Matrix protein VP40 - Zaire ebolavirus (strain Mayinga-76) (ZEBOV)

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Q05128 (VP40_EBOZM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 76. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Matrix protein VP40

Alternative name(s):
Membrane-associated protein VP40

Gene names

Name:

VP40

Organism

Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus) [Reference proteome]

Taxonomic identifier

128952 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Mononegavirales › Filoviridae › Ebolavirus ›

Virus host

Epomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]
Homo sapiens (Human) [TaxID: 9606]
Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.13 Ref.14
Subunit structure	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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.15 Ref.16
Subcellular location	Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein; 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.
Domain	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. Ref.7
Miscellaneous	Most abundant protein in the virion.
Sequence similarities	Belongs to the filoviridae matrix protein VP40 family.

Ontologies

Keywords
Biological process	Host-virus interaction Viral RNA replication Viral budding Viral budding via the host ESCRT complexes Virus exit from host cell
Cellular component	Host cell membrane Host membrane Membrane Viral matrix protein Virion
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	viral release from host cell Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 326

326

Matrix protein VP40

PRO_0000222164

Regions

Region

212 – 214

Important for oligomerization

Region

213 – 326

114

Membrane-binding By similarity

Motif

7 – 10

PTAP/PSAP motif

Motif

10 – 13

PPXY motif

Experimental info

Mutagenesis

P → A: Partial loss of budding. Ref.10

Mutagenesis

10 – 11

PP → AA: 90% loss of budding.

Mutagenesis

P → A: Complete loss of budding.

Mutagenesis

Y → A: Complete loss of interaction with WW domain containing proteins. Ref.7

Mutagenesis

125

F → A: Partial loss of RNA-binding. Complete loss of virus infectivity. Ref.12

Mutagenesis

134

R → A: Complete loss of RNA-binding. Complete loss of virus infectivity. Ref.12

Mutagenesis

212 – 214

KLR → AAA: 85% loss of budding efficiency. Impaired oligomerization. Ref.17

Mutagenesis

212 – 214

KLR → ALA: 80% loss of budding efficiency. No effect on oligomerization. Ref.17

Mutagenesis

212 – 213

KL → AA: 84% loss of budding efficiency. Impaired oligomerization.

Mutagenesis

212

K → A: 40% loss of budding efficiency. No effect on oligomerization.

Mutagenesis

213 – 214

LR → AA: 84% loss of budding efficiency. Impaired oligomerization.

Mutagenesis

213

L → A: 87% loss of budding efficiency. Impaired oligomerization.

Mutagenesis

213

L → I: 40% loss of budding efficiency.

Mutagenesis

214

R → A: 65% loss of budding efficiency. No effect on oligomerization.

Secondary structure

326

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q05128 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 1AB132C0DB8E9003
Show »

FASTA

326

35,183

        10         20         30         40         50         60 
MRRVILPTAP PEYMEAIYPV RSNSTIARGG NSNTGFLTPE SVNGDTPSNP LRPIADDTID 

        70         80         90        100        110        120 
HASHTPGSVS SAFILEAMVN VISGPKVLMK QIPIWLPLGV ADQKTYSFDS TTAAIMLASY 

       130        140        150        160        170        180 
TITHFGKATN PLVRVNRLGP GIPDHPLRLL RIGNQAFLQE FVLPPVQLPQ YFTFDLTALK 

       190        200        210        220        230        240 
LITQPLPAAT WTDDTPTGSN GALRPGISFH PKLRPILLPN KSGKKGNSAD LTSPEKIQAI 

       250        260        270        280        290        300 
MTSLQDFKIV PIDPTKNIMG IEVPETLVHK LTGKKVTSKN GQPIIPVLLP KYIGLDPVAP 

       310        320 
GDLTMVITQD CDTCHSPASL PAVIEK

« Hide

References

[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]	"VP40 octamers are essential for Ebola virus replication." Hoenen T., Volchkov V., Kolesnikova L., Mittler E., Timmins J., Ottmann M., Reynard O., Becker S., Weissenhorn W. J. Virol. 79:1898-1905(2005) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

RefSeq

NP_066245.1. NC_002549.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q05128.

SMR

Q05128. Positions 44-321.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

911825.

Family and domain databases

InterPro

IPR008986. EV_matrix.
[Graphical view]

Pfam

PF07447. VP40. 1 hit.
[Graphical view]

PIRSF

PIRSF018327. VP40_FiloV. 1 hit.

SUPFAM

SSF50012. EV_matrix. 2 hits.

ProtoNet

Search...

Other

EvolutionaryTrace

Q05128.

Entry information

Entry name

VP40_EBOZM

Accession

Primary (citable) accession number: Q05128

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Other

Entry information

Relevant documents