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Matrix protein VP40 (Membrane-associated protein VP40)

 VP40_EBOZM              Reviewed;         326 AA.
Q05128;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
28-MAR-2018, entry version 106.
RecName: Full=Matrix protein VP40;
AltName: Full=Membrane-associated protein VP40;
Name=VP40;
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Filoviridae; Ebolavirus.
NCBI_TaxID=128952;
NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8482365; DOI=10.1016/0014-5793(93)81107-B;
Bukreyev A.A., Volchkov V.E., Blinov V.M., Netesov S.V.;
"The VP35 and VP40 proteins of filoviruses. Homology between Marburg
and Ebola viruses.";
FEBS Lett. 322:41-46(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8237108; DOI=10.1016/0168-1702(93)90063-S;
Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
"Sequence analysis of the Ebola virus genome: organization, genetic
elements, and comparison with the genome of Marburg virus.";
Virus Res. 29:215-240(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=10073695;
Volchkov V.E., Volchkova V.A., Chepurnov A.A., Blinov V.M.,
Netesov S.V., Feldmann H.;
"Characterization of the L gene and 5' trailer region of Ebola
virus.";
J. Gen. Virol. 80:355-362(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate guinea pig-adapted;
PubMed=11062045; DOI=10.1006/viro.2000.0572;
Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A.,
Klenk H.D.;
"Molecular characterization of guinea pig-adapted variants of Ebola
virus.";
Virology 277:147-155(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[6]
MULTIMERIZATION.
PubMed=11118208; DOI=10.1093/emboj/19.24.6732;
Scianimanico S., Schoehn G., Timmins J., Ruigrok R.H., Klenk H.D.,
Weissenhorn W.;
"Membrane association induces a conformational change in the Ebola
virus matrix protein.";
EMBO J. 19:6732-6741(2000).
[7]
INTERACTION WITH WW DOMAINS OF HOST UBIQUITIN LIGASES, AND MUTAGENESIS
OF TYR-13.
PubMed=11095724; DOI=10.1073/pnas.250277297;
Harty R.N., Brown M.E., Wang G., Huibregtse J., Hayes F.P.;
"A PPxY motif within the VP40 protein of Ebola virus interacts
physically and functionally with a ubiquitin ligase: implications for
filovirus budding.";
Proc. Natl. Acad. Sci. U.S.A. 97:13871-13876(2000).
[8]
MULTIMERIZATION.
PubMed=12919741; DOI=10.1016/S0042-6822(03)00260-5;
Timmins J., Schoehn G., Kohlhaas C., Klenk H.D., Ruigrok R.W.,
Weissenhorn W.;
"Oligomerization and polymerization of the filovirus matrix protein
VP40.";
Virology 312:359-368(2003).
[9]
INTERACTION WITH HUMAN TSG101 AND NEDD4.
PubMed=12559917; DOI=10.1016/S0022-2836(02)01406-7;
Timmins J., Schoehn G., Ricard-Blum S., Scianimanico S., Vernet T.,
Ruigrok R.W., Weissenhorn W.;
"Ebola virus matrix protein VP40 interaction with human cellular
factors Tsg101 and Nedd4.";
J. Mol. Biol. 326:493-502(2003).
[10]
MUTAGENESIS OF PRO-7 AND 10-PRO-PRO-11.
PubMed=16051823; DOI=10.1128/JVI.79.16.10300-10307.2005;
Neumann G., Ebihara H., Takada A., Noda T., Kobasa D., Jasenosky L.D.,
Watanabe S., Kim J.H., Feldmann H., Kawaoka Y.;
"Ebola virus VP40 late domains are not essential for viral replication
in cell culture.";
J. Virol. 79:10300-10307(2005).
[11]
MULTIMERIZATION.
PubMed=15908231; DOI=10.1016/j.jsb.2005.02.013;
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.;
"An all-atom model of the pore-like structure of hexameric VP40 from
Ebola: structural insights into the monomer-hexamer transition.";
J. Struct. Biol. 151:30-40(2005).
[12]
MUTAGENESIS OF PHE-125 AND ARG-134.
PubMed=15650213; DOI=10.1128/JVI.79.3.1898-1905.2005;
Hoenen T., Volchkov V., Kolesnikova L., Mittler E., Timmins J.,
Ottmann M., Reynard O., Becker S., Weissenhorn W.;
"VP40 octamers are essential for Ebola virus replication.";
J. Virol. 79:1898-1905(2005).
[13]
FUNCTION.
PubMed=15892969; DOI=10.1016/j.virol.2005.03.027;
Irie T., Licata J.M., Harty R.N.;
"Functional characterization of Ebola virus L-domains using VSV
recombinants.";
Virology 336:291-298(2005).
[14]
FUNCTION.
PubMed=16719918; DOI=10.1186/1743-422X-3-31;
Johnson R.F., Bell P., Harty R.N.;
"Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP
morphology.";
Virol. J. 3:31-31(2006).
[15]
INTERACTION WITH VP35.
