Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

RING finger protein Z



Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV)
Reviewed-Annotation score: -Experimental evidence at protein leveli


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. 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.UniRule annotation1 Publication


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri32 – 68RING-type; atypicalUniRule annotationAdd BLAST37

GO - Molecular functioni

GO - Biological processi

  • viral budding from plasma membrane Source: UniProtKB
  • viral budding via host ESCRT complex Source: UniProtKB-KW


Biological processHost-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Viral release from host cell
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
RING finger protein ZUniRule annotation
Short name:
Protein ZUniRule annotation
Alternative name(s):
Zinc-binding proteinUniRule annotation
Gene namesi
Name:ZUniRule annotation
Ordered Locus Names:Segment L
OrganismiLymphocytic choriomeningitis virus (strain Armstrong) (LCMV)
Taxonomic identifieri11624 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesArenaviridaeMammarenavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mesocricetus auratus (Golden hamster) [TaxID: 10036]
Mus musculus (Mouse) [TaxID: 10090]
  • UP000121528 Componenti: Genome
  • UP000002474 Componenti: Genome

Subcellular locationi

  • Virion UniRule annotation
  • host perinuclear region UniRule annotation
  • Host cell membrane UniRule annotation; Lipid-anchor UniRule annotation; Cytoplasmic side UniRule annotation
  • Note: Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells.UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host membrane, Membrane, Virion

Pathology & Biotechi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Complete loss of myristoylation. Complete loss of virion budding. 1 Publication1
Mutagenesisi32C → F: Complete loss of inhibitory activity on viral RNA synthesis; when associated with G-35. 1 Publication1
Mutagenesisi35C → G: Complete loss of inhibitory activity on viral RNA synthesis; when associated with F-32. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostUniRule annotation
ChainiPRO_00000792022 – 90RING finger protein ZUniRule annotationAdd BLAST89

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostUniRule annotation1 Publication1

Keywords - PTMi

Lipoprotein, Myristate

PTM databases



Subunit structurei

Interacts with protein NP; this interaction probably directs the encapsidated genome to budding sites. Interacts (via RING domain) with polymerase L; this interaction inhibits viral transcription and replication. Interacts with the glycoprotein complex; this interaction plays a role in virion budding. Interacts with host eIF4E; this interaction results in eIF4E reduced affinity for its substrate, the 5'-m7 G cap structure. Interacts (via late-budding domain) with host TSG101; this interaction is essential for budding and release of viral particles. Interacts with host RPLP0; this interaction may serve to load ribosome-like particles inside the virion. Interacts with host PML; this interaction induces PML bodies redistribution in the cytoplasm upon viral infection.UniRule annotation3 Publications

Protein-protein interaction databases

IntActiP18541, 1 interactor


3D structure databases


Family & Domainsi


Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi85 – 88PPXY motif4


The RING finger domain is essential for the inhibitory activity of protein Z in transcription and RNA replication.
Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins.UniRule annotation

Sequence similaritiesi

Belongs to the arenaviridae Z protein family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri32 – 68RING-type; atypicalUniRule annotationAdd BLAST37

Keywords - Domaini


Phylogenomic databases


Family and domain databases

Gene3Di3.30.160.310, 1 hit
HAMAPiMF_04087 ARENA_Z, 1 hit
InterProiView protein in InterPro
IPR024183 RING_finger_Z_arenaviridae
IPR038485 Z_RING-type_Znf_sf
IPR003224 Z_RING_Znf
PfamiView protein in Pfam
PF03854 zf-P11, 1 hit
PIRSFiPIRSF004030 Z_ArenaV, 1 hit


Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18541-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
60 70 80 90
Mass (Da):10,184
Last modified:January 23, 2007 - v3

Sequence databases

Select the link destinations:
Links Updated
M27693 Genomic RNA Translation: AAA46268.1
AY847351 Genomic RNA Translation: AAX49343.1
DQ361066 Genomic RNA Translation: ABC96003.1

Similar proteinsi

Entry informationi

Entry nameiZ_LYCVA
AccessioniPrimary (citable) accession number: P18541
Secondary accession number(s): Q49K85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 95 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program


Keywords - Technical termi

Complete proteome, Reference proteome


  1. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health