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O73557

- Z_LASSJ

UniProt

O73557 - Z_LASSJ

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
  1. 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)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri31 – 6737RING-type; atypicalAdd
    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

    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

    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. 2 Publications
    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. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by host
    Chaini2 – 9998RING finger protein ZPRO_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.By similarity4 Publications

    Protein-protein interaction databases

    DIPiDIP-58625N.

    Structurei

    Secondary structure

    1
    99
    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[»]
    ModBaseiSearch...
    MobiDBiSearch...

    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.By similarity

    Sequence similaritiesi

    Belongs to the arenaviridae Z protein family.Curated
    Contains 1 RING-type zinc finger.Curated

    Zinc finger

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

    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: October 1, 2014
    This is version 77 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