VP40_EBOZM
ID VP40_EBOZM Reviewed; 326 AA.
AC Q05128;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Matrix protein VP40;
DE AltName: Full=Ebola VP40 {ECO:0000303|PubMed:28768865};
DE Short=eVP40 {ECO:0000303|PubMed:28768865};
DE AltName: Full=Membrane-associated protein VP40;
GN Name=VP40;
OS Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128952;
OH NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8482365; DOI=10.1016/0014-5793(93)81107-b;
RA Bukreyev A.A., Volchkov V.E., Blinov V.M., Netesov S.V.;
RT "The VP35 and VP40 proteins of filoviruses. Homology between Marburg and
RT Ebola viruses.";
RL FEBS Lett. 322:41-46(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8237108; DOI=10.1016/0168-1702(93)90063-s;
RA Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
RT "Sequence analysis of the Ebola virus genome: organization, genetic
RT elements, and comparison with the genome of Marburg virus.";
RL Virus Res. 29:215-240(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10073695; DOI=10.1099/0022-1317-80-2-355;
RA Volchkov V.E., Volchkova V.A., Chepurnov A.A., Blinov V.M., Netesov S.V.,
RA Feldmann H.;
RT "Characterization of the L gene and 5' trailer region of Ebola virus.";
RL J. Gen. Virol. 80:355-362(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate guinea pig-adapted;
RX PubMed=11062045; DOI=10.1006/viro.2000.0572;
RA Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A., Klenk H.D.;
RT "Molecular characterization of guinea pig-adapted variants of Ebola
RT virus.";
RL Virology 277:147-155(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBUNIT.
RX PubMed=11118208; DOI=10.1093/emboj/19.24.6732;
RA Scianimanico S., Schoehn G., Timmins J., Ruigrok R.H., Klenk H.D.,
RA Weissenhorn W.;
RT "Membrane association induces a conformational change in the Ebola virus
RT matrix protein.";
RL EMBO J. 19:6732-6741(2000).
RN [7]
RP INTERACTION WITH WW DOMAINS OF HOST UBIQUITIN LIGASES, AND MUTAGENESIS OF
RP TYR-13.
RX PubMed=11095724; DOI=10.1073/pnas.250277297;
RA Harty R.N., Brown M.E., Wang G., Huibregtse J., Hayes F.P.;
RT "A PPxY motif within the VP40 protein of Ebola virus interacts physically
RT and functionally with a ubiquitin ligase: implications for filovirus
RT budding.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13871-13876(2000).
RN [8]
RP SUBUNIT.
RX PubMed=12919741; DOI=10.1016/s0042-6822(03)00260-5;
RA Timmins J., Schoehn G., Kohlhaas C., Klenk H.D., Ruigrok R.W.,
RA Weissenhorn W.;
RT "Oligomerization and polymerization of the filovirus matrix protein VP40.";
RL Virology 312:359-368(2003).
RN [9]
RP INTERACTION WITH HUMAN TSG101 AND NEDD4.
RX PubMed=12559917; DOI=10.1016/s0022-2836(02)01406-7;
RA Timmins J., Schoehn G., Ricard-Blum S., Scianimanico S., Vernet T.,
RA Ruigrok R.W., Weissenhorn W.;
RT "Ebola virus matrix protein VP40 interaction with human cellular factors
RT Tsg101 and Nedd4.";
RL J. Mol. Biol. 326:493-502(2003).
RN [10]
RP MUTAGENESIS OF PRO-7 AND 10-PRO-PRO-11.
RX PubMed=16051823; DOI=10.1128/jvi.79.16.10300-10307.2005;
RA Neumann G., Ebihara H., Takada A., Noda T., Kobasa D., Jasenosky L.D.,
RA Watanabe S., Kim J.H., Feldmann H., Kawaoka Y.;
RT "Ebola virus VP40 late domains are not essential for viral replication in
RT cell culture.";
RL J. Virol. 79:10300-10307(2005).
