AC MF_04087; DC Protein; auto TR HAMAP; MF_04087; -; 1; level=0 XX Names: ARENA_Z XX ID Z DE RecName: Full=RING finger protein Z; DE Short=Protein Z; DE AltName: Full=Zinc-binding protein; GN Name=Z; XX 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. 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. 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 -!- SIMILARITY: Belongs to the arenaviridae Z protein family. XX DR Pfam; PF03854; zf-P11; 1; trigger=no DR PIRSF; PIRSF004030; Z_ArenaV; 1; trigger=no XX 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 XX 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 XX 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 XX Size: 90-101; Related: None; Template: O73557; Scope: Viruses; Arenaviridae Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.4 2021/06/04 //