Z_LYCVT
ID Z_LYCVT Reviewed; 72 AA.
AC P19325;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 89.
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 Traub) (LCMV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11626;
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; P19325; -.
DR PRIDE; P19325; -.
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; Myristate; Virion; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255"
FT CHAIN 2..>72
FT /note="RING finger protein Z"
FT /id="PRO_0000079204"
FT ZN_FING 32..68
FT /note="RING-type; atypical"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT NON_TER 72
SQ SEQUENCE 72 AA; 8184 MW; F94E801714ADA87B CRC64;
MGQSKSKEEK GISGTSRAEI LPDTTYLGPL NCKSCWQKFD SFSKCHDHYL CRHCLNLLLT
SSDRCPLCKY PL
