SubmitCancel

Skip Header

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

O73557

- Z_LASSJ

UniProt

O73557 - Z_LASSJ

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
RING finger protein Z
Gene
Z
Organism
Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
Status
Reviewed - 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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri31 – 6737RING-type; atypical
Add
BLAST

GO - Molecular functioni

  1. RNA binding Source: InterPro
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. viral budding via host ESCRT complex Source: UniProtKB-KW
  2. viral release from host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral budding, Viral budding via the host ESCRT complexes, Virus exit from host cell

Keywords - Ligandi

Metal-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 negative-strand virusesArenaviridaeArenavirusOld world arenaviruses
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mastomys natalensis (African soft-furred rat) (Praomys natalensis) [TaxID: 10112]
ProteomesiUP000002473: Genome

Subcellular locationi

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.

GO - Cellular componenti

  1. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
  2. host cell plasma membrane Source: UniProtKB-SubCell
  3. membrane Source: UniProtKB-KW
  4. virion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Complete loss of myristoylation. Complete loss of virion budding. 1 Publication
Mutagenesisi81 – 844PTAP → ATAA: 50% decrease of virus budding. 1 Publication
Mutagenesisi94 – 974PPPY → AAAA: 90% decrease of virus budding. 1 Publication
Mutagenesisi97 – 971Y → A: 90% decrease of virus budding.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host
Chaini2 – 9998RING finger protein Z
PRO_0000079201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host1 Publication

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.4 Publications

Protein-protein interaction databases

DIPiDIP-58625N.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 435
Beta strandi48 – 503
Helixi51 – 566
Turni57 – 604
Beta strandi61 – 644
Turni65 – 684

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M1SNMR-A1-99[»]

Miscellaneous databases

EvolutionaryTraceiO73557.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi81 – 844PTAP/PSAP motif
Motifi94 – 974PPXY motif

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.2 Publications

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR024183. RING_finger_Z_arenaviridae.
IPR003224. Znf_P11.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF03854. zf-P11. 1 hit.
[Graphical view]
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

MGNKQAKAPE SKDSPRASLI PDATHLGPQF CKSCWFENKG LVECNNHYLC   50
LNCLTLLLSV SNRCPICKMP LPTKLRPSAA PTAPPTGAAD SIRPPPYSP 99
Length:99
Mass (Da):10,675
Last modified:January 23, 2007 - v4
Checksum:iF68877962B65F045
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U73035 Genomic RNA. Translation: AAC05818.2 .
U73034 Genomic RNA. Translation: AAC05816.2 .
AY628202 Genomic RNA. Translation: AAT49001.1 .
RefSeqi NP_694871.1. NC_004297.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M1S NMR - A 1-99 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-58625N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 956586.

Miscellaneous databases

EvolutionaryTracei O73557.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR024183. RING_finger_Z_arenaviridae.
IPR003224. Znf_P11.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF03854. zf-P11. 1 hit.
[Graphical view ]
PIRSFi PIRSF004030. Z_ArenaV. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiZ_LASSJ
AccessioniPrimary (citable) accession number: O73557
Entry historyi
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 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

External Data

Dasty 3

Similar proteinsi