RN [11]
RP SUBUNIT.
RX PubMed=15908231; DOI=10.1016/j.jsb.2005.02.013;
RA Nguyen T.L., Schoehn G., Weissenhorn W., Hermone A.R., Burnett J.C.,
RA Panchal R.G., McGrath C., Zaharevitz D.W., Aman M.J., Gussio R., Bavari S.;
RT "An all-atom model of the pore-like structure of hexameric VP40 from Ebola:
RT structural insights into the monomer-hexamer transition.";
RL J. Struct. Biol. 151:30-40(2005).
RN [12]
RP MUTAGENESIS OF PHE-125 AND ARG-134.
RX PubMed=15650213; DOI=10.1128/jvi.79.3.1898-1905.2005;
RA Hoenen T., Volchkov V., Kolesnikova L., Mittler E., Timmins J., Ottmann M.,
RA Reynard O., Becker S., Weissenhorn W.;
RT "VP40 octamers are essential for Ebola virus replication.";
RL J. Virol. 79:1898-1905(2005).
RN [13]
RP FUNCTION.
RX PubMed=15892969; DOI=10.1016/j.virol.2005.03.027;
RA Irie T., Licata J.M., Harty R.N.;
RT "Functional characterization of Ebola virus L-domains using VSV
RT recombinants.";
RL Virology 336:291-298(2005).
RN [14]
RP FUNCTION.
RX PubMed=16719918; DOI=10.1186/1743-422x-3-31;
RA Johnson R.F., Bell P., Harty R.N.;
RT "Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology.";
RL Virol. J. 3:31-31(2006).
RN [15]
RP INTERACTION WITH VP35.
RX PubMed=16698994; DOI=10.1128/jvi.01857-05;
RA Johnson R.F., McCarthy S.E., Godlewski P.J., Harty R.N.;
RT "Ebola virus VP35-VP40 interaction is sufficient for packaging 3E-5E
RT minigenome RNA into virus-like particles.";
RL J. Virol. 80:5135-5144(2006).
RN [16]
RP INTERACTION WITH THE NUCLEOPROTEIN.
RX PubMed=17229682; DOI=10.1128/jvi.02183-06;
RA Noda T., Watanabe S., Sagara H., Kawaoka Y.;
RT "Mapping of the VP40-binding regions of the nucleoprotein of Ebola virus.";
RL J. Virol. 81:3554-3562(2007).
RN [17]
RP MUTAGENESIS OF 212-LYS--ARG-214.
RX PubMed=17699576; DOI=10.1128/jvi.00853-07;
RA McCarthy S.E., Johnson R.F., Zhang Y.-A., Sunyer J.O., Harty R.N.;
RT "Role for amino acids 212KLR214 of Ebola virus VP40 in assembly and
RT budding.";
RL J. Virol. 81:11452-11460(2007).
RN [18]
RP INTERACTION WITH NP, AND SUBCELLULAR LOCATION.
RX PubMed=21987757; DOI=10.1093/infdis/jir293;
RA Liu Y., Stone S., Harty R.N.;
RT "Characterization of filovirus protein-protein interactions in mammalian
RT cells using bimolecular complementation.";
RL J. Infect. Dis. 204:817-824(2011).
RN [19]
RP FUNCTION, INTERACTION WITH HOST IQGAP1, AND SUBCELLULAR LOCATION.
RX PubMed=23637409; DOI=10.1128/jvi.00470-13;
RA Lu J., Qu Y., Liu Y., Jambusaria R., Han Z., Ruthel G., Freedman B.D.,
RA Harty R.N.;
RT "Host IQGAP1 and Ebola virus VP40 interactions facilitate virus-like
RT particle egress.";
RL J. Virol. 87:7777-7780(2013).
RN [20]
RP SUBUNIT.
