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Protein

Matrix protein VP40

Gene

VP40

Organism
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • intracellular transport of virus Source: CACAO
  • suppression of host defenses Source: CACAO
  • viral budding Source: CACAO
  • viral budding from plasma membrane Source: UniProtKB
  • 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 virusesssRNA 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]
Proteomesi
  • UP000007209 Componenti: Genome

Subcellular locationi

  • Virion membrane By similarity; Peripheral membrane protein By similarity
  • Host late endosome membrane By similarity; Peripheral membrane protein By similarity
  • Host cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Host endomembrane system By similarity; Peripheral membrane protein 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

GO - Cellular componenti

  • host cell endomembrane system Source: UniProtKB-SubCell
  • host cell late endosome membrane Source: UniProtKB-SubCell
  • host cell plasma membrane Source: UniProtKB-SubCell
  • integral to membrane of host cell Source: CACAO
  • membrane raft Source: CACAO
  • virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host endosome, 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 – 644Combined sources
Beta strandi71 – 8414Combined sources
Beta strandi87 – 10115Combined sources
Beta strandi103 – 1064Combined sources
Helixi108 – 11710Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi132 – 1398Combined sources
Helixi148 – 1514Combined sources
Beta strandi153 – 1586Combined sources
Helixi159 – 1624Combined sources
Beta strandi173 – 18513Combined sources
Turni198 – 2003Combined sources
Beta strandi203 – 2097Combined sources
Beta strandi211 – 2133Combined sources
Helixi234 – 24310Combined sources
Turni244 – 2463Combined sources
Beta strandi248 – 2536Combined sources
Helixi254 – 2563Combined sources
Beta strandi258 – 2625Combined sources
Helixi265 – 2728Combined sources
Beta strandi284 – 2885Combined sources
Beta strandi304 – 3096Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:
EMBLi
GenBanki
DDBJi
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.
KEGGivg:911825.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

MINTiMINT-151825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi911825.
KEGGivg:911825.

Miscellaneous databases

EvolutionaryTraceiQ05128.

Family and domain databases

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

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: June 8, 2016
This is version 97 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.