VP40_MABVR
ID VP40_MABVR Reviewed; 303 AA.
AC Q1PDC8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Matrix protein VP40;
DE AltName: Full=Marburg VP40 {ECO:0000250|UniProtKB:P35260};
DE Short=mVP40 {ECO:0000250|UniProtKB:P35260};
DE AltName: Full=Membrane-associated protein VP40;
GN Name=VP40;
OS Lake Victoria marburgvirus (strain Ravn-87) (MARV) (Marburg virus (strain
OS Kenya/Ravn/1987)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=378809;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16775337; DOI=10.1128/jvi.00069-06;
RA Towner J.S., Khristova M.L., Sealy T.K., Vincent M.J., Erickson B.R.,
RA Bawiec D.A., Hartman A.L., Comer J.A., Zaki S.R., Stroeher U.,
RA Gomes da Silva F., del Castillo F., Rollin P.E., Ksiazek T.G., Nichol S.T.;
RT "Marburgvirus genomics and association with a large hemorrhagic fever
RT outbreak in Angola.";
RL J. Virol. 80:6497-6516(2006).
CC -!- FUNCTION: Plays an essential role virus particle assembly and budding.
CC Promotes virus assembly and budding by interacting with host proteins
CC of the multivesicular body pathway. The interaction with host E3
CC ubiquitin ligase SMURF2 facilitates virus budding (By similarity). The
CC interaction with the nucleocapsid and the plasma membrane may also
CC facilitate virus budding. Specific interactions with membrane-
CC associated GP and VP24 during the budding process may also occur (By
CC similarity). May play a role in genome replication (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P35260}.
CC -!- SUBUNIT: Exists as a dimer until it reorganizes at the plasma membrane
CC into multimeric form. Interacts with host TSG101. Interacts (via PPXY
CC motif) with SMURF2 (via WW domains); the interaction positively
CC regulates virus budding. {ECO:0000250|UniProtKB:P35260}.
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 one L domain: a PPXY motif
CC which potentially 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:P35260, ECO:0000250|UniProtKB:Q05128}.
CC -!- MISCELLANEOUS: Most abundant protein in the virion.
CC -!- SIMILARITY: Belongs to the filoviridae matrix protein VP40 family.
CC {ECO:0000305}.
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DR EMBL; DQ447649; ABE27070.1; -; Genomic_RNA.
DR SMR; Q1PDC8; -.
DR Proteomes; UP000008239; 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:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0039576; P:suppression by virus of host JAK-STAT cascade via inhibition of JAK1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 2.70.20.20; -; 1.
DR InterPro; IPR008986; EV_matrix.
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; 1.
PE 3: Inferred from homology;
KW Host cell membrane; Host endosome; Host membrane; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host JAK1 by virus; Membrane; Reference proteome;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral immunoevasion; Viral matrix protein; Viral release from host cell;
KW Virion.
FT CHAIN 1..303
FT /note="Matrix protein VP40"
FT /id="PRO_0000315000"
FT MOTIF 16..19
FT /note="PPXY motif"
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 33718 MW; EE9040B31F9AD59E CRC64;
MASSSNYNTY MQYLNPPPYA DHGANQLIPA DQLSNQHGIT PNYVGDLNLD DQFKGNVCHA
FTLEAIIDIS AYNERTVKGV PAWLPLGIMS NFEYPLAHTV AALLTGSYTI TQFTHNGQKF
VRVNRLGTGI PAHPLRMLRE GNQAFVQNMV IPRNFSTNQF TYNLTNLVLS VQKLPDDAWR
PSKDKLIGNT MHPAVSVHPN LPPIVLPTVK KQAYRQHKNP NNGPLLAISG ILHQLRVEKV
PEKTSLFRIS LPADMFSVKE GMMKKRGEGS PVVYFQAPEN FPLNGFNNRQ VVLAYANPTL
SAV
