LOCATION: Capsid protein p30: Virion
{ECO:0000250|UniProtKB:P03332}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p10-Gag: Virion
{ECO:0000250|UniProtKB:P03332}.
-!- SUBCELLULAR LOCATION: RNA-binding phosphoprotein p12: Host
cytoplasm {ECO:0000250|UniProtKB:P03332}. Note=Localizes to the
host cytoplasm early in infection and binds to the mitotic
chromosomes later on. {ECO:0000250|UniProtKB:P03332}.
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle budding. They
recruit proteins of the host ESCRT machinery (Endosomal Sorting
Complex Required for Transport) or ESCRT-associated proteins. RNA-
binding phosphoprotein p12 contains one L domain: a PPXY motif
which interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase.
PPXY motif is essential for virus egress. Matrix protein p15
contains one L domain: a PTAP/PSAP motif, which interacts with the
UEV domain of TSG101. The junction between the matrix protein p15
and RNA-binding phosphoprotein p12 also contains one L domain: a
LYPX(n)L motif which interacts with PDCD6IP. Both PSAP and
LYPX(n)L domains might play little to no role in budding and
possibly drive residual virus release.
{ECO:0000250|UniProtKB:P03332}.
-!- PTM: Gag polyprotein: Ubiquitinated by ITCH. Gag can recruit the
ubiquitin ligase Itch in an L domain-independent manner to
facilitate virus release via a mechanism that involves Gag
ubiquitination. {ECO:0000250|UniProtKB:P03332}.
-!- PTM: Gag polyprotein: Specific enzymatic cleavages by the viral
protease yield mature proteins. The protease is released by
autocatalytic cleavage. The polyprotein is cleaved during and
after budding, this process is termed maturation.
{ECO:0000250|UniProtKB:P03332}.
-!- PTM: Capsid protein p30: Sumoylated; required for virus
replication. {ECO:0000250|UniProtKB:P03332}.
-!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
residues. {ECO:0000250|UniProtKB:P03332}.
-----------------------------------------------------------------------
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EMBL; K03363; AAA46518.1; -; Genomic_RNA.
PIR; A26183; FOMVRV.
ProteinModelPortal; P11269; -.
SMR; P11269; -.
PRIDE; P11269; -.
OrthoDB; VOG0900014R; -.
Proteomes; UP000007778; Genome.
GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 1.10.150.180; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 4.10.60.10; -; 1.
InterPro; IPR000840; G_retro_matrix.
InterPro; IPR036946; G_retro_matrix_sf.
InterPro; IPR002079; Gag_p12.
InterPro; IPR003036; Gag_P30.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF01140; Gag_MA; 1.
Pfam; PF01141; Gag_p12; 1.
Pfam; PF02093; Gag_p30; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
Capsid protein; Coiled coil; Complete proteome;
Direct protein sequencing; Host cell membrane; Host cytoplasm;
Host endosome; Host membrane; Host-virus interaction; Lipoprotein;
Membrane; Metal-binding; Myristate; Phosphoprotein; RNA-binding;
Ubl conjugation; Viral budding;
Viral budding via the host ESCRT complexes; Viral matrix protein;
Viral nucleoprotein; Viral release from host cell; Virion; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000255}.
CHAIN 2 537 Gag polyprotein. {ECO:0000250}.
/FTId=PRO_0000390816.
CHAIN 2 129 Matrix protein p15.
/FTId=PRO_0000040916.
CHAIN 130 214 RNA-binding phosphoprotein p12.
/FTId=PRO_0000040917.
CHAIN 215 477 Capsid protein p30.
/FTId=PRO_0000040918.
CHAIN 478 537 Nucleocapsid protein p10-Gag.
/FTId=PRO_0000040919.
ZN_FING 501 518 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
REGION 344 392 Interaction with host PIAS4.
{ECO:0000250|UniProtKB:P03332}.
REGION 429 434 Interaction with host UBE2I.
{ECO:0000250|UniProtKB:P03332}.
COILED 437 477 {ECO:0000255}.
MOTIF 109 112 PTAP/PSAP motif.
{ECO:0000250|UniProtKB:P03332}.
MOTIF 128 132 LYPX(n)L motif.
{ECO:0000250|UniProtKB:P03332}.
MOTIF 161 164 PPXY motif.
{ECO:0000250|UniProtKB:P03332}.
SITE 129 130 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03332}.
SITE 214 215 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03332}.
SITE 477 478 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03332}.
MOD_RES 191 191 Phosphoserine; by host.
{ECO:0000250|UniProtKB:P03332}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255}.
CONFLICT 479 479 T -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 482 482 T -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 537 AA; 60784 MW; 312AF7B2BBB4B7FB CRC64;
MGQTVTTPLS LTLEHWGDVQ RIASNQSVEV KKRRRVTFCP AEWPTFDVGW PQDGTFNLDI
ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPSWVKPF VSPKLSLSPT APILPSGPST
QPPPRSALYP ALTPSIKPRP SKPQVLSDNG GPLIDLLTED PPPYGEQGPS SPDGDGDREE
ATYTSEIPAP SPMVSRLRGK RDPPAADSTT SRAFPLRLGG NGQLQYWPFS SSDLYNWKNN
NPSFSEDPGK LTALIESVLT THQPTWDDCQ QLLGTLLTGE EKQRVLLEAR KAVRGNDGRP
TQLPNEVNSA FPLERPDWDY TTPEGRNHLV LYRQLLLAGL QNAGRSPTNL AKVKGITQGP
NESPSAFLER LKEAYRRYTP YDPEDHGQET SVSMSFIWQS APDIGRKLER LEDLKSKTLR
DLVREAEKIF NKRETPEERE ERFRRETEEN EERRRAEDEQ REKERDRRRQ REMSKLLATV
VTGQRQDRQG GERKRPQLDK DQCAYCKEKG HWAKDCPKKP RGPRGPRPQT SLLTLDD


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