GAG_MLVBM
ID GAG_MLVBM Reviewed; 537 AA.
AC P29167;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 109.
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-Gag;
DE Short=NC-gag;
GN Name=gag;
OS Murine leukemia virus (strain BM5 eco).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=31687;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1649328; DOI=10.1128/jvi.65.8.4232-4241.1991;
RA Chattopadhyay S.K., Sengupta D.N., Fredrickson T.N., Morse H.C. III,
RA Hartley J.W.;
RT "Characteristics and contributions of defective, ecotropic, and mink cell
RT focus-inducing viruses involved in a retrovirus-induced immunodeficiency
RT syndrome of mice.";
RL J. Virol. 65:4232-4241(1991).
CC -!- FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed
CC by 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 links the viral protein to the host ESCRT pathway and
CC facilitates release. {ECO:0000250|UniProtKB:P03332}.
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.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [RNA-binding phosphoprotein p12]: Constituent of the pre-
CC integration complex (PIC) which tethers the latter to mitotic
CC chromosomes. {ECO:0000250|UniProtKB:P03332}.
CC -!- FUNCTION: [Capsid protein p30]: Forms the spherical core of the virion
CC that encapsulates the genomic RNA-nucleocapsid complex.
CC {ECO:0000250|UniProtKB:P03336}.
CC -!- FUNCTION: [Nucleocapsid protein p10-Gag]: Involved in the packaging and
CC encapsidation of two copies of the genome. Binds with high affinity to
CC conserved UCUG elements within the packaging signal, located near the
CC 5'-end of the genome. This binding is dependent on genome dimerization.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBUNIT: [Capsid protein p30]: Homohexamer; further associates as
CC homomultimer (By similarity). The virus core is composed of a lattice
CC formed from hexagonal rings, each containing six capsid monomers.
CC Interacts with mouse UBE2I and mouse PIAS4.
CC {ECO:0000250|UniProtKB:P03332, ECO:0000250|UniProtKB:P03336}.
CC -!- SUBUNIT: [Gag polyprotein]: Interacts (via PPXY motif) with host NEDD4.
CC Interacts (via PSAP motif) with host TSG101. Interacts (via LYPX(n)L
CC motif) with host PDCD6IP. {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [Gag polyprotein]: Virion
CC {ECO:0000250|UniProtKB:P03332}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03332}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body
CC {ECO:0000250|UniProtKB:P26807}.
CC -!- SUBCELLULAR LOCATION: [Matrix protein p15]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein p30]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [Nucleocapsid protein p10-Gag]: Virion
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P03332}. Note=Localizes to the host cytoplasm
CC early in infection and binds to the mitotic chromosomes later on.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- DOMAIN: [Gag polyprotein]: Late-budding domains (L domains) are short
CC sequence motifs essential for viral particle budding. They recruit
CC proteins of the host ESCRT machinery (Endosomal Sorting Complex
CC Required for Transport) or ESCRT-associated proteins. RNA-binding
CC phosphoprotein p12 contains one L domain: a PPXY motif which interacts
CC with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is
CC essential for virus egress. Matrix protein p15 contains one L domain: a
CC PTAP/PSAP motif, which interacts with the UEV domain of TSG101. The
CC junction between the matrix protein p15 and RNA-binding phosphoprotein
CC p12 also contains one L domain: a LYPX(n)L motif which interacts with
CC PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in
CC budding and possibly drive residual virus release.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: [Gag polyprotein]: Ubiquitinated by ITCH. Gag can recruit the
CC ubiquitin ligase Itch in an L domain-independent manner to facilitate
CC virus release via a mechanism that involves Gag ubiquitination.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral
CC protease yield mature proteins. The protease is released by
CC autocatalytic cleavage. The polyprotein is cleaved during and after
CC budding, this process is termed maturation.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: [Capsid protein p30]: Sumoylated; required for virus replication.
CC {ECO:0000250|UniProtKB:P03332}.
CC -!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
CC residues. {ECO:0000250|UniProtKB:P03332}.
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DR EMBL; M64095; AAA46510.1; -; Genomic_DNA.
DR PIR; A40416; FOMVMB.
DR SMR; P29167; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0072494; C:host multivesicular body; 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: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 3: Inferred from homology;
KW Capsid protein; Coiled coil; Host cell membrane; Host cytoplasm;
KW Host endosome; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Metal-binding; Myristate; Phosphoprotein; RNA-binding;
KW Ubl conjugation; Viral budding; Viral budding via the host ESCRT complexes;
KW Viral matrix protein; Viral nucleoprotein; Viral release from host cell;
KW Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255"
FT CHAIN 2..537
FT /note="Gag polyprotein"
FT /id="PRO_0000390807"
FT CHAIN 2..129
FT /note="Matrix protein p15"
FT /id="PRO_0000040880"
FT CHAIN 130..214
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000040881"
FT CHAIN 215..477
FT /note="Capsid protein p30"
FT /id="PRO_0000040882"
FT CHAIN 478..537
FT /note="Nucleocapsid protein p10-Gag"
FT /id="PRO_0000040883"
FT ZN_FING 501..518
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 112..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..392
FT /note="Interaction with host PIAS4"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT REGION 429..434
FT /note="Interaction with host UBE2I"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT REGION 433..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..470
FT /evidence="ECO:0000255"
FT MOTIF 109..112
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 128..132
FT /note="LYPX(n)L motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 161..164
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT COMPBIAS 115..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..522
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|UniProtKB:P03332"
FT SITE 214..215
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 477..478
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOD_RES 191
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 537 AA; 60423 MW; ABD2E70299BFFD64 CRC64;
MGQTVTTPLS LTLEHWGDVQ RIASNQSVGV KKRRWVTFCS AEWPTFGVGW PQDGTFNLDI
ILQVKSKVFS PGPHGHPDQV PYIVTWEAIA YEPPPWVKPF VSPKLSLSPT APILPSGPST
QPPPRSALYP AFTPSIKPRP SKPQVLSDDG GPLIDLLTED PPPYGEQGPS SPDGDGDREE
ATSTSEIPAP SPMVSRLRGK RDPPAADSTT SRAFPLRLGG NGQLQYWPFS SSDLYNWKNN
NPSFSEDPGK LTALIESVLT THQPTWDDCQ QLLGTLLTGE EKQRVLLEAR KAVRGNDGRP
TQLPNEVNSA FPLERPDWDY TTPEGRNHLV LYRQLLLAGL QNAGRSPTNL AKVKGITQGP
NESPSAFLER LKEAYRRYTP YDPEDPGQET NVSMSFIWQS APAIGRKLER LEDLKSKTLG
DLVREAEKIF NKRETPEERE ERIRRETEEK EERRRAGDEQ REKERDRRRQ REMSKLLATV
VTGQRQDRQG GERRRPQLDK DQCAYCKEKG HWAKDCPKKP RGPRGPRPQT SLLTLDD
