ID   Z_LYCVP                 Reviewed;          51 AA.
AC   P19326;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   29-SEP-2021, entry version 85.
DE   RecName: Full=RING finger protein Z;
DE            Short=Protein Z;
DE   AltName: Full=Zinc-binding protein;
DE   Flags: Fragment;
GN   Name=Z;
OS   Lymphocytic choriomeningitis virus (strain Pasteur) (LCMV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX   NCBI_TaxID=11625;
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).
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. The
CC       budding of the virus progeny occurs after association of protein Z with
CC       the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step
CC       that requires myristoylation of protein Z (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with protein N; 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.
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 (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The RING finger domain is essential for the inhibitory activity
CC       of protein Z in transcription and RNA replication. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the arenaviridae Z protein family.
CC       {ECO:0000305}.
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DR   SMR; P19326; -.
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-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.160.310; -; 1.
DR   InterPro; IPR038485; Z_RING-type_Znf_sf.
DR   InterPro; IPR003224; Z_RING_Znf.
DR   Pfam; PF03854; zf-P11; 1.
PE   3: Inferred from homology;
KW   Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW   Lipoprotein; Membrane; Metal-binding; Virion; Zinc; Zinc-finger.
FT   CHAIN           <1..>51
FT                   /note="RING finger protein Z"
FT                   /id="PRO_0000079203"
FT   ZN_FING         11..47
FT                   /note="RING-type; atypical"
FT   NON_TER         1
FT   NON_TER         51
SQ   SEQUENCE   51 AA;  5972 MW;  1B2E383153CD8582 CRC64;
     PDTTYLGPLN CKSCWQKFDS LVRCHDHYLC RHCLNLLLTS SDRCPLCKYP L