RX PubMed=23953110; DOI=10.1016/j.cell.2013.07.015;
RA Bornholdt Z.A., Noda T., Abelson D.M., Halfmann P., Wood M.R., Kawaoka Y.,
RA Saphire E.O.;
RT "Structural rearrangement of ebola virus VP40 begets multiple functions in
RT the virus life cycle.";
RL Cell 154:763-774(2013).
RN [21]
RP REVIEW.
RX PubMed=25159197; DOI=10.1002/pro.2541;
RA Radzimanowski J., Effantin G., Weissenhorn W.;
RT "Conformational plasticity of the Ebola virus matrix protein.";
RL Protein Sci. 23:1519-1527(2014).
RN [22]
RP FUNCTION, INTERACTION WITH HOST PDCD6IP/ALIX, AND MOTIF.
RX PubMed=25786915; DOI=10.1093/infdis/jiu838;
RA Han Z., Madara J.J., Liu Y., Liu W., Ruthel G., Freedman B.D., Harty R.N.;
RT "ALIX Rescues Budding of a Double PTAP/PPEY L-Domain Deletion Mutant of
RT Ebola VP40: A Role for ALIX in Ebola Virus Egress.";
RL J. Infect. Dis. 212:S138-S145(2015).
RN [23]
RP FUNCTION, AND INTERACTION WITH HOST ITCH.
RX PubMed=27489272; DOI=10.1128/jvi.01078-16;
RA Han Z., Sagum C.A., Bedford M.T., Sidhu S.S., Sudol M., Harty R.N.;
RT "ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate
RT Budding.";
RL J. Virol. 90:9163-9171(2016).
RN [24]
RP SUBCELLULAR LOCATION, SUBUNIT, AND FUNCTION.
RX PubMed=26753796; DOI=10.1038/srep19125;
RA Johnson K.A., Taghon G.J., Scott J.L., Stahelin R.V.;
RT "The Ebola Virus matrix protein, VP40, requires phosphatidylinositol 4,5-
RT bisphosphate (PI(4,5)P2) for extensive oligomerization at the plasma
RT membrane and viral egress.";
RL Sci. Rep. 6:19125-19125(2016).
RN [25]
RP SUMOYLATION AT LYS-326, AND MUTAGENESIS OF LYS-326.
RX PubMed=27849047; DOI=10.1038/srep37258;
RA Baz-Martinez M., El Motiam A., Ruibal P., Condezo G.N.,
RA de la Cruz-Herrera C.F., Lang V., Collado M., San Martin C.,
RA Rodriguez M.S., Munoz-Fontela C., Rivas C.;
RT "Regulation of Ebola virus VP40 matrix protein by SUMO.";
RL Sci. Rep. 6:37258-37258(2016).
RN [26]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27872619; DOI=10.3389/fmicb.2016.01765;
RA Pleet M.L., Mathiesen A., DeMarino C., Akpamagbo Y.A., Barclay R.A.,
RA Schwab A., Iordanskiy S., Sampey G.C., Lepene B., Nekhai S., Aman M.J.,
RA Kashanchi F.;
RT "Ebola VP40 in Exosomes Can Cause Immune Cell Dysfunction.";
RL Front. Microbiol. 7:1765-1765(2016).
RN [27]
RP SUBCELLULAR LOCATION, UBIQUITINATION BY HOST WWP1, AND NOMENCLATURE.
RX PubMed=28768865; DOI=10.1128/jvi.00812-17;
RA Han Z., Sagum C.A., Takizawa F., Ruthel G., Berry C.T., Kong J.,
RA Sunyer J.O., Freedman B.D., Bedford M.T., Sidhu S.S., Sudol M., Harty R.N.;
RT "Ubiquitin Ligase WWP1 Interacts with Ebola Virus VP40 To Regulate
RT Egress.";
RL J. Virol. 91:0-0(2017).
RN [28]
RP REVIEW.
RX PubMed=28177658; DOI=10.1089/dna.2017.3639;
RA Pleet M.L., DeMarino C., Lepene B., Aman M.J., Kashanchi F.;
RT "The Role of Exosomal VP40 in Ebola Virus Disease.";
RL DNA Cell Biol. 36:243-248(2017).
