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Protein

RING finger protein Z

Gene

Z

Organism
Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
Status
Reviewed-Annotation score: -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. 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 annotation2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 67RING-type; atypicalUniRule annotationAdd BLAST37

GO - Molecular functioni

GO - Biological processi

Keywordsi

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
OrganismiLassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
Taxonomic identifieri11622 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesArenaviridaeMammarenavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mastomys natalensis (African soft-furred rat) (Praomys natalensis) [TaxID: 10112]
Proteomesi
  • UP000002473 Componenti: Genome
  • UP000162624 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. 2 Publications1
Mutagenesisi81 – 84PTAP → ATAA: 50% decrease of virus budding. 1 Publication4
Mutagenesisi94 – 97PPPY → AAAA: 90% decrease of virus budding. 1 Publication4
Mutagenesisi97Y → A: 90% decrease of virus budding. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostUniRule annotation
ChainiPRO_00000792012 – 99RING finger protein ZUniRule annotationAdd BLAST98

Amino acid modifications

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

Keywords - PTMi

Lipoprotein, Myristate

PTM databases

iPTMnetiO73557

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.UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF4EP067303EBI-15840965,EBI-73440From Homo sapiens.

Protein-protein interaction databases

DIPiDIP-58625N
ELMiO73557
IntActiO73557, 1 interactor

Structurei

Secondary structure

199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00820
SMRiO73557
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO73557

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi81 – 84PTAP/PSAP motifUniRule annotation4
Motifi94 – 97PPXY motifUniRule annotation4

Domaini

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 fingeri31 – 67RING-type; atypicalUniRule annotationAdd BLAST37

Keywords - Domaini

Zinc-finger

Phylogenomic databases

OrthoDBiVOG090001O4

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

Sequencei

Sequence statusi: Complete.

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

O73557-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGNKQAKAPE SKDSPRASLI PDATHLGPQF CKSCWFENKG LVECNNHYLC
60 70 80 90
LNCLTLLLSV SNRCPICKMP LPTKLRPSAA PTAPPTGAAD SIRPPPYSP
Length:99
Mass (Da):10,675
Last modified:January 23, 2007 - v4
Checksum:iF68877962B65F045
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73035 Genomic RNA Translation: AAC05818.2
U73034 Genomic RNA Translation: AAC05816.2
AY628202 Genomic RNA Translation: AAT49001.1
RefSeqiNP_694871.1, NC_004297.1

Genome annotation databases

GeneIDi956586
KEGGivg:956586

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73035 Genomic RNA Translation: AAC05818.2
U73034 Genomic RNA Translation: AAC05816.2
AY628202 Genomic RNA Translation: AAT49001.1
RefSeqiNP_694871.1, NC_004297.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M1SNMR-A1-99[»]
5I72X-ray2.90A/B25-77[»]
DisProtiDP00820
SMRiO73557
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58625N
ELMiO73557
IntActiO73557, 1 interactor

PTM databases

iPTMnetiO73557

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi956586
KEGGivg:956586

Phylogenomic databases

OrthoDBiVOG090001O4

Miscellaneous databases

EvolutionaryTraceiO73557

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
ProtoNetiSearch...

Entry informationi

Entry nameiZ_LASSJ
AccessioniPrimary (citable) accession number: O73557
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 92 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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