Z_LASSJ
ID Z_LASSJ Reviewed; 99 AA.
AC O73557;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=RING finger protein Z {ECO:0000255|HAMAP-Rule:MF_04087};
DE Short=Protein Z {ECO:0000255|HAMAP-Rule:MF_04087};
DE AltName: Full=Zinc-binding protein {ECO:0000255|HAMAP-Rule:MF_04087};
GN Name=Z {ECO:0000255|HAMAP-Rule:MF_04087};
OS Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11622;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10112; Mastomys natalensis (African soft-furred rat) (Praomys natalensis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9281522; DOI=10.1006/viro.1997.8722;
RA Djavani M., Lukashevich I.S., Sanchez A., Nichol S.T., Salvato M.S.;
RT "Completion of the Lassa fever virus sequence and identification of a RING
RT finger open reading frame at the L RNA 5' End.";
RL Virology 235:414-418(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Hajjaj A., Chain P.S.G., Do L.H., Smith K.L., Imbro P.M., Malfatti S.A.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH HUMAN PML.
RX PubMed=9420283; DOI=10.1128/jvi.72.1.758-766.1998;
RA Borden K.L., Campbell-Dwyer E.J., Salvato M.S.;
RT "An arenavirus RING (zinc-binding) protein binds the oncoprotein
RT promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the
RT cytoplasm.";
RL J. Virol. 72:758-766(1998).
RN [4]
RP LATE-BUDDING DOMAIN, FUNCTION, AND MUTAGENESIS OF 81-PRO--PRO-84 AND
RP 94-PRO--PRO-97.
RX PubMed=12970458; DOI=10.1128/jvi.77.19.10700-10705.2003;
RA Strecker T., Eichler R., Meulen J., Weissenhorn W., Dieter Klenk H.,
RA Garten W., Lenz O.;
RT "Lassa virus Z protein is a matrix protein and sufficient for the release
RT of virus-like particles.";
RL J. Virol. 77:10700-10705(2003).
RN [5]
RP FUNCTION.
RX PubMed=14990716; DOI=10.1128/jvi.78.6.2979-2983.2004;
RA Cornu T.I., Feldmann H., de la Torre J.C.;
RT "Cells expressing the RING finger Z protein are resistant to arenavirus
RT infection.";
RL J. Virol. 78:2979-2983(2004).
RN [6]
RP INTERACTION WITH NP.
RX PubMed=15019244; DOI=10.1016/j.virusres.2003.11.017;
RA Eichler R., Strecker T., Kolesnikova L., ter Meulen J., Weissenhorn W.,
RA Becker S., Klenk H.D., Garten W., Lenz O.;
RT "Characterization of the Lassa virus matrix protein Z: electron microscopic
RT study of virus-like particles and interaction with the nucleoprotein
RT (NP).";
RL Virus Res. 100:249-255(2004).
RN [7]
RP MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=15452271; DOI=10.1128/jvi.78.20.11443-11448.2004;
RA Perez M., Greenwald D.L., de la Torre J.C.;
RT "Myristoylation of the RING finger Z protein is essential for arenavirus
RT budding.";
RL J. Virol. 78:11443-11448(2004).
RN [8]
RP LATE-BUDDING DOMAIN, AND INTERACTION WITH HUMAN TSG101.
RX PubMed=16571837; DOI=10.1128/jvi.80.8.4191-4195.2006;
RA Urata S., Noda T., Kawaoka Y., Yokosawa H., Yasuda J.;
RT "Cellular factors required for Lassa virus budding.";
RL J. Virol. 80:4191-4195(2006).
RN [9]
RP STRUCTURE BY NMR IN COMPLEX WITH ZINC IONS, AND INTERACTION WITH HOST
RP EIF4E.
RX PubMed=20212144; DOI=10.1073/pnas.0909877107;
RA Volpon L., Osborne M.J., Capul A.A., de la Torre J.C., Borden K.L.;
RT "Structural characterization of the Z RING-eIF4E complex reveals a distinct
RT mode of control for eIF4E.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5441-5446(2010).
CC -!- FUNCTION: Plays a crucial role in virion assembly and budding.
CC Expressed late in the virus life cycle, it acts as an inhibitor of
CC viral transcription and RNA synthesis by interacting with the viral
CC polymerase L. Presumably recruits the NP encapsidated genome to
CC cellular membranes at budding sites via direct interaction with NP.
CC Plays critical roles in the final steps of viral release by interacting
CC with host TSG101, a member of the vacuolar protein-sorting pathway and
CC using other cellular host proteins involved in vesicle formation
CC pathway. The budding of the virus progeny occurs after association of
CC protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell
CC periphery, step that requires myristoylation of protein Z. Also
CC selectively represses protein production by associating with host
CC eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087, ECO:0000269|PubMed:12970458,
CC ECO:0000269|PubMed:14990716}.
