AC   MF_04087;
DC   Protein; auto
TR   HAMAP; MF_04087; -; 1; level=0
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Names: ARENA_Z
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ID   Z
DE   RecName: Full=RING finger protein Z;
DE            Short=Protein Z;
DE   AltName: Full=Zinc-binding protein;
GN   Name=Z;
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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.
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, Z partially blocks the product exit tunnel for the
CC       releasing nascent RNA product. Interacts with the glycoprotein complex;
CC       this interaction plays a role in virion budding. Interacts with host
CC       eIF4E; this interaction results in eIF4E reduced affinity for its
CC       substrate, the 5'-m7 G cap structure. Interacts (via late-budding
CC       domain) with host TSG101; this interaction is essential for budding and
CC       release of viral particles. Interacts with host RPLP0; this interaction
CC       may serve to load ribosome-like particles inside the virion. Interacts
CC       with host PML; this interaction induces PML bodies redistribution in
CC       the cytoplasm upon viral infection.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm, host perinuclear region.
CC       Host cell membrane; Lipid-anchor; Cytoplasmic side. Note=Mainly
CC       perinuclear. During budding, associates at the inner side of the plasma
CC       membrane of infected cells.
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.
CC   -!- PTM: Myristoylation is required for the role of RING finger protein Z
CC       in assembly and budding.
CC   -!- SIMILARITY: Belongs to the arenaviridae Z protein family.
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DR   Pfam; PF03854; zf-P11; 1; trigger=no
DR   PIRSF; PIRSF004030; Z_ArenaV; 1; trigger=no
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KW   Host cell membrane
KW   Host cytoplasm
KW   Host membrane
KW   Host-virus interaction
KW   Lipoprotein
KW   Membrane
KW   Metal-binding
KW   Myristate
KW   Viral budding
KW   Viral budding via the host ESCRT complexes
KW   Viral release from host cell
KW   Virion
KW   Zinc
KW   Zinc-finger
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GO   GO:0044220; C:host cell perinuclear region of cytoplasm
GO   GO:0020002; C:host cell plasma membrane
GO   GO:0016020; C:membrane
GO   GO:0044423; C:virion component
GO   GO:0003723; F:RNA binding
GO   GO:0008270; F:zinc ion binding
GO   GO:0046761; P:viral budding from plasma membrane
GO   GO:0039702; P:viral budding via host ESCRT complex
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FT   From: Z_LASSJ (O73557)
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT   Condition: M
FT   CHAIN           2..Cter
FT                   /note="RING finger protein Z"
FT   ZN_FING         31..67
FT                   /note="RING-type; atypical"
FT   Condition: C-x-x-C-x*-C-x-x-C
FT   MOTIF           81..84
FT                   /note="PTAP/PSAP motif"
FT   Condition: P-[TS]-A-P
FT   MOTIF           94..97
FT                   /note="PPXY motif"
FT   Condition: P-P-P-Y
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT   Condition: G
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Size: 90-101;
Related: None;
Template: O73557;
Scope:
 Viruses; Arenaviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Version: 6
# Last updated date: 2025-02-11
# Created date: 2018-02-08
//