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Protein

RING finger protein Z

Gene

Z

Organism
Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Regions

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

GO - Molecular functioni

GO - Biological processi

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

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
RING finger protein Z
Short name:
Protein Z
Alternative name(s):
Zinc-binding protein
Gene namesi
Name:Z
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]
Proteomesi
  • UP000121528 Componenti: Genome
  • UP000002474 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

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 host
ChainiPRO_00000792022 – 90RING finger protein ZAdd BLAST89

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by host1 Publication1

Keywords - PTMi

Lipoprotein, Myristate

Interactioni

Subunit structurei

Interacts with protein NP; this interaction probably directs the encapsidated genome to budding sites (By similarity). Interacts (via RING domain) with polymerase L; this interaction inhibits viral transcription and replication (By similarity). 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.By similarity3 Publications

Protein-protein interaction databases

DIPiDIP-59720N.

Structurei

3D structure databases

SMRiP18541.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Domaini

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. Ring-finger protein Z contains one L domain: a PPXY motif which probably binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases (By similarity).By similarity

Sequence similaritiesi

Belongs to the arenaviridae Z protein family.Curated

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

OrthoDBiVOG090001O4.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR024183. RING_finger_Z_arenaviridae.
IPR003224. Znf_P11.
IPR013083. Znf_RING/FYVE/PHD.
PfamiView protein in Pfam
PF03854. zf-P11. 1 hit.
PIRSFiPIRSF004030. Z_ArenaV. 1 hit.

Sequencei

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
MGQGKSREEK GTNSTNRAEI LPDTTYLGPL SCKSCWQKFD SLVRCHDHYL
60 70 80 90
CRHCLNLLLS VSDRCPLCKY PLPTRLKIST APSSPPPYEE
Length:90
Mass (Da):10,184
Last modified:January 23, 2007 - v3
Checksum:iD25AF9EC2287E4EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27693 Genomic RNA. Translation: AAA46268.1.
AY847351 Genomic RNA. Translation: AAX49343.1.
DQ361066 Genomic RNA. Translation: ABC96003.1.
PIRiA32592. ZNXPLC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27693 Genomic RNA. Translation: AAA46268.1.
AY847351 Genomic RNA. Translation: AAX49343.1.
DQ361066 Genomic RNA. Translation: ABC96003.1.
PIRiA32592. ZNXPLC.

3D structure databases

SMRiP18541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59720N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG090001O4.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiView protein in InterPro
IPR024183. RING_finger_Z_arenaviridae.
IPR003224. Znf_P11.
IPR013083. Znf_RING/FYVE/PHD.
PfamiView protein in Pfam
PF03854. zf-P11. 1 hit.
PIRSFiPIRSF004030. Z_ArenaV. 1 hit.
ProtoNetiSearch...

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 15, 2017
This is version 90 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.