RN [29]
RP SUBUNIT.
RX PubMed=29950600; DOI=10.1038/s41598-018-28077-7;
RA Pavadai E., Gerstman B.S., Chapagain P.P.;
RT "A cylindrical assembly model and dynamics of the Ebola virus VP40
RT structural matrix.";
RL Sci. Rep. 8:9776-9776(2018).
RN [30]
RP ACETYLATION.
RX PubMed=30205953; DOI=10.1016/j.bbrc.2018.09.007;
RA Hatakeyama D., Ohmi N., Saitoh A., Makiyama K., Morioka M., Okazaki H.,
RA Kuzuhara T.;
RT "Acetylation of lysine residues in the recombinant nucleoprotein and VP40
RT matrix protein of Zaire Ebolavirus by eukaryotic histone
RT acetyltransferases.";
RL Biochem. Biophys. Res. Commun. 504:635-640(2018).
RN [31]
RP FUNCTION.
RX PubMed=29339477; DOI=10.1073/pnas.1712263115;
RA Takamatsu Y., Kolesnikova L., Becker S.;
RT "Ebola virus proteins NP, VP35, and VP24 are essential and sufficient to
RT mediate nucleocapsid transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:1075-1080(2018).
RN [32]
RP FUNCTION, INTERACTION WITH HOST SMURF2, DOMAIN, AND MUTAGENESIS OF
RP 10-PRO--TYR-13.
RX PubMed=33673144; DOI=10.3390/v13020288;
RA Shepley-McTaggart A., Schwoerer M.P., Sagum C.A., Bedford M.T.,
RA Jaladanki C.K., Fan H., Cassel J., Harty R.N.;
RT "Ubiquitin Ligase SMURF2 Interacts with Filovirus VP40 and Promotes Egress
RT of VP40 VLPs.";
RL Viruses 13:0-0(2021).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 55-194 IN COMPLEX WITH RNA.
RX PubMed=12679020; DOI=10.1016/s0969-2126(03)00050-9;
RA Gomis-Ruth F.X., Dessen A., Timmins J., Bracher A., Kolesnikowa L.,
RA Becker S., Klenk H.D., Weissenhorn W.;
RT "The matrix protein VP40 from Ebola virus octamerizes into pore-like
RT structures with specific RNA binding properties.";
RL Structure 11:423-433(2003).
CC -!- FUNCTION: Plays an essential role virus particle assembly and budding
CC (PubMed:16719918, PubMed:33673144). Acts by interacting with viral
CC ribonucleocapsid and host members of the ESCRT (endosomal sorting
CC complex required for transport) system such as host VPS4, PDCD6IP/ALIX,
CC NEDD4 or TGS101 (PubMed:15892969, PubMed:16719918, PubMed:23637409,
CC PubMed:25786915, PubMed:26753796, PubMed:27489272). The interaction
CC with host E3 ubiquitin ligase SMURF2 also facilitates virus budding
CC (PubMed:33673144). May play a role in immune cell dysfunction by being
CC packaged into exosomes that can decrease the viability of recipient
CC cells (via RNAi suppression and exosome-bystander apoptosis)
CC (PubMed:27872619). {ECO:0000269|PubMed:15892969,
CC ECO:0000269|PubMed:16719918, ECO:0000269|PubMed:23637409,
CC ECO:0000269|PubMed:25786915, ECO:0000269|PubMed:26753796,
CC ECO:0000269|PubMed:27489272, ECO:0000269|PubMed:27872619,
CC ECO:0000269|PubMed:33673144}.
