Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-11622-00636
Entry Name
UniProt Accession
Theoretical PI
8.95
Molecular Weight
10675.43
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
RING finger protein Z
Protein Synonyms/Alias
Protein Z; Zinc-binding protein;
Gene Name
Z
Gene Synonyms/Alias
Created Date
06-DEC-2005
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNKQAKAP
[1]
N-Myristoylation
Organism
Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
NCBI Taxa ID
11622
Reference
[1] Perez M, Greenwald DL, de la Torre JC. Myristoylation of the RING finger Zprotein is essential for arenavirus budding. J Virol. 2004 Oct;78(20):11443-8.[PMID:15452271]
Functional Description
Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L (By similarity). Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E.
Sequence Annotation
Motif: 81 84 PTAP/PSAP motif.
Motif: 94 97 PPXY motif.
Protein Length
99 AA.
Protein Sequence
(Canonical)
MGNKQAKAPE SKDSPRASLI PDATHLGPQF CKSCWFENKG LVECNNHYLC LNCLTLLLSV  60
SNRCPICKMP LPTKLRPSAA PTAPPTGAAD SIRPPPYSP                         99
FASTA
(Canonical)
>LipidDB-11622-00636|O73557
MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSV
SNRCPICKMPLPTKLRPSAAPTAPPTGAADSIRPPPYSP
Gene Ontology
GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0019012; C:virion; IEA:UniProtKB-KW
GO:0003723; F:RNA binding; IEA:InterPro
GO:0008270; F:zinc ion binding; IEA:InterPro
GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW
GO:0019076; P:viral release from host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR024183; RING_finger_Z_arenaviridae
InterPro; IPR003224; Znf_P11
InterPro; IPR013083; Znf_RING/FYVE/PHD
Pfam
Pfam; PF03854; zf-P11;
SMART
PROSITE
PRINTS