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O73557 (Z_LASSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
RING finger protein Z

Short name=Protein Z
Alternative name(s):
Zinc-binding protein
Gene names
Name:Z
OrganismLassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV) [Reference proteome]
Taxonomic identifier11622 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesArenaviridaeArenavirusOld world arenaviruses
Virus hostHomo sapiens (Human) [TaxID: 9606]
Mastomys natalensis (African soft-furred rat) (Praomys natalensis) [TaxID: 10112]

Protein attributes

Sequence length99 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5

Subunit structure

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. Ref.3 Ref.6 Ref.8 Ref.9

Subcellular location

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

Domain

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. Ref.4 Ref.8

Sequence similarities

Belongs to the arenaviridae Z protein family.

Contains 1 RING-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host
Chain2 – 9998RING finger protein Z
PRO_0000079201

Regions

Zinc finger31 – 6737RING-type; atypical
Motif81 – 844PTAP/PSAP motif
Motif94 – 974PPXY motif

Amino acid modifications

Lipidation21N-myristoyl glycine; by host Ref.7

Experimental info

Mutagenesis21G → A: Complete loss of myristoylation. Complete loss of virion budding. Ref.7
Mutagenesis81 – 844PTAP → ATAA: 50% decrease of virus budding. Ref.4
Mutagenesis94 – 974PPPY → AAAA: 90% decrease of virus budding. Ref.4
Mutagenesis971Y → A: 90% decrease of virus budding.

Secondary structure

......... 99
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O73557 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: F68877962B65F045

FASTA9910,675
        10         20         30         40         50         60 
MGNKQAKAPE SKDSPRASLI PDATHLGPQF CKSCWFENKG LVECNNHYLC LNCLTLLLSV 

        70         80         90 
SNRCPICKMP LPTKLRPSAA PTAPPTGAAD SIRPPPYSP 

« Hide

References

[1]"Completion of the Lassa fever virus sequence and identification of a RING finger open reading frame at the L RNA 5' End."
Djavani M., Lukashevich I.S., Sanchez A., Nichol S.T., Salvato M.S.
Virology 235:414-418(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]Hajjaj A., Chain P.S.G., Do L.H., Smith K.L., Imbro P.M., Malfatti S.A.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"An arenavirus RING (zinc-binding) protein binds the oncoprotein promyelocyte leukemia protein (PML) and relocates PML nuclear bodies to the cytoplasm."
Borden K.L., Campbell-Dwyer E.J., Salvato M.S.
J. Virol. 72:758-766(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN PML.
[4]"Lassa virus Z protein is a matrix protein and sufficient for the release of virus-like particles."
Strecker T., Eichler R., Meulen J., Weissenhorn W., Dieter Klenk H., Garten W., Lenz O.
J. Virol. 77:10700-10705(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LATE-BUDDING DOMAIN, FUNCTION, MUTAGENESIS OF 81-PRO--PRO-84 AND 94-PRO--PRO-97.
[5]"Cells expressing the RING finger Z protein are resistant to arenavirus infection."
Cornu T.I., Feldmann H., de la Torre J.C.
J. Virol. 78:2979-2983(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Characterization of the Lassa virus matrix protein Z: electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP)."
Eichler R., Strecker T., Kolesnikova L., ter Meulen J., Weissenhorn W., Becker S., Klenk H.D., Garten W., Lenz O.
Virus Res. 100:249-255(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NP.
[7]"Myristoylation of the RING finger Z protein is essential for arenavirus budding."
Perez M., Greenwald D.L., de la Torre J.C.
J. Virol. 78:11443-11448(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2.
[8]"Cellular factors required for Lassa virus budding."
Urata S., Noda T., Kawaoka Y., Yokosawa H., Yasuda J.
J. Virol. 80:4191-4195(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: LATE-BUDDING DOMAIN, INTERACTION WITH HUMAN TSG101.
[9]"Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E."
Volpon L., Osborne M.J., Capul A.A., de la Torre J.C., Borden K.L.
Proc. Natl. Acad. Sci. U.S.A. 107:5441-5446(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH ZINC IONS, INTERACTION WITH HOST EIF4E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73035 Genomic RNA. Translation: AAC05818.2.
U73034 Genomic RNA. Translation: AAC05816.2.
AY628202 Genomic RNA. Translation: AAT49001.1.
RefSeqNP_694871.1. NC_004297.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M1SNMR-A1-99[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-58625N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956586.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR024183. RING_finger_Z_arenaviridae.
IPR003224. Znf_P11.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF03854. zf-P11. 1 hit.
[Graphical view]
PIRSFPIRSF004030. Z_ArenaV. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO73557.

Entry information

Entry nameZ_LASSJ
AccessionPrimary (citable) accession number: O73557
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 76 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references