CC -!- SUBUNIT: Homodimer (PubMed:23953110). Homohexamer (PubMed:23953110,
CC PubMed:11118208). Homooctamer (PubMed:12919741). Exists as a dimer
CC until it reorganizes at the plasma membrane into a hexameric form using
CC phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) (PubMed:23953110,
CC PubMed:25159197, PubMed:26753796, PubMed:29950600). Hexamers are
CC critical for budding (PubMed:23953110). Octamers function in genome
CC replication and RNA binding (PubMed:12919741). Interacts with host
CC TSG101 (PubMed:12559917). As a homohexamer, interacts with the WW
CC domain 3 of host NEDD4 (PubMed:11095724, PubMed:12559917). Interacts
CC with the nucleoprotein/NP (PubMed:17229682, PubMed:21987757). Interacts
CC (via YPx(n)L/I motif) with host PDCD6IP/ALIX; this interaction supports
CC efficient egress of viral particles (PubMed:25786915). Interacts with
CC VP35 (PubMed:16698994). Interacts with host ITCH; this interaction is
CC required for efficient egress (PubMed:27489272). Interacts (via PPXY
CC motif) with host SMURF2 (via WW domains); the interaction positively
CC regulates virus budding (PubMed:33673144).
CC {ECO:0000269|PubMed:11095724, ECO:0000269|PubMed:11118208,
CC ECO:0000269|PubMed:12559917, ECO:0000269|PubMed:12919741,
CC ECO:0000269|PubMed:16698994, ECO:0000269|PubMed:17229682,
CC ECO:0000269|PubMed:21987757, ECO:0000269|PubMed:23953110,
CC ECO:0000269|PubMed:25159197, ECO:0000269|PubMed:25786915,
CC ECO:0000269|PubMed:26753796, ECO:0000269|PubMed:27489272,
CC ECO:0000269|PubMed:29950600, ECO:0000269|PubMed:33673144}.
CC -!- INTERACTION:
CC Q05128; Q05128: VP40; NbExp=4; IntAct=EBI-25753960, EBI-25753960;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:21987757}.
CC Host cell membrane {ECO:0000269|PubMed:21987757,
CC ECO:0000269|PubMed:26753796, ECO:0000269|PubMed:28768865}. Virion
CC membrane {ECO:0000250|UniProtKB:P35260}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P35260}. Host late endosome membrane
CC {ECO:0000250|UniProtKB:P35260}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P35260}. Host cell membrane
CC {ECO:0000250|UniProtKB:P35260}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P35260}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P35260}. Host endomembrane system
CC {ECO:0000250|UniProtKB:P35260}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P35260}. Secreted, extracellular exosome
CC {ECO:0000269|PubMed:27872619}. Note=In virion, localizes on the inner
CC side of the membrane. In the host cell, it is found associated with
CC virus-induced membrane proliferation foci and probably also in
CC multivesicular bodies. These VP40-enriched membrane clusters are then
CC redistributed to the plasma membrane where budding takes place.
CC {ECO:0000250|UniProtKB:P35260}.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. VP40 contains two overlapping L domains: a
CC PTAP/PSAP motif, which interacts with the UEV domain of TSG101 and a
CC PPXY motif which interacts with the WW domain 3 of NEDD4 E3 ubiquitin
CC ligase and the three WW domains of SMURF2 E3 ubiquitin ligase.
CC {ECO:0000269|PubMed:11095724, ECO:0000269|PubMed:12559917,
CC ECO:0000269|PubMed:33673144}.
CC -!- PTM: Sumoylated with host SUMO1, SUMO2. Sumoylation provides stability
CC to VP40 (PubMed:27849047). Acetylated by host EP300 in vitro
CC (PubMed:30205953). {ECO:0000269|PubMed:27849047,
CC ECO:0000269|PubMed:30205953}.
CC -!- PTM: Ubiquitinated by host WWP1. This modification mediates efficient
CC viral budding. {ECO:0000269|PubMed:28768865}.
CC -!- MISCELLANEOUS: Most abundant protein in the virion.
CC -!- SIMILARITY: Belongs to the filoviridae matrix protein VP40 family.
CC {ECO:0000305}.
