VP40_EBOG4
ID VP40_EBOG4 Reviewed; 326 AA.
AC Q2PDK5; Q913A4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 29-SEP-2021, entry version 80.
DE RecName: Full=Matrix protein VP40;
DE AltName: Full=Ebola VP40 {ECO:0000250|UniProtKB:Q05128};
DE Short=eVP40 {ECO:0000250|UniProtKB:Q05128};
DE AltName: Full=Membrane-associated protein VP40;
GN Name=VP40;
OS Zaire ebolavirus (strain Gabon-94) (ZEBOV) (Zaire Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128947;
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 [MRNA].
RA Prehaud C.J.;
RT "VP40 of Ebola virus Gabon 94 strain.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate Bouee-96;
RX PubMed=11752702; DOI=10.1099/0022-1317-83-1-67;
RA Leroy E.M., Baize S., Mavoungou E., Apetrei C.;
RT "Sequence analysis of the GP, NP, VP40 and VP24 genes of Ebola virus
RT isolated from deceased, surviving and asymptomatically infected individuals
RT during the 1996 outbreak in Gabon: comparative studies and phylogenetic
RT characterization.";
RL J. Gen. Virol. 83:67-73(2002).
CC -!- FUNCTION: Plays an essential role virus particle assembly and budding.
CC Acts by interacting with viral ribonucleocapsid and host members of the
CC ESCRT (endosomal sorting complex required for transport) system such as
CC host VPS4, PDCD6IP/ALIX, NEDD4 or TGS101. The interaction with host E3
CC ubiquitin ligase SMURF2 also facilitates virus budding. May play a role
CC in immune cell dysfunction by being packaged into exosomes that can
CC decrease the viability of recipient cells (via RNAi suppression and
CC exosome-bystander apoptosis). {ECO:0000250|UniProtKB:Q05128}.
CC -!- SUBUNIT: Homodimer. Homohexamer. Homooctamer. Exists as a dimer until
CC it reorganizes at the plasma membrane into a hexameric form using
CC phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). Hexamers are
CC critical for budding. Octamers function in genome replication and RNA
CC binding. Interacts with host TSG101. As a homohexamer, interacts with
CC the WW domain 3 of host NEDD4. Interacts with the nucleoprotein/NP.
CC Interacts (via YPx(n)L/I motif) with host PDCD6IP/ALIX; this
CC interaction supports efficient egress of viral particles. Interacts
CC with VP35. Interacts with host ITCH; this interaction is required for
CC efficient egress. Interacts (via PPXY motif) with host SMURF2 (via WW
CC domains); the interaction positively regulates virus budding.
CC {ECO:0000250|UniProtKB:Q05128}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:Q05128}.
CC Host cell membrane {ECO:0000250|UniProtKB:Q05128}. Virion membrane
CC {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:0000250|UniProtKB:Q05128}. 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:0000250|UniProtKB:Q05128}.
CC -!- PTM: Sumoylated with host SUMO1, SUMO2. Sumoylation provides stability
CC to VP40. {ECO:0000250|UniProtKB:Q05128}.
CC -!- PTM: Ubiquitinated by host WWP1. This modification mediates efficient
CC viral budding. {ECO:0000250|UniProtKB:Q05128}.
CC -!- MISCELLANEOUS: Most abundant protein in the virion.
CC {ECO:0000250|UniProtKB:Q05128}.
CC -!- SIMILARITY: Belongs to the filoviridae matrix protein VP40 family.
CC {ECO:0000305}.
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DR EMBL; AJ001707; CAC79598.1; -; mRNA.
DR EMBL; AY058896; AAL25816.1; -; mRNA.
DR SMR; Q2PDK5; -.
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:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Host cell membrane; Host cytoplasm; Host endosome; Host membrane;
KW Host-virus interaction; Isopeptide bond; Membrane; Ribonucleoprotein;
KW RNA-binding; Secreted; Suppressor of RNA silencing; Ubl conjugation;
KW Viral budding; Viral budding via the host ESCRT complexes;
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_0000245079"
FT REGION 212..214
FT /note="Important for oligomerization"
FT /evidence="ECO:0000250"
FT REGION 213..326
FT /note="Membrane-binding"
FT /evidence="ECO:0000250"
FT MOTIF 7..10
FT /note="PTAP/PSAP motif"
FT MOTIF 10..13
FT /note="PPXY motif"
FT VARIANT 65
FT /note="T -> I (in strain: Isolate Bouee-96)"
FT VARIANT 233
FT /note="F -> S (in strain: Isolate Bouee-96)"
FT VARIANT 247
FT /note="L -> F (in strain: Isolate Bouee-96)"
SQ SEQUENCE 326 AA; 35209 MW; 8C67320BA6FAD51F CRC64;
MRRVILPTAP PEYMEAIYPV RSNSTIARGG NSNTGFLTPE SVNGDTPSNP LRPIADDTID
HASHTPGSVS SAFILEAMVN VISGPKVLMK QIPIWLPLGV ADQKTYSFDS TTAAIMLASY
TITHFGKATN PLVRVNRLGP GIPDHPLRLL RIGNQAFLQE FVLPPVQLPQ YFTFDLTALK
LITQPLPAAT WTDDTPTGSN GALRPGISFH PKLRPILLPN KSGKKGNSAD LTFPEKIQAI
MTSLQDLKIV PIDPTKNIMG IEVPETLVHK LTGKKVTSKN GQPIIPVLLP KYIGLDPVAP
GDLTMVITQD CDTCHSPASL PAVIEK