PubMed=16698994; DOI=10.1128/JVI.01857-05;
Johnson R.F., McCarthy S.E., Godlewski P.J., Harty R.N.;
"Ebola virus VP35-VP40 interaction is sufficient for packaging 3E-5E
minigenome RNA into virus-like particles.";
J. Virol. 80:5135-5144(2006).
[16]
INTERACTION WITH THE NUCLEOPROTEIN.
PubMed=17229682; DOI=10.1128/JVI.02183-06;
Noda T., Watanabe S., Sagara H., Kawaoka Y.;
"Mapping of the VP40-binding regions of the nucleoprotein of Ebola
virus.";
J. Virol. 81:3554-3562(2007).
[17]
MUTAGENESIS OF 212-LYS--ARG-214.
PubMed=17699576; DOI=10.1128/JVI.00853-07;
McCarthy S.E., Johnson R.F., Zhang Y.-A., Sunyer J.O., Harty R.N.;
"Role for amino acids 212KLR214 of Ebola virus VP40 in assembly and
budding.";
J. Virol. 81:11452-11460(2007).
[18]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 55-194 IN COMPLEX WITH RNA.
PubMed=12679020; DOI=10.1016/S0969-2126(03)00050-9;
Gomis-Ruth F.X., Dessen A., Timmins J., Bracher A., Kolesnikowa L.,
Becker S., Klenk H.D., Weissenhorn W.;
"The matrix protein VP40 from Ebola virus octamerizes into pore-like
structures with specific RNA binding properties.";
Structure 11:423-433(2003).
-!- 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.
{ECO:0000269|PubMed:15892969, ECO:0000269|PubMed:16719918}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:11095724,
ECO:0000269|PubMed:12559917, ECO:0000269|PubMed:12679020,
ECO:0000269|PubMed:16698994, ECO:0000269|PubMed:17229682}.
-!- SUBCELLULAR LOCATION: Virion membrane
{ECO:0000250|UniProtKB:P35260}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P35260}. Host late endosome membrane
{ECO:0000250|UniProtKB:P35260}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P35260}. Host cell membrane
{ECO:0000250|UniProtKB:P35260}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P35260}; Cytoplasmic side
{ECO:0000250|UniProtKB:P35260}. Host endomembrane system
{ECO:0000250|UniProtKB:P35260}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P35260}. 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. {ECO:0000250|UniProtKB:P35260}.
-!- 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.
-!- MISCELLANEOUS: Most abundant protein in the virion.
-!- SIMILARITY: Belongs to the filoviridae matrix protein VP40 family.
{ECO:0000305}.
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EMBL; X61274; CAA43579.1; -; Genomic_RNA.
EMBL; L11365; AAB81003.1; -; Genomic_RNA.
EMBL; AF086833; AAD14583.1; -; Genomic_RNA.
EMBL; AF272001; AAG40166.1; -; Genomic_RNA.
EMBL; AF499101; AAM76033.1; -; Genomic_RNA.
EMBL; AY142960; AAN37506.1; -; Genomic_RNA.
RefSeq; NP_066245.1; NC_002549.1.
PDB; 1H2C; X-ray; 1.60 A; A=55-194.
PDB; 1H2D; X-ray; 2.60 A; A/B=31-212.
PDB; 2KQ0; NMR; -; B=5-16.
PDB; 4EJE; X-ray; 2.20 A; C/D=5-13.
PDB; 4LDB; X-ray; 3.10 A; A/B/C/D=44-326.
PDB; 4LDD; X-ray; 3.50 A; A/B/C=44-326.
PDB; 4LDI; X-ray; 4.15 A; A/B=44-326.
PDB; 4LDM; X-ray; 1.85 A; A=44-188.
PDBsum; 1H2C; -.
PDBsum; 1H2D; -.
PDBsum; 2KQ0; -.
PDBsum; 4EJE; -.
PDBsum; 4LDB; -.
PDBsum; 4LDD; -.
PDBsum; 4LDI; -.
PDBsum; 4LDM; -.
ProteinModelPortal; Q05128; -.
SMR; Q05128; -.
ELM; Q05128; -.
GeneID; 911825; -.
KEGG; vg:911825; -.
OrthoDB; VOG090000FQ; -.
EvolutionaryTrace; Q05128; -.
Proteomes; UP000007209; Genome.
Proteomes; UP000109874; Genome.
Proteomes; UP000149419; Genome.
Proteomes; UP000150973; Genome.
GO; GO:0033645; C:host cell endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IDA:CACAO.
GO; GO:0045121; C:membrane raft; IDA:CACAO.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0075733; P:intracellular transport of virus; IMP:CACAO.
GO; GO:0044414; P:suppression of host defenses; IMP:CACAO.
GO; GO:0046755; P:viral budding; IMP:CACAO.
GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
Gene3D; 2.60.510.10; -; 1.
InterPro; IPR008986; EV_matrix.
InterPro; IPR035092; EV_matrix_protein_C-terminal.
InterPro; IPR038057; EV_matrix_sf.
Pfam; PF07447; VP40; 1.