CC -!- CAUTION: Acetylation has been show in vitro using purified recombinant
CC proteins. This PTM is unsure util proven in vivo.
CC {ECO:0000269|PubMed:30205953}.
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DR EMBL; X61274; CAA43579.1; -; Genomic_RNA.
DR EMBL; L11365; AAB81003.1; -; Genomic_RNA.
DR EMBL; AF086833; AAD14583.1; -; Genomic_RNA.
DR EMBL; AF272001; AAG40166.1; -; Genomic_RNA.
DR EMBL; AF499101; AAM76033.1; -; Genomic_RNA.
DR EMBL; AY142960; AAN37506.1; -; Genomic_RNA.
DR RefSeq; NP_066245.1; NC_002549.1.
DR PDB; 1H2C; X-ray; 1.60 A; A=55-194.
DR PDB; 1H2D; X-ray; 2.60 A; A/B=31-212.
DR PDB; 2KQ0; NMR; -; B=5-16.
DR PDB; 4EJE; X-ray; 2.20 A; C/D=5-13.
DR PDB; 4LDB; X-ray; 3.10 A; A/B/C/D=44-326.
DR PDB; 4LDD; X-ray; 3.50 A; A/B/C=44-326.
DR PDB; 4LDI; X-ray; 4.15 A; A/B=44-326.
DR PDB; 4LDM; X-ray; 1.85 A; A=44-188.
DR PDB; 7JZJ; X-ray; 2.46 A; A/B/C/D=43-326.
DR PDB; 7JZT; X-ray; 3.77 A; A/B/C/D=43-326.
DR PDB; 7K5D; X-ray; 1.78 A; A=44-194.
DR PDB; 7K5L; X-ray; 1.38 A; A=44-194.
DR PDBsum; 1H2C; -.
DR PDBsum; 1H2D; -.
DR PDBsum; 2KQ0; -.
DR PDBsum; 4EJE; -.
DR PDBsum; 4LDB; -.
DR PDBsum; 4LDD; -.
DR PDBsum; 4LDI; -.
DR PDBsum; 4LDM; -.
DR PDBsum; 7JZJ; -.
DR PDBsum; 7JZT; -.
DR PDBsum; 7K5D; -.
DR PDBsum; 7K5L; -.
DR BMRB; Q05128; -.
DR SMR; Q05128; -.
DR ELM; Q05128; -.
DR TCDB; 9.A.73.1.1; the virus matrix protein (vmp) family.
DR DNASU; 911825; -.
DR GeneID; 911825; -.
DR KEGG; vg:911825; -.
DR EvolutionaryTrace; Q05128; -.
DR Proteomes; UP000007209; Genome.
DR Proteomes; UP000109874; Genome.
DR Proteomes; UP000149419; Genome.
DR Proteomes; UP000150973; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033645; C:host cell endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0044185; C:host cell late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044385; C:integral to membrane of host cell; IDA:CACAO.
DR GO; GO:0045121; C:membrane raft; IDA:CACAO.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0075733; P:intracellular transport of virus; IMP:CACAO.
DR GO; GO:0044414; P:suppression of host defenses by symbiont; IMP:CACAO.
DR GO; GO:0046755; P:viral budding; IMP:CACAO.
DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR DisProt; DP02967; -.
DR Gene3D; 2.60.510.10; -; 1.
DR Gene3D; 2.70.20.20; -; 1.
DR InterPro; IPR008986; EV_matrix.
DR InterPro; IPR035092; EV_matrix_protein_C.
DR InterPro; IPR043079; EV_matrix_protein_N.
DR InterPro; IPR038057; EV_matrix_sf.
DR Pfam; PF07447; VP40; 1.
DR PIRSF; PIRSF018327; VP40_FiloV; 1.