CC -!- SUBUNIT: Interacts with protein NP; this interaction probably directs
CC the encapsidated genome to budding sites (By similarity). Interacts
CC (via RING domain) with polymerase L; this interaction inhibits viral
CC transcription and replication (By similarity). Interacts with the
CC glycoprotein complex; this interaction plays a role in virion budding.
CC Interacts with host eIF4E; this interaction results in eIF4E reduced
CC affinity for its substrate, the 5'-m7 G cap structure. Interacts (via
CC late-budding domain) with host TSG101; this interaction is essential
CC for budding and release of viral particles. Interacts with host RPLP0;
CC this interaction may serve to load ribosome-like particles inside the
CC virion. Interacts with host PML; this interaction induces PML bodies
CC redistribution in the cytoplasm upon viral infection.
CC {ECO:0000255|HAMAP-Rule:MF_04087, ECO:0000269|PubMed:15019244,
CC ECO:0000269|PubMed:16571837, ECO:0000269|PubMed:20212144,
CC ECO:0000269|PubMed:9420283}.
CC -!- INTERACTION:
CC O73557; P06730: EIF4E; Xeno; NbExp=3; IntAct=EBI-15840965, EBI-73440;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host
CC cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}.
CC Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at
CC the inner side of the plasma membrane of infected cells.
CC {ECO:0000255|HAMAP-Rule:MF_04087}.
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. {ECO:0000255|HAMAP-Rule:MF_04087}.
CC -!- SIMILARITY: Belongs to the arenaviridae Z protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04087}.
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DR EMBL; U73035; AAC05818.2; -; Genomic_RNA.
DR EMBL; U73034; AAC05816.2; -; Genomic_RNA.
DR EMBL; AY628202; AAT49001.1; -; Genomic_RNA.
DR RefSeq; NP_694871.1; NC_004297.1.
DR PDB; 2M1S; NMR; -; A=1-99.
DR PDB; 5I72; X-ray; 2.90 A; A/B=25-77.
DR PDBsum; 2M1S; -.
DR PDBsum; 5I72; -.
DR BMRB; O73557; -.
DR SMR; O73557; -.
DR DIP; DIP-58625N; -.
DR ELM; O73557; -.
DR IntAct; O73557; 1.
DR iPTMnet; O73557; -.
DR GeneID; 956586; -.
DR KEGG; vg:956586; -.
DR EvolutionaryTrace; O73557; -.
DR Proteomes; UP000002473; Genome.
DR Proteomes; UP000162624; Genome.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-UniRule.
DR DisProt; DP00820; -.
DR Gene3D; 3.30.160.310; -; 1.
DR HAMAP; MF_04087; ARENA_Z; 1.
DR InterPro; IPR024183; RING_finger_Z_arenaviridae.
DR InterPro; IPR038485; Z_RING-type_Znf_sf.
DR InterPro; IPR003224; Z_RING_Znf.
DR Pfam; PF03854; zf-P11; 1.
DR PIRSF; PIRSF004030; Z_ArenaV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host cytoplasm; Host membrane;
KW Host-virus interaction; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral release from host cell;
KW Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT CHAIN 2..99
FT /note="RING finger protein Z"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT /id="PRO_0000079201"
FT ZN_FING 31..67
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT REGION 74..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..84
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT MOTIF 94..97
FT /note="PPXY motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087,
FT ECO:0000269|PubMed:15452271"
FT MUTAGEN 2
FT /note="G->A: Complete loss of myristoylation. Complete loss
FT of virion budding."
FT /evidence="ECO:0000269|PubMed:12970458,
FT ECO:0000269|PubMed:15452271"
FT MUTAGEN 81..84
FT /note="PTAP->ATAA: 50% decrease of virus budding."
FT /evidence="ECO:0000269|PubMed:12970458"
FT MUTAGEN 94..97
FT /note="PPPY->AAAA: 90% decrease of virus budding."
FT /evidence="ECO:0000269|PubMed:12970458"
FT MUTAGEN 97
FT /note="Y->A: 90% decrease of virus budding."
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:5I72"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5I72"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:5I72"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:5I72"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:5I72"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2M1S"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:5I72"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5I72"
SQ SEQUENCE 99 AA; 10675 MW; F68877962B65F045 CRC64;
MGNKQAKAPE SKDSPRASLI PDATHLGPQF CKSCWFENKG LVECNNHYLC LNCLTLLLSV
SNRCPICKMP LPTKLRPSAA PTAPPTGAAD SIRPPPYSP