PIRSF; PIRSF018327; VP40_FiloV; 1.
SUPFAM; SSF50012; SSF50012; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Host cell membrane; Host endosome;
Host membrane; Host-virus interaction; Membrane; Reference proteome;
Ribonucleoprotein; RNA-binding; Viral budding;
Viral budding via the host ESCRT complexes; Viral matrix protein;
Viral release from host cell; Viral RNA replication; Virion.
CHAIN 1 326 Matrix protein VP40.
/FTId=PRO_0000222164.
REGION 212 214 Important for oligomerization.
REGION 213 326 Membrane-binding. {ECO:0000250}.
MOTIF 7 10 PTAP/PSAP motif.
MOTIF 10 13 PPXY motif.
MUTAGEN 7 7 P->A: Partial loss of budding.
{ECO:0000269|PubMed:16051823}.
MUTAGEN 10 11 PP->AA: 90% loss of budding.
{ECO:0000269|PubMed:16051823}.
MUTAGEN 11 11 P->A: Complete loss of budding.
MUTAGEN 13 13 Y->A: Complete loss of interaction with
WW domain containing proteins.
{ECO:0000269|PubMed:11095724}.
MUTAGEN 125 125 F->A: Partial loss of RNA-binding.
Complete loss of virus infectivity.
{ECO:0000269|PubMed:15650213}.
MUTAGEN 134 134 R->A: Complete loss of RNA-binding.
Complete loss of virus infectivity.
{ECO:0000269|PubMed:15650213}.
MUTAGEN 212 214 KLR->AAA: 85% loss of budding efficiency.
Impaired oligomerization.
{ECO:0000269|PubMed:17699576}.
MUTAGEN 212 214 KLR->ALA: 80% loss of budding efficiency.
No effect on oligomerization.
{ECO:0000269|PubMed:17699576}.
MUTAGEN 212 213 KL->AA: 84% loss of budding efficiency.
Impaired oligomerization.
MUTAGEN 212 212 K->A: 40% loss of budding efficiency. No
effect on oligomerization.
MUTAGEN 213 214 LR->AA: 84% loss of budding efficiency.
Impaired oligomerization.
MUTAGEN 213 213 L->A: 87% loss of budding efficiency.
Impaired oligomerization.
MUTAGEN 213 213 L->I: 40% loss of budding efficiency.
MUTAGEN 214 214 R->A: 65% loss of budding efficiency. No
effect on oligomerization.
HELIX 61 64 {ECO:0000244|PDB:4LDB}.
STRAND 71 84 {ECO:0000244|PDB:1H2C}.
STRAND 87 101 {ECO:0000244|PDB:1H2C}.
STRAND 103 106 {ECO:0000244|PDB:1H2C}.
HELIX 108 117 {ECO:0000244|PDB:1H2C}.
STRAND 120 126 {ECO:0000244|PDB:1H2C}.
STRAND 128 130 {ECO:0000244|PDB:4LDB}.
STRAND 132 139 {ECO:0000244|PDB:1H2C}.
HELIX 148 151 {ECO:0000244|PDB:1H2C}.
STRAND 153 158 {ECO:0000244|PDB:1H2C}.
HELIX 159 162 {ECO:0000244|PDB:1H2C}.
STRAND 173 185 {ECO:0000244|PDB:1H2C}.
TURN 198 200 {ECO:0000244|PDB:4LDB}.
STRAND 203 209 {ECO:0000244|PDB:4LDB}.
STRAND 211 213 {ECO:0000244|PDB:4LDB}.
HELIX 234 243 {ECO:0000244|PDB:4LDB}.
TURN 244 246 {ECO:0000244|PDB:4LDB}.
STRAND 248 253 {ECO:0000244|PDB:4LDB}.
HELIX 254 256 {ECO:0000244|PDB:4LDB}.
STRAND 258 262 {ECO:0000244|PDB:4LDB}.
HELIX 265 272 {ECO:0000244|PDB:4LDB}.
STRAND 284 288 {ECO:0000244|PDB:4LDB}.
STRAND 304 309 {ECO:0000244|PDB:4LDB}.
SEQUENCE 326 AA; 35183 MW; 1AB132C0DB8E9003 CRC64;
MRRVILPTAP PEYMEAIYPV RSNSTIARGG NSNTGFLTPE SVNGDTPSNP LRPIADDTID
HASHTPGSVS SAFILEAMVN VISGPKVLMK QIPIWLPLGV ADQKTYSFDS TTAAIMLASY
TITHFGKATN PLVRVNRLGP GIPDHPLRLL RIGNQAFLQE FVLPPVQLPQ YFTFDLTALK
LITQPLPAAT WTDDTPTGSN GALRPGISFH PKLRPILLPN KSGKKGNSAD LTSPEKIQAI
MTSLQDFKIV PIDPTKNIMG IEVPETLVHK LTGKKVTSKN GQPIIPVLLP KYIGLDPVAP
GDLTMVITQD CDTCHSPASL PAVIEK


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