DR SUPFAM; SSF50012; SSF50012; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host cytoplasm; Host endosome;
KW Host membrane; Host-virus interaction; Isopeptide bond; Membrane;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Secreted;
KW Suppressor of RNA silencing; Ubl conjugation; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral immunoevasion;
KW Viral matrix protein; Viral release from host cell; Viral RNA replication;
KW Virion.
FT CHAIN 1..326
FT /note="Matrix protein VP40"
FT /id="PRO_0000222164"
FT REGION 212..214
FT /note="Important for oligomerization"
FT REGION 213..326
FT /note="Membrane-binding"
FT /evidence="ECO:0000250"
FT MOTIF 7..10
FT /note="PTAP/PSAP motif"
FT /evidence="ECO:0000269|PubMed:15892969"
FT MOTIF 10..13
FT /note="PPXY motif"
FT /evidence="ECO:0000269|PubMed:15892969"
FT MOTIF 18..26
FT /note="Essential for interaction with host PDCD6IP/ALIX"
FT /evidence="ECO:0000269|PubMed:25786915"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in host SUMO1 or SUMO2)"
FT /evidence="ECO:0000269|PubMed:27849047"
FT MUTAGEN 7
FT /note="P->A: Partial loss of budding."
FT /evidence="ECO:0000269|PubMed:16051823"
FT MUTAGEN 10..13
FT /note="PPEY->AAEA: Abolishes interaction with host SMURF2."
FT /evidence="ECO:0000269|PubMed:33673144"
FT MUTAGEN 10..11
FT /note="PP->AA: 90% loss of budding."
FT /evidence="ECO:0000269|PubMed:16051823"
FT MUTAGEN 11
FT /note="P->A: Complete loss of budding."
FT MUTAGEN 13
FT /note="Y->A: Complete loss of interaction with WW domain
FT containing proteins."
FT /evidence="ECO:0000269|PubMed:11095724"
FT MUTAGEN 125
FT /note="F->A: Partial loss of RNA-binding. Complete loss of
FT virus infectivity."
FT /evidence="ECO:0000269|PubMed:15650213"
FT MUTAGEN 134
FT /note="R->A: Complete loss of RNA-binding. Complete loss of
FT virus infectivity."
FT /evidence="ECO:0000269|PubMed:15650213"
FT MUTAGEN 212..214
FT /note="KLR->AAA: 85% loss of budding efficiency. Impaired
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:17699576"
FT MUTAGEN 212..214
FT /note="KLR->ALA: 80% loss of budding efficiency. No effect
FT on oligomerization."
FT /evidence="ECO:0000269|PubMed:17699576"
FT MUTAGEN 212..213
FT /note="KL->AA: 84% loss of budding efficiency. Impaired
FT oligomerization."
FT MUTAGEN 212
FT /note="K->A: 40% loss of budding efficiency. No effect on
FT oligomerization."
FT MUTAGEN 213..214
FT /note="LR->AA: 84% loss of budding efficiency. Impaired
FT oligomerization."
FT MUTAGEN 213
FT /note="L->A: 87% loss of budding efficiency. Impaired
FT oligomerization."
FT MUTAGEN 213
FT /note="L->I: 40% loss of budding efficiency."
FT MUTAGEN 214
FT /note="R->A: 65% loss of budding efficiency. No effect on
FT oligomerization."
FT MUTAGEN 326
FT /note="K->R: Complete loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:27849047"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:7JZJ"
FT STRAND 71..84
FT /evidence="ECO:0007829|PDB:7K5L"
FT STRAND 87..101
FT /evidence="ECO:0007829|PDB:7K5L"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:7K5L"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:7K5L"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:7K5L"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7JZJ"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:7K5L"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:7K5L"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:7K5L"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:7K5L"
FT STRAND 173..185
FT /evidence="ECO:0007829|PDB:7K5L"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:4LDB"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:7JZJ"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4LDB"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:7JZJ"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:7JZJ"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:4LDB"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7JZJ"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:7JZJ"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:7JZJ"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:7JZJ"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:7JZJ"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:7JZJ"
SQ 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
