Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q05128

- VP40_EBOZM

UniProt

Q05128 - VP40_EBOZM

Protein

Matrix protein VP40

Gene

VP40

Organism
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Promotes virus assembly and budding by interacting with host proteins of the multivesicular body pathway. May facilitate virus budding by interacting with the nucleocapsid and the plasma membrane. Specific interactions with membrane-associated GP and VP24 during the budding process may also occur. The hexamer form seems to be involved in budding. The octamer form binds RNA, and may play a role in genome replication.2 Publications

    GO - Molecular functioni

    1. RNA binding Source: UniProtKB-KW
    2. structural constituent of virion Source: UniProtKB-KW

    GO - Biological processi

    1. suppression of host defenses Source: CACAO
    2. viral budding from plasma membrane Source: CACAO
    3. viral budding via host ESCRT complex Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

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

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix protein VP40
    Alternative name(s):
    Membrane-associated protein VP40
    Gene namesi
    Name:VP40
    OrganismiZaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
    Taxonomic identifieri128952 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesFiloviridaeEbolavirus
    Virus hostiEpomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]
    Homo sapiens (Human) [TaxID: 9606]
    Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]
    ProteomesiUP000007209: Genome

    Subcellular locationi

    Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: In virion, localizes on the intravirional side of the membrane. In the host cell, it is found associated with virus-induced membrane proliferation foci and probably also in multivesicular bodies. These VP40-enriched membrane clusters are then redistributed to the plasma membrane where budding takes place By similarity.By similarity

    GO - Cellular componenti

    1. host cell endomembrane system Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. integral to membrane of host cell Source: CACAO
    4. membrane raft Source: CACAO
    5. ribonucleoprotein complex Source: UniProtKB-KW
    6. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host membrane, Membrane, Viral matrix protein, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71P → A: Partial loss of budding. 2 Publications
    Mutagenesisi10 – 112PP → AA: 90% loss of budding. 1 Publication
    Mutagenesisi11 – 111P → A: Complete loss of budding. 1 Publication
    Mutagenesisi13 – 131Y → A: Complete loss of interaction with WW domain containing proteins. 2 Publications
    Mutagenesisi125 – 1251F → A: Partial loss of RNA-binding. Complete loss of virus infectivity. 2 Publications
    Mutagenesisi134 – 1341R → A: Complete loss of RNA-binding. Complete loss of virus infectivity. 2 Publications
    Mutagenesisi212 – 2143KLR → AAA: 85% loss of budding efficiency. Impaired oligomerization. 1 Publication
    Mutagenesisi212 – 2143KLR → ALA: 80% loss of budding efficiency. No effect on oligomerization. 1 Publication
    Mutagenesisi212 – 2132KL → AA: 84% loss of budding efficiency. Impaired oligomerization. 1 Publication
    Mutagenesisi212 – 2121K → A: 40% loss of budding efficiency. No effect on oligomerization. 1 Publication
    Mutagenesisi213 – 2142LR → AA: 84% loss of budding efficiency. Impaired oligomerization. 1 Publication
    Mutagenesisi213 – 2131L → A: 87% loss of budding efficiency. Impaired oligomerization. 1 Publication
    Mutagenesisi213 – 2131L → I: 40% loss of budding efficiency. 1 Publication
    Mutagenesisi214 – 2141R → A: 65% loss of budding efficiency. No effect on oligomerization. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 326326Matrix protein VP40PRO_0000222164Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer, homo-hexamer or homo-octamer. Membrane association induces conformational switch from monomer to hexamer. Interacts with host TSG101. Homo-hexamer interacts with the WW domain 3 of host NEDD4. Interacts with the nucleoprotein. May interact with VP35.5 Publications

    Protein-protein interaction databases

    MINTiMINT-151825.

