GAG_XMRV6
ID GAG_XMRV6 Reviewed; 536 AA.
AC Q27ID9;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 02-JUN-2021, entry version 73.
DE RecName: Full=Gag polyprotein;
DE Short=Pr65gag;
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 Xenotropic MuLV-related virus (isolate VP62) (XMRV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC unclassified Gammaretrovirus.
OX NCBI_TaxID=373193;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RETRACTED PAPER.
RX PubMed=16609730; DOI=10.1371/journal.ppat.0020025;
RA Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A.,
RA Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H.,
RA DeRisi J.L.;
RT "Identification of a novel Gammaretrovirus in prostate tumors of patients
RT homozygous for R462Q RNASEL variant.";
RL PLoS Pathog. 2:E25-E25(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17234809; DOI=10.1073/pnas.0610291104;
RA Dong B., Kim S., Hong S., Das Gupta J., Malathi K., Klein E.A., Ganem D.,
RA Derisi J.L., Chow S.A., Silverman R.H.;
RT "An infectious retrovirus susceptible to an IFN antiviral pathway from
RT human prostate tumors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1655-1660(2007).
RN [3]
RP RETRACTION NOTICE OF PUBMED:16609730.
RX PubMed=23028303;
RX DOI=10.1371/annotation/7e2efc01-2e9b-4e9b-aef0-87ab0e4e4732;
RA Urisman A., Molinaro R.J., Fischer N., Plummer S.J., Casey G., Klein E.A.,
RA Malathi K., Magi-Galluzzi C., Tubbs R.R., Ganem D., Silverman R.H.,
RA DeRisi J.L.;
RL PLoS Pathog. 8:0-0(2012).
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 elements within the packaging signal, located near the 5'-end
CC of the genome. This binding is dependent on genome dimerization (By
CC 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.
CC -!- PTM: RNA-binding phosphoprotein p12 is phosphorylated on serine
CC residues. {ECO:0000250}.
CC -!- CAUTION: Originally thought to be characterized from prostate tumors,
CC the described gammaretrovirus XMRV is in fact laboratory-derived and
CC there is no association of XMRV with prostate cancer.
CC {ECO:0000305|PubMed:16609730, ECO:0000305|PubMed:23028303}.
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DR EMBL; DQ399707; ABD49686.1; -; Genomic_RNA.
DR EMBL; EF185282; ABM47427.1; -; Genomic_RNA.
DR SMR; Q27ID9; -.
DR ELM; Q27ID9; -.
DR Proteomes; UP000002240; Genome.
DR Proteomes; UP000180675; Genome.
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: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; Reference proteome; RNA-binding;
KW Viral budding; Viral budding via the host ESCRT complexes;
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..536
FT /note="Gag polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000390845"
FT CHAIN 2..129
FT /note="Matrix protein p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390846"
FT CHAIN 130..213
FT /note="RNA-binding phosphoprotein p12"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390847"
FT CHAIN 214..476
FT /note="Capsid protein p30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390848"
FT CHAIN 477..536
FT /note="Nucleocapsid protein p10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000390849"
FT ZN_FING 500..517
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 108..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..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 MOTIF 128..132
FT /note="LYPX(n)L motif"
FT MOTIF 161..164
FT /note="PPXY motif"
FT COMPBIAS 108..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
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 MOD_RES 190
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 536 AA; 60446 MW; 63CD1FB1561E0836 CRC64;
MGQTVTTPLS LTLQHWGDVQ RIASNQSVDV KKRRWVTFCS AEWPTFNVGW PQDGTFNLGV
ISQVKSRVFC PGPHGHPDQV PYIVTWEALA YDPPPWVKPF VSPKPPPLPT APVLPPGPSA
QPPSRSALYP ALTPSIKSKP PKPQVLPDSG GPLIDLLTED PPPYGAQPSS SARENNEEEA
ATTSEVSPPS PMVSRLRGRR DPPAADSTTS QAFPLRMGGD GQLQYWPFSS SDLYNWKNNN
PSFSEDPGKL TALIESVLIT HQPTWDDCQQ LLGTLLTGEE KQRVLLEARK AVRGNDGRPT
QLPNEVNAAF PLERPDWDYT TTEGRNHLVL YRQLLLAGLQ NAGRSPTNLA KVKGITQGPN
ESPSAFLERL KEAYRRYTPY DPEDPGQETN VSMSFIWQSA PDIGRKLERL EDLKSKTLGD
LVREAEKIFN KRETPEEREE RIRREIEEKE ERRRAEDEQR ERERDRRRHR EMSKLLATVV
IGQRQDRQGG ERRRPQLDKD QCAYCKEKGH WAKDCPKKPR GPRGPRPQTS LLTLGD
