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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: 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 similarity2 Publications

Regions

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

GO - Molecular functioni

GO - Biological processi

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
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 host
ChainiPRO_00000792012 – 99RING finger protein ZAdd BLAST98

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 similarity4 Publications

Protein-protein interaction databases

DIPiDIP-58625N.
ELMiO73557.

Structurei

Secondary structure

199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 31Combined sources4
Turni32 – 34Combined sources3
Beta strandi39 – 43Combined sources5
Beta strandi45 – 50Combined sources6
Helixi51 – 60Combined sources10
Beta strandi61 – 64Combined sources4
Turni65 – 67Combined sources3
Beta strandi68 – 70Combined sources3

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...

Miscellaneous databases

EvolutionaryTraceiO73557.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi81 – 84PTAP/PSAP motif4
Motifi94 – 97PPXY motif4

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. Ring-finger protein Z contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and 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 fingeri31 – 67RING-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.

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

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: August 30, 2017
This is version 88 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families