    Structurei

    Secondary structure

    1
    326
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi61 – 644
    Beta strandi71 – 8414
    Beta strandi87 – 10115
    Beta strandi103 – 1064
    Helixi108 – 11710
    Beta strandi120 – 1267
    Beta strandi128 – 1303
    Beta strandi132 – 1398
    Helixi148 – 1514
    Beta strandi153 – 1586
    Helixi159 – 1624
    Beta strandi173 – 18513
    Turni198 – 2003
    Beta strandi203 – 2097
    Beta strandi211 – 2133
    Helixi234 – 24310
    Turni244 – 2463
    Beta strandi248 – 2536
    Helixi254 – 2563
    Beta strandi258 – 2625
    Helixi265 – 2728
    Beta strandi284 – 2885
    Beta strandi304 – 3096

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H2CX-ray1.60A55-194[»]
    1H2DX-ray2.60A/B31-212[»]
    2KQ0NMR-B5-16[»]
    4EJEX-ray2.20C/D5-13[»]
    4LDBX-ray3.10A/B/C/D44-326[»]
    4LDDX-ray3.50A/B/C44-326[»]
    4LDIX-ray4.15A/B44-326[»]
    4LDMX-ray1.85A44-188[»]
    ProteinModelPortaliQ05128.
    SMRiQ05128. Positions 44-321.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05128.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni212 – 2143Important for oligomerization
    Regioni213 – 326114Membrane-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi7 – 104PTAP/PSAP motif
    Motifi10 – 134PPXY 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. VP40 contains two overlapping L domains: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 and a PPXY motif which interacts with the WW domain 3 of NEDD4.

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR008986. EV_matrix.
    [Graphical view]
    PfamiPF07447. VP40. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018327. VP40_FiloV. 1 hit.
    SUPFAMiSSF50012. SSF50012. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q05128-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRVILPTAP PEYMEAIYPV RSNSTIARGG NSNTGFLTPE SVNGDTPSNP    50
    LRPIADDTID HASHTPGSVS SAFILEAMVN VISGPKVLMK QIPIWLPLGV 100
    ADQKTYSFDS TTAAIMLASY TITHFGKATN PLVRVNRLGP GIPDHPLRLL 150
    RIGNQAFLQE FVLPPVQLPQ YFTFDLTALK LITQPLPAAT WTDDTPTGSN 200
    GALRPGISFH PKLRPILLPN KSGKKGNSAD LTSPEKIQAI MTSLQDFKIV 250
    PIDPTKNIMG IEVPETLVHK LTGKKVTSKN GQPIIPVLLP KYIGLDPVAP 300
    GDLTMVITQD CDTCHSPASL PAVIEK 326
    Length:326
    Mass (Da):35,183
    Last modified:February 1, 1994 - v1
    Checksum:i1AB132C0DB8E9003
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61274 Genomic RNA. Translation: CAA43579.1.
    L11365 Genomic RNA. Translation: AAB81003.1.
    AF086833 Genomic RNA. Translation: AAD14583.1.
    AF272001 Genomic RNA. Translation: AAG40166.1.
    AF499101 Genomic RNA. Translation: AAM76033.1.
    AY142960 Genomic RNA. Translation: AAN37506.1.
    RefSeqiNP_066245.1. NC_002549.1.

    Genome annotation databases

    GeneIDi911825.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61274 Genomic RNA. Translation: CAA43579.1 .
    L11365 Genomic RNA. Translation: AAB81003.1 .
    AF086833 Genomic RNA. Translation: AAD14583.1 .
    AF272001 Genomic RNA. Translation: AAG40166.1 .
    AF499101 Genomic RNA. Translation: AAM76033.1 .
    AY142960 Genomic RNA. Translation: AAN37506.1 .
    RefSeqi NP_066245.1. NC_002549.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H2C X-ray 1.60 A 55-194 [» ]
    1H2D X-ray 2.60 A/B 31-212 [» ]
    2KQ0 NMR - B 5-16 [» ]
    4EJE X-ray 2.20 C/D 5-13 [» ]
    4LDB X-ray 3.10 A/B/C/D 44-326 [» ]
    4LDD X-ray 3.50 A/B/C 44-326 [» ]
    4LDI X-ray 4.15 A/B 44-326 [» ]
    4LDM X-ray 1.85 A 44-188 [» ]
    ProteinModelPortali Q05128.
    SMRi Q05128. Positions 44-321.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-151825.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 911825.

    Miscellaneous databases

    EvolutionaryTracei Q05128.

