GAG_MLVFF
ID GAG_MLVFF Reviewed; 538 AA.
AC P26806;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Gag polyprotein;
DE AltName: Full=Core polyprotein;
DE Contains:
DE RecName: Full=Matrix protein p15;
DE Contains:
DE RecName: Full=RNA-binding phosphoprotein p12;
DE AltName: Full=pp12;
DE Contains:
DE RecName: Full=Capsid protein p30;
DE Contains:
DE RecName: Full=Nucleocapsid protein p10-Gag;
DE Short=NC-gag;
GN Name=gag;
OS Friend murine leukemia virus (isolate FB29) (FrMLV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11797;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1762923; DOI=10.1093/nar/19.24.6950;
RA Perryman S., Nishio J., Chesebro B.;
RT "Complete nucleotide sequence of Friend murine leukemia virus, strain
RT FB29.";
RL Nucleic Acids Res. 19:6950-6950(1991).
RN [2]
RP PROTEIN SEQUENCE OF 479-512.
RX PubMed=6267042; DOI=10.1016/s0021-9258(19)68857-5;
RA Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W., Oroszlan S.;
RT "Primary structure of the low molecular weight nucleic acid-binding
RT proteins of murine leukemia viruses.";
RL J. Biol. Chem. 256:8400-8406(1981).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Gag polyprotein;
CC IsoId=P26806-1; Sequence=Displayed;
CC Name=Glyco-Gag protein;
CC IsoId=P0DOH5-1; Sequence=External;
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; Z11128; CAA77478.1; -; Genomic_DNA.
DR PIR; S70394; S70394.
DR RefSeq; NP_040332.1; NC_001362.1.
DR SMR; P26806; -.
DR DIP; DIP-61620N; -.
DR ELM; P26806; -.
DR IntAct; P26806; 1.
DR GeneID; 1491876; -.
DR KEGG; vg:1491876; -.
DR Proteomes; UP000008877; Genome.
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 1: Evidence at protein level;
KW Alternative initiation; Capsid protein; Coiled coil;
KW Direct protein sequencing; 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..538
FT /note="Gag polyprotein"
FT /id="PRO_0000390812"
FT CHAIN 2..131
FT /note="Matrix protein p15"
FT /id="PRO_0000040900"
FT CHAIN 132..215
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000040901"
FT CHAIN 216..478
FT /note="Capsid protein p30"
FT /id="PRO_0000040902"
FT CHAIN 479..538
FT /note="Nucleocapsid protein p10-Gag"
FT /id="PRO_0000040903"
FT ZN_FING 502..519
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 110..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..393
FT /note="Interaction with host PIAS4"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT REGION 430..435
FT /note="Interaction with host UBE2I"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT REGION 434..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 438..478
FT /evidence="ECO:0000255"
FT MOTIF 111..114
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 130..134
FT /note="LYPX(n)L motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOTIF 162..165
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT COMPBIAS 110..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..523
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|UniProtKB:P03332"
FT SITE 215..216
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 478..479
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOD_RES 192
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"
FT CONFLICT 501
FT /note="H -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 60929 MW; 2E652DDB9E0D4A3C CRC64;
MGQAVTTPLS LTLDHWKDVE RTAHNLSVEV RKRRWVTFCS AEWPTFNVGW PRDGTFNPDI
ITQVKIKVFS PGPHGHPDQV PYIVTWEAIA VDPPPWVRPF VHPKPPLSLP PSAPSLPPEP
PLSTPPQSSL YPALTSPLNT KPRPQVLPDS GGPLIDLLTE DPPPYRDPGP PSPDGNGDSG
EVAPTEGAPD PSPMVSRLRG RKEPPVADST TSQAFPLRLG GNGQYQYWPF SSSDLYNWKN
NNPSFSEDPA KLTALIESVL LTHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGEDGR
PTQLPNDIND AFPLERPDWD YNTQRGRNHL VHYRQLLLAG LQNAGRSPTN LAKVKGITQG
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVAMSFIWQ SAPDIGRKLE RLEDLKSKTL
GDLVREAEKI FNKRETPEER EERIRRETEE KEERRRAEDV QREKERDRRR HREMSKLLAT
VVSGQRQDRQ GGERRRPQLD HDQCAYCKEK GHWARDCPKK PRGPRGPRPQ ASLLTLDD
