VP40_EBORE
ID VP40_EBORE Reviewed; 331 AA.
AC Q91DD9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 23-FEB-2022, entry version 100.
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 Reston ebolavirus (strain Philippines-96) (REBOV) (Reston Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=129003;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH NCBI_TaxID=77225; Pteropodinae.
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11722021; DOI=10.1007/s007050170049;
RA Ikegami T., Calaor A.B., Miranda M.E., Niikura M., Saijo M., Kurane I.,
RA Yoshikawa Y., Morikawa S.;
RT "Genome structure of Ebola virus subtype Reston: differences among Ebola
RT subtypes.";
RL Arch. Virol. 146:2021-2027(2001).
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: Virion membrane {ECO:0000250|UniProtKB:P35260};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P35260}. Host late
CC endosome membrane {ECO:0000250|UniProtKB:P35260}; Peripheral membrane
CC protein {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}. Note=In virion, localizes on the
CC intravirional side of the membrane. In the host cell, it is found
CC associated with virus-induced membrane proliferation foci and probably
CC also in multivesicular bodies. These VP40-enriched membrane clusters
CC are then redistributed to the plasma membrane where budding takes
CC place. {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 -!- MISCELLANEOUS: Most abundant protein in the virion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the filoviridae matrix protein VP40 family.
CC {ECO:0000305}.
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DR EMBL; AB050936; BAB69005.1; -; Genomic_RNA.
DR SMR; Q91DD9; -.
DR Proteomes; UP000002322; Genome.
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 3: Inferred from homology;
KW Host cell membrane; Host endosome; Host membrane; Host-virus interaction;
KW Membrane; Ribonucleoprotein; RNA-binding; Suppressor of RNA silencing;
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..331
FT /note="Matrix protein VP40"
FT /id="PRO_0000245080"
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"
SQ SEQUENCE 331 AA; 35863 MW; C5FEB11D60218C20 CRC64;
MRRGVLPTAP PAYNDIAYSM SILPTRPSVI VNETKSDVLA VPGADVPSNS MRPVADDNID
HSSHTPSGVA SAFILEAKVN VISGTKVLMK QIPIWLPLGV ADQKIYSFDS TTAAIMLASY
TVTHFGKISN PLVRVNRLGP GIPDHPLRLL RLGNQAFLQE FVLPPVQLPQ YFTFDLTALK
LITQPLPAAT WTDETPAGAV NALRPGLSLH PKLRPILLPG KIGKKGHASD LTSPDKIQTI
MNAIPDLKIV PIDPIKNIVG IEVPELLVQR LTGKKPQPKN GQPIIPVLLP KYVGLDPISP
GDLTMVITQD CDSCHSPASH PYHMDKQDSY Q