    Family and domain databases

    InterProi IPR008986. EV_matrix.
    [Graphical view ]
    Pfami PF07447. VP40. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018327. VP40_FiloV. 1 hit.
    SUPFAMi SSF50012. SSF50012. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The VP35 and VP40 proteins of filoviruses. Homology between Marburg and Ebola viruses."
      Bukreyev A.A., Volchkov V.E., Blinov V.M., Netesov S.V.
      FEBS Lett. 322:41-46(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Sequence analysis of the Ebola virus genome: organization, genetic elements, and comparison with the genome of Marburg virus."
      Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.
      Virus Res. 29:215-240(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Characterization of the L gene and 5' trailer region of Ebola virus."
      Volchkov V.E., Volchkova V.A., Chepurnov A.A., Blinov V.M., Netesov S.V., Feldmann H.
      J. Gen. Virol. 80:355-362(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    4. "Molecular characterization of guinea pig-adapted variants of Ebola virus."
      Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A., Klenk H.D.
      Virology 277:147-155(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate guinea pig-adapted.
    5. Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    6. "Membrane association induces a conformational change in the Ebola virus matrix protein."
      Scianimanico S., Schoehn G., Timmins J., Ruigrok R.H., Klenk H.D., Weissenhorn W.
      EMBO J. 19:6732-6741(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MULTIMERIZATION.
    7. "A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding."
      Harty R.N., Brown M.E., Wang G., Huibregtse J., Hayes F.P.
      Proc. Natl. Acad. Sci. U.S.A. 97:13871-13876(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WW DOMAINS OF HOST UBIQUITIN LIGASES, MUTAGENESIS OF TYR-13.
    8. "Oligomerization and polymerization of the filovirus matrix protein VP40."
      Timmins J., Schoehn G., Kohlhaas C., Klenk H.D., Ruigrok R.W., Weissenhorn W.
      Virology 312:359-368(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MULTIMERIZATION.
    9. "Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4."
      Timmins J., Schoehn G., Ricard-Blum S., Scianimanico S., Vernet T., Ruigrok R.W., Weissenhorn W.
      J. Mol. Biol. 326:493-502(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN TSG101 AND NEDD4.
    10. "Ebola virus VP40 late domains are not essential for viral replication in cell culture."
      Neumann G., Ebihara H., Takada A., Noda T., Kobasa D., Jasenosky L.D., Watanabe S., Kim J.H., Feldmann H., Kawaoka Y.
      J. Virol. 79:10300-10307(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-7 AND 10-PRO-PRO-11.
    11. "An all-atom model of the pore-like structure of hexameric VP40 from Ebola: structural insights into the monomer-hexamer transition."
      Nguyen T.L., Schoehn G., Weissenhorn W., Hermone A.R., Burnett J.C., Panchal R.G., McGrath C., Zaharevitz D.W., Aman M.J., Gussio R., Bavari S.
      J. Struct. Biol. 151:30-40(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MULTIMERIZATION.
    12. Cited for: MUTAGENESIS OF PHE-125 AND ARG-134.
    13. "Functional characterization of Ebola virus L-domains using VSV recombinants."
      Irie T., Licata J.M., Harty R.N.
      Virology 336:291-298(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology."
      Johnson R.F., Bell P., Harty R.N.
      Virol. J. 3:31-31(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Ebola virus VP35-VP40 interaction is sufficient for packaging 3E-5E minigenome RNA into virus-like particles."
      Johnson R.F., McCarthy S.E., Godlewski P.J., Harty R.N.
      J. Virol. 80:5135-5144(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VP35.
    16. "Mapping of the VP40-binding regions of the nucleoprotein of Ebola virus."
      Noda T., Watanabe S., Sagara H., Kawaoka Y.
      J. Virol. 81:3554-3562(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE NUCLEOPROTEIN.
    17. "Role for amino acids 212KLR214 of Ebola virus VP40 in assembly and budding."
      McCarthy S.E., Johnson R.F., Zhang Y.-A., Sunyer J.O., Harty R.N.
      J. Virol. 81:11452-11460(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 212-LYS--ARG-214.
    18. "The matrix protein VP40 from Ebola virus octamerizes into pore-like structures with specific RNA binding properties."
      Gomis-Ruth F.X., Dessen A., Timmins J., Bracher A., Kolesnikowa L., Becker S., Klenk H.D., Weissenhorn W.
      Structure 11:423-433(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 55-194 IN COMPLEX WITH RNA.

    Entry informationi

    Entry nameiVP40_EBOZM
    AccessioniPrimary (citable) accession number: Q05128
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Most abundant protein in the virion.

    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