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Q05128

- VP40_EBOZM

UniProt

Q05128 - VP40_EBOZM

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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

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
Complete GO annotation...

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 plasma membrane Source: UniProtKB-KW
  2. integral to membrane of host cell Source: CACAO
  3. membrane raft Source: CACAO
  4. ribonucleoprotein complex Source: UniProtKB-KW
  5. virion Source: UniProtKB-KW
Complete GO annotation...

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. 1 Publication
Mutagenesisi10 – 112PP → AA: 90% loss of budding. 1 Publication
Mutagenesisi11 – 111P → A: Complete loss of budding.
Mutagenesisi13 – 131Y → A: Complete loss of interaction with WW domain containing proteins. 1 Publication
Mutagenesisi125 – 1251F → A: Partial loss of RNA-binding. Complete loss of virus infectivity. 1 Publication
Mutagenesisi134 – 1341R → A: Complete loss of RNA-binding. Complete loss of virus infectivity. 1 Publication
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.
Mutagenesisi212 – 2121K → A: 40% loss of budding efficiency. No effect on oligomerization.
Mutagenesisi213 – 2142LR → AA: 84% loss of budding efficiency. Impaired oligomerization.
Mutagenesisi213 – 2131L → A: 87% loss of budding efficiency. Impaired oligomerization.
Mutagenesisi213 – 2131L → I: 40% loss of budding efficiency.
Mutagenesisi214 – 2141R → A: 65% loss of budding efficiency. No effect on oligomerization.

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

        10         20         30         40         50
MRRVILPTAP PEYMEAIYPV RSNSTIARGG NSNTGFLTPE SVNGDTPSNP
60 70 80 90 100
LRPIADDTID HASHTPGSVS SAFILEAMVN VISGPKVLMK QIPIWLPLGV
110 120 130 140 150
ADQKTYSFDS TTAAIMLASY TITHFGKATN PLVRVNRLGP GIPDHPLRLL
160 170 180 190 200
RIGNQAFLQE FVLPPVQLPQ YFTFDLTALK LITQPLPAAT WTDDTPTGSN
210 220 230 240 250
GALRPGISFH PKLRPILLPN KSGKKGNSAD LTSPEKIQAI MTSLQDFKIV
260 270 280 290 300
PIDPTKNIMG IEVPETLVHK LTGKKVTSKN GQPIIPVLLP KYIGLDPVAP
310 320
GDLTMVITQD CDTCHSPASL PAVIEK
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 29, 2014
This is version 83 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