GAG_MLVHO
ID GAG_MLVHO Reviewed; 540 AA.
AC P21435; Q80877; Q80878; Q80879; Q80880;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 110.
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 Hortulanus murine leukemia virus (HoMuLV) (Mus hortulanus virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11799;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2554579; DOI=10.1016/0042-6822(89)90221-3;
RA Voytek P., Kozak C.A.;
RT "Nucleotide sequence and mode of transmission of the wild mouse ecotropic
RT virus, HoMuLV.";
RL Virology 173:58-67(1989).
CC -!- FUNCTION: Gag polyprotein plays a role in budding and is processed by
CC 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 link the viral protein to the host ESCRT pathway and
CC facilitate release (By similarity). {ECO:0000250}.
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}. Host late
CC endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Host
CC endosome, host multivesicular body {ECO:0000250}. Note=These locations
CC are probably linked to virus assembly sites. {ECO:0000250}.
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. RNA-binding phosphoprotein p12 contains one
CC L domain: a PPXY motif which potentially interacts with the WW domain 3
CC of NEDD4 E3 ubiquitin ligase. Matrix protein p15 contains one L domain:
CC a PTAP/PSAP motif, which potentially interacts with the UEV domain of
CC TSG101. The junction between the matrix protein p15 and RNA-binding
CC phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which
CC potentially interacts with PDCD6IP (By similarity). {ECO:0000250}.
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}.
CC -!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
CC residues. {ECO:0000250}.
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DR EMBL; M26528; AAA45464.1; -; Genomic_RNA.
DR PIR; A32594; FOMVHL.
DR SMR; P21435; -.
DR ELM; P21435; -.
DR GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
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 endosome;
KW Host membrane; Host-virus interaction; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Phosphoprotein; RNA-binding; 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:0000250"
FT CHAIN 2..540
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390814"
FT CHAIN 2..129
FT /note="Matrix protein p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040908"
FT CHAIN 130..217
FT /note="RNA-binding phosphoprotein p12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040909"
FT CHAIN 218..480
FT /note="Capsid protein p30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040910"
FT CHAIN 481..540
FT /note="Nucleocapsid protein p10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040911"
FT ZN_FING 504..521
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 107..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 440..481
FT /evidence="ECO:0000255"
FT MOTIF 109..112
FT /note="PTAP/PSAP motif"
FT MOTIF 128..132
FT /note="LYPX(n)L motif"
FT MOTIF 160..163
FT /note="PPXY motif"
FT COMPBIAS 107..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..525
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 217..218
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT SITE 480..481
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT MOD_RES 194
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 540 AA; 61383 MW; 5F25150086F9EE95 CRC64;
MGQTITTPLS LTLDHWRDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW PQDGTFNKDI
ITQVKIKVFS PGPHGHPDQV PYIVTWEAIA YDPPPWAKPF VHPQLSVSPS APSAFSHEVS
GPPTRSSLYP ALTPTKSPSP KTQVLSDDGG PLIDLLSDDP PPYRGPENQP PAGRPTTTMQ
EMPRLPLKVP QEPSPMASRL RGRREHPAAD STTSQAFPLR TGGNGQLQYW PFSSADLYNW
KNNNPSFSED PGKLTALIES VLITHQPTWD DCQQLLGTLL TGEEKQRVLL EARKAVRGND
GRPTQLPNEI NDAFPLERPD WDYTTPAGRN HLVLYRQLLL AGLQHAGRSP TNLAKVKGIT
QGPNESPSAF LERLKEAYRR YTPYDPEDPG QETNVSMSFI WQSAPDIGRK LERLEDLKSK
TLGDLVREAE RIFNKRETPE EREERIRRET EEKEERRRAE NEQREKERDR RRHREMSKLL
ATVVSGQRQD RQGGERRRPQ LDKDQCAYCK EKGHWAKDCP KKPRGPRGPR PQTSLLTLDD
