GAG_MLVDU
ID GAG_MLVDU Reviewed; 529 AA.
AC P23090;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 104.
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 Duplan murine leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11794;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2538760; DOI=10.1038/338505a0;
RA Aziz D.C., Hanna Z., Jolicoeur P.;
RT "Severe immunodeficiency disease induced by a defective murine leukaemia
RT virus.";
RL Nature 338:505-508(1989).
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 UCUG elements within the packaging signal, located near the
CC 5'-end of the genome. This binding is dependent on genome dimerization
CC (By 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. Gag-p12 contains one L domain: a PPXY motif
CC which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC ligase (Potential). {ECO:0000305}.
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; X14576; CAA32715.1; -; Genomic_DNA.
DR PIR; S03901; FOMVDU.
DR SMR; P23090; -.
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: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:0019068; P:virion assembly; IEA:InterPro.
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 membrane;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Phosphoprotein;
KW RNA-binding; Viral matrix protein; Viral nucleoprotein; Virion; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..529
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390810"
FT CHAIN 2..129
FT /note="Matrix protein p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040892"
FT CHAIN 130..206
FT /note="RNA-binding phosphoprotein p12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040893"
FT CHAIN 207..469
FT /note="Capsid protein p30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040894"
FT CHAIN 470..529
FT /note="Nucleocapsid protein p10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040895"
FT ZN_FING 493..510
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 116..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..467
FT /evidence="ECO:0000255"
FT MOTIF 176..179
FT /note="PPXY motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 168..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 129..130
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT SITE 206..207
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT SITE 469..470
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 529 AA; 60318 MW; 4B0677A58AADDD15 CRC64;
MGQTVTTPLS LTLDHWKDVQ CIASNQSVDV KRRRWVTFCS VEWPSFDVGW PLDGTFNLDI
ILQVKSKVTC PGPHGHPDQV PYIVTWEALV YHPPPWVKPF VSPKPFPLST LPFSPPGPSA
HPPSRSDLYT ALIPSKPPKS RVLPPNGGPL IDLLTENLPN LPPLSKGPVK KRRPPPPRYS
PPNPMESRVR GRRDPPAADS TSSQAFPLRM GGDGQLQYWP FSSSDLYNWK NNNPSFSEDP
GKLTALIESV LTTHQPTWDD CQQLLGTLLT GEEKQRVLLE ARKAVRGNDG RPTQLPNEVN
SAFPLERPDW NYSTPEGRNH LVLYRQLLLA GLHNAGRSPT NLAKVKRITQ GPNESPSAFL
ERLKEAYRRY TPYDPEDPGQ ETNVSMSFIW QSAPDIGRKL ERLEDLKSKT LGDLVREAEK
IFNKRETPEE REERIRRETE EKEERRRAED EQREKERDRR RHREMSKFLA TVVTGQRQDR
QGGERRRPQL DEDQCAYCKE KGHWAKDCPK KPRGPRGPRP QTSLLTLGD
