GAG_MLVDE
ID GAG_MLVDE Reviewed; 536 AA.
AC P29168;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 101.
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 Murine leukemia virus (strain DEF27).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=31688;
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: 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; M64096; AAA46509.1; ALT_SEQ; Genomic_DNA.
DR PIR; B40416; FOMVME.
DR SMR; P29168; -.
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..536
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390809"
FT CHAIN 2..129
FT /note="Matrix protein p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040888"
FT CHAIN 130..213
FT /note="RNA-binding phosphoprotein p12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040889"
FT CHAIN 214..476
FT /note="Capsid protein p30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040890"
FT CHAIN 477..536
FT /note="Nucleocapsid protein p10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040891"
FT ZN_FING 500..517
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 139..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..474
FT /evidence="ECO:0000255"
FT MOTIF 183..186
FT /note="PPXY motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 165..190
FT /note="Pro 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 p14"
FT /evidence="ECO:0000250"
FT SITE 213..214
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT SITE 476..477
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 536 AA; 60891 MW; 4D990FD5C5AEF39B CRC64;
MGQTITTPLS LTLEHWRDVQ CIASNQSVDV KRRRWVTFCS VEWPSFDVGW PLDGTFNLDI
ILQVKSKVFC PGPHGHPDQV PYIVTWEALA YHPPPWVKPF VSPKPFPLST LPFSPPGPSA
HPPSRSDLYT ALIPSIKTKP PKSRVLPTNG GPLIDLLTEN PPNLGEQGPP LPKGPVKKRR
PPPPRYSPPG PMVSRLRGNR DPPAADSTTS RAFPLRLGGN GQLQYWPFSS SDLYNWKNNN
PSFSEDPGKL TALIESVLTT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGNDGRPT
QLPNEVNSAF PLERPDWDYT TPEGRNHLVL YRQLLLAGLQ NAGRSPTNLA KVKGITQGPS
ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA PDIGRKLERL EDLKSKTLGD
LVREAEKIFN KRETPEEREE RIRRETEEKE ERRRAEDEQR EKERDRRRHR EMSKFLATVV
TGQRQDRQGG ERRRPQLDKD QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGD
