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   08-NOV-2023, entry version 108.
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;
OC   Mammarenavirus lassaense.
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   INTERACTION WITH HOST TAX1BP1.
RX   PubMed=30909570; DOI=10.3390/v11030293;
RA   Baillet N., Krieger S., Journeaux A., Caro V., Tangy F., Vidalain P.O.,
RA   Baize S.;
RT   "Autophagy Promotes Infectious Particle Production of Mopeia and Lassa
RT   Viruses.";
RL   Viruses 11:0-0(2019).
RN   [10]
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. Interacts with
CC       host TAX1BP1 (PubMed:30909570). {ECO:0000255|HAMAP-Rule:MF_04087,
CC       ECO:0000269|PubMed:15019244, ECO:0000269|PubMed:16571837,
CC       ECO:0000269|PubMed:20212144, 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.
DR   SUPFAM; SSF57850; RING/U-box; 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
//