VP40_EBOSU
ID VP40_EBOSU Reviewed; 326 AA.
AC Q5XX06;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Sudan ebolavirus (strain Human/Uganda/Gulu/2000) (SEBOV) (Sudan Ebola
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=386033;
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=16139097; DOI=10.1016/j.virusres.2005.03.028;
RA Sanchez A., Rollin P.E.;
RT "Complete genome sequence of an Ebola virus (Sudan species) responsible for
RT a 2000 outbreak of human disease in Uganda.";
RL Virus Res. 113:16-25(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY729654; AAU43885.1; -; Genomic_RNA.
DR RefSeq; YP_138522.1; NC_006432.1.
DR PDB; 4LD8; X-ray; 1.83 A; A=44-326.
DR PDBsum; 4LD8; -.
DR SMR; Q5XX06; -.
DR PRIDE; Q5XX06; -.
DR GeneID; 3160775; -.
DR KEGG; vg:3160775; -.
DR Proteomes; UP000000277; 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 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host endosome; Host membrane;
KW Host-virus interaction; Membrane; Ribonucleoprotein; RNA-binding;
KW Suppressor of RNA silencing; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral matrix protein;
KW Viral release from host cell; Viral RNA replication; Virion.
FT CHAIN 1..326
FT /note="Matrix protein VP40"
FT /id="PRO_0000245082"
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 HELIX 61..63
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 71..83
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 86..101
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:4LD8"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 118..125
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:4LD8"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4LD8"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 173..185
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4LD8"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:4LD8"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:4LD8"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:4LD8"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:4LD8"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4LD8"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4LD8"
SQ SEQUENCE 326 AA; 35475 MW; 74BE224F8BD047F7 CRC64;
MRRVTVPTAP PAYADIGYPM SMLPIKSSRA VSGIQQKQEV LPGMDTPSNS MRPVADDNID
HTSHTPNGVA SAFILEATVN VISGPKVLMK QIPIWLPLGI ADQKTYSFDS TTAAIMLASY
TITHFGKANN PLVRVNRLGQ GIPDHPLRLL RMGNQAFLQE FVLPPVQLPQ YFTFDLTALK
LVTQPLPAAT WTDETPSNLS GALRPGLSFH PKLRPVLLPG KTGKKGHVSD LTAPDKIQTI
VNLMQDFKIV PIDPAKSIIG IEVPELLVHK LTGKKMSQKN GQPIIPVLLP KYIGLDPISP
GDLTMVITPD YDDCHSPASC SYLSEK
