Z_CPXVB
ID Z_CPXVB Reviewed; 96 AA.
AC B0BLK9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 Cupixi mammarenavirus (isolate Rat/Brasil/BeAn 119303/1970) (CPXV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=208899;
OH NCBI_TaxID=89099; Hylaeamys megacephalus (Large-headed rice rat) (Oryzomys megacephalus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14698659; DOI=10.1016/j.virol.2003.08.016;
RA Charrel R.N., Lemasson J.J., Garbutt M., Khelifa R., De Micco P.,
RA Feldmann H., de Lamballerie X.;
RT "New insights into the evolutionary relationships between arenaviruses
RT provided by comparative analysis of small and large segment sequences.";
RL Virology 317:191-196(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Emonet S., de Lamballerie X., de Micco P., Charrel R.N.;
RT "Complete sequence determination and analysis of the large RNA segment of
RT arenaviruses.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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 -!- 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.
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DR EMBL; AY216519; ABY59842.1; -; Genomic_RNA.
DR RefSeq; YP_001649219.1; NC_010252.1.
DR GeneID; 5848387; -.
DR KEGG; vg:5848387; -.
DR Proteomes; UP000008164; 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; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW Lipoprotein; Membrane; Metal-binding; Myristate; 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..96
FT /note="RING finger protein Z"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT /id="PRO_0000361030"
FT ZN_FING 41..77
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04087"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..94
FT /note="PTAP/PSAP 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"
SQ SEQUENCE 96 AA; 10981 MW; B005B1F345336857 CRC64;
MGNCRSKQES HPICPNTQTP EPTEAEFRRA AVNSLYGRYN CKCCWFADRN LINCSDHYLC
LRCLNVMLRT SNLCNICWKP LPTRISVPTE PTAPSE
