Z_LYCVA
ID Z_LYCVA Reviewed; 90 AA.
AC P18541; Q49K85;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
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}; OrderedLocusNames=Segment L;
OS Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11624;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10036; Mesocricetus auratus (Golden hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2510401; DOI=10.1016/0042-6822(89)90216-x;
RA Salvato M.S., Shimomaye E.M.;
RT "The completed sequence of lymphocytic choriomeningitis virus reveals a
RT unique RNA structure and a gene for a zinc finger protein.";
RL Virology 173:1-10(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Armstrong 53b;
RX PubMed=16051837; DOI=10.1128/jvi.79.16.10451-10459.2005;
RA Grande-Perez A., Gomez-Mariano G., Lowenstein P.R., Domingo E.;
RT "Mutagenesis-induced, large fitness variations with an invariant arenavirus
RT consensus genomic nucleotide sequence.";
RL J. Virol. 79:10451-10459(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Armstrong-derived variant Cl13;
RX PubMed=16537369; DOI=10.1073/pnas.0600652103;
RA Flatz L., Bergthaler A., de la Torre J.C., Pinschewer D.D.;
RT "Recovery of an arenavirus entirely from RNA polymerase I/II-driven cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4663-4668(2006).
RN [4]
RP INTERACTION WITH HOST RPLP0 AND HOST PML.
RX PubMed=9557665; DOI=10.1128/jvi.72.5.3819-3826.1998;
RA Borden K.L., Campbell-Dwyer E.J., Carlile G.W., Djavani M., Salvato M.S.;
RT "Two RING finger proteins, the oncoprotein PML and the arenavirus Z
RT protein, colocalize with the nuclear fraction of the ribosomal P
RT proteins.";
RL J. Virol. 72:3819-3826(1998).
RN [5]
RP INTERACTION WITH HOST EIF4E.
RX PubMed=10708446; DOI=10.1128/jvi.74.7.3293-3300.2000;
RA Campbell-Dwyer E.J., Lai H., MacDonald R.C., Salvato M.S., Borden K.L.;
RT "The lymphocytic choriomeningitis virus RING protein Z associates with
RT eukaryotic initiation factor 4E and selectively represses translation in a
RT RING-dependent manner.";
RL J. Virol. 74:3293-3300(2000).
RN [6]
RP MUTAGENESIS OF CYS-32 AND CYS-35.
RX PubMed=11533204; DOI=10.1128/jvi.75.19.9415-9426.2001;
RA Cornu T.I., de la Torre J.C.;
RT "RING finger Z protein of lymphocytic choriomeningitis virus (LCMV)
RT inhibits transcription and RNA replication of an LCMV S-segment
RT minigenome.";
RL J. Virol. 75:9415-9426(2001).
RN [7]
RP FUNCTION.
RX PubMed=12050381; DOI=10.1128/jvi.76.13.6678-6688.2002;
RA Cornu T.I., de la Torre J.C.;
RT "Characterization of the arenavirus RING finger Z protein regions required
RT for Z-mediated inhibition of viral RNA synthesis.";
RL J. Virol. 76:6678-6688(2002).
RN [8]
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 [9]
RP INTERACTION WITH GLYCOPROTEIN COMPLEX GPC.
RX PubMed=17581989; DOI=10.1128/jvi.00499-07;
RA Capul A.A., Perez M., Burke E., Kunz S., Buchmeier M.J., de la Torre J.C.;
RT "Arenavirus Z-glycoprotein association requires Z myristoylation but not
RT functional RING or late domains.";
RL J. Virol. 81:9451-9460(2007).
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:12050381}.
CC -!- SUBUNIT: Interacts with protein NP; this interaction probably directs
CC the encapsidated genome to budding sites. Interacts (via RING domain)
CC with polymerase L; this interaction inhibits viral transcription and
CC replication. Interacts with the glycoprotein complex; this interaction
CC plays a role in virion budding. Interacts with host eIF4E; this
CC interaction results in eIF4E reduced affinity for its substrate, the
CC 5'-m7 G cap structure. Interacts (via late-budding domain) with host
CC TSG101; this interaction is essential for budding and release of viral
CC particles. Interacts with host RPLP0; this interaction may serve to
CC load ribosome-like particles inside the virion. Interacts with host
CC PML; this interaction induces PML bodies redistribution in the
CC cytoplasm upon viral infection. {ECO:0000255|HAMAP-Rule:MF_04087,
CC ECO:0000269|PubMed:10708446, ECO:0000269|PubMed:17581989,
CC ECO:0000269|PubMed:9557665}.
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: The RING finger domain is essential for the inhibitory activity
CC of protein Z in transcription and RNA replication.
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; M27693; AAA46268.1; -; Genomic_RNA.
DR EMBL; AY847351; AAX49343.1; -; Genomic_RNA.
DR EMBL; DQ361066; ABC96003.1; -; Genomic_RNA.
DR PIR; A32592; ZNXPLC.
DR SMR; P18541; -.
DR DIP; DIP-59720N; -.
DR ELM; P18541; -.
DR IntAct; P18541; 1.
DR iPTMnet; P18541; -.
DR Proteomes; UP000002474; Genome.
DR Proteomes; UP000121528; 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 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 Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Reference proteome;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral release from host cell; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT CHAIN 2..90
FT /note="RING finger protein Z"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT /id="PRO_0000079202"
FT ZN_FING 32..68
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT MOTIF 85..88
FT /note="PPXY motif"
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:15452271"
FT MUTAGEN 32
FT /note="C->F: Complete loss of inhibitory activity on viral
FT RNA synthesis; when associated with G-35."
FT /evidence="ECO:0000269|PubMed:11533204"
FT MUTAGEN 35
FT /note="C->G: Complete loss of inhibitory activity on viral
FT RNA synthesis; when associated with F-32."
FT /evidence="ECO:0000269|PubMed:11533204"
SQ SEQUENCE 90 AA; 10184 MW; D25AF9EC2287E4EA CRC64;
MGQGKSREEK GTNSTNRAEI LPDTTYLGPL SCKSCWQKFD SLVRCHDHYL CRHCLNLLLS
VSDRCPLCKY PLPTRLKIST APSSPPPYEE
