GAG_MLVCB
ID GAG_MLVCB Reviewed; 536 AA.
AC P27460;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 112.
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 Cas-Br-E murine leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11792;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840655; DOI=10.1093/nar/19.7.1707;
RA Perryman S.M., McAtee F.J., Portis J.L.;
RT "Complete nucleotide sequence of the neurotropic murine retrovirus CAS-BR-
RT E.";
RL Nucleic Acids Res. 19:1707-1707(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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Gag polyprotein;
CC IsoId=P27460-1; Sequence=Displayed;
CC Name=Glyco-Gag protein;
CC IsoId=P0DOH4-1; 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; X57540; CAA40759.1; -; Genomic_DNA.
DR SMR; P27460; -.
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 Alternative initiation; Capsid protein; Coiled coil; Host cell membrane;
KW Host cytoplasm; Host endosome; Host membrane; Host-virus interaction;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Phosphoprotein;
KW RNA-binding; Ubl conjugation; 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:0000255"
FT CHAIN 2..536
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390808"
FT CHAIN 2..129
FT /note="Matrix protein p15"
FT /id="PRO_0000040884"
FT CHAIN 130..213
FT /note="RNA-binding phosphoprotein p12"
FT /id="PRO_0000040885"
FT CHAIN 214..476
FT /note="Capsid protein p30"
FT /id="PRO_0000040886"
FT CHAIN 477..536
FT /note="Nucleocapsid protein p10-Gag"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040887"
FT ZN_FING 500..517
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 112..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..391
FT /note="Interaction with host PIAS4"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT REGION 428..433
FT /note="Interaction with host UBE2I"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT REGION 432..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..476
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 160..163
FT /note="PPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT COMPBIAS 168..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..521
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 213..214
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT SITE 476..477
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250|UniProtKB:P03332"
FT MOD_RES 190
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 536 AA; 60740 MW; 3E0F863A393960AE CRC64;
MGQTVTTPLS LTLDHWKDVE RTAHNQSVDV KKRRWVTFCS VEWPTFNVGW PQDGTFNRDI
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPLPPS APSLLPEPPL
STSPRSSLYP ALTPSLGAKP KPQVLPDSGG PLIDLLTEDP PPYRDPGPPP SDRDRDDGEA
APAGEAPDPS PMASRLRGRR ELPVADSTTS QAFPLRSGGN GQLQYWPFSS SDLYNWKNNN
PSFSEDPGKL TALIESVLLT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGEDGRPT
QLPNEINDAF PLERPDWDYN TQRGRNHLVL YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN
ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA PDIGRKLERL EDLKSKTLGD
LVREAEKIFN KRETPEEREE RIKRETEEKE ERRRAEDEQK EKERDRRRHR EMSKLLATVV
SGQKQDRQGG ERRRPQLDKD QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLALDD
