MATRX_VSIVS
ID MATRX_VSIVS Reviewed; 229 AA.
AC Q8B0H7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 23-FEB-2022, entry version 77.
DE RecName: Full=Matrix protein {ECO:0000250|UniProtKB:P03519};
DE Short=M protein {ECO:0000250|UniProtKB:P03519};
GN Name=M;
OS Vesicular stomatitis Indiana virus (strain 85CLB South America) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=434490;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=58271; Culicoides.
OH NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=252607; Lutzomyia.
OH NCBI_TaxID=7370; Musca domestica (House fly).
OH NCBI_TaxID=7190; Simuliidae (black flies).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12237430; DOI=10.1099/0022-1317-83-10-2475;
RA Rodriguez L.L., Pauszek S.J., Bunch T.A., Schumann K.R.;
RT "Full-length genome analysis of natural isolates of vesicular stomatitis
RT virus (Indiana 1 serotype) from North, Central and South America.";
RL J. Gen. Virol. 83:2475-2483(2002).
CC -!- FUNCTION: Plays a major role in assembly and budding of virion, by
CC recruiting cellular partners of the ESCRT complexes that play a key
CC role in releasing the budding particle from the host membrane.
CC Condensates the ribonucleocapsid core during virus assembly.
CC {ECO:0000250|UniProtKB:P03519}.
CC -!- FUNCTION: Inhibits mRNA nuclear export through direct interaction with
CC host RAE1-NUP98 complex, thereby preventing interferon signaling and
CC establishment of antiviral state in infected cells. Induces cell-
CC rounding, cytoskeleton disorganization and apoptosis in infected cell.
CC Inhibits host transcription, possibly through interaction with host DNA
CC repair factor IIH/TFIIH GTF2H5 subunit (By similarity).
CC {ECO:0000250|UniProtKB:P03519}.
CC -!- SUBUNIT: Homomultimer. Interacts with viral nucleocapsid. Interacts
CC with host NEDD4 and TSG101. Interacts with host dynamin. Interacts with
CC host RAE1-NUP98 complex. Interacts with host NDUFAF4; the interaction
CC inhibits viral propagation and is independent of interferon activation.
CC Interacts with host GTF2H5; the interaction may inhibit host
CC transcription. {ECO:0000250|UniProtKB:P03519}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P03519};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host
CC endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane
CC {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P03519}. Host nucleus
CC {ECO:0000250|UniProtKB:P03519}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P03519}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=M;
CC IsoId=Q8B0H7-1; Sequence=Displayed;
CC Name=M2;
CC IsoId=Q8B0H7-2; Sequence=VSP_025413;
CC Name=M3;
CC IsoId=Q8B0H7-3; Sequence=VSP_025412;
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. M contains two overlapping L domains: a PPXY
CC motif which interacts with the WW domain 3 of NEDD4 and a PTAP/PSAP
CC motif, which interacts with the UEV domain of TSG101.
CC {ECO:0000250|UniProtKB:P03519}.
CC -!- PTM: Phosphorylated by host. {ECO:0000250|UniProtKB:P03519}.
CC -!- BIOTECHNOLOGY: VSV is used as an oncolytic agent for cancer therapy,
CC because of his wide host range, rapid replication and mild
CC pathogenicity in humans. VSV used are mutated at M51R in their matrix
CC protein. These mutated viruses cannot successfully infect normal cells,
CC being unable to counteract the antiviral state induced by interferon-
CC alpha in normal cells. Cancer cells are impeded with responsiveness to
CC interferon, and then can be successfully infected and lysed by the
CC virus.
CC -!- MISCELLANEOUS: Most abundant protein in the virion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vesiculoviruses matrix protein family.
CC {ECO:0000305}.
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DR EMBL; AF473865; AAN16987.1; -; Genomic_RNA.
DR PDB; 4OWR; X-ray; 3.15 A; C=44-229.
DR PDBsum; 4OWR; -.
DR SMR; Q8B0H7; -.
DR Proteomes; UP000007625; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044200; C:host cell nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:InterPro.
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:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR GO; GO:0039602; P:suppression by virus of host transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR Gene3D; 3.10.460.10; -; 1.
DR InterPro; IPR009397; Vesiculo_matrix.
DR InterPro; IPR036711; VSV_matrix_sf.
DR Pfam; PF06326; Vesiculo_matrix; 1.
DR SUPFAM; SSF75404; SSF75404; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Apoptosis;
KW Eukaryotic host gene expression shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host membrane;
KW Host mRNA suppression by virus; Host nucleus; Host-virus interaction;
KW Inhibition of host mRNA nuclear export by virus; Membrane; Phosphoprotein;
KW Viral budding; Viral budding via the host ESCRT complexes;
KW Viral matrix protein; Viral release from host cell; Virion.
FT CHAIN 1..229
FT /note="Matrix protein"
FT /id="PRO_0000287257"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 24..27
FT /note="PPXY motif"
FT MOTIF 37..40
FT /note="PTAP/PSAP motif"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform M3)"
FT /evidence="ECO:0000305"
FT /id="VSP_025412"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform M2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025413"
FT STRAND 60..76
FT /evidence="ECO:0007829|PDB:4OWR"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:4OWR"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4OWR"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4OWR"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:4OWR"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4OWR"
FT STRAND 130..143
FT /evidence="ECO:0007829|PDB:4OWR"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:4OWR"
FT STRAND 167..179
FT /evidence="ECO:0007829|PDB:4OWR"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4OWR"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:4OWR"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:4OWR"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4OWR"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:4OWR"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:4OWR"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:4OWR"
SQ SEQUENCE 229 AA; 26024 MW; BE54567021F5B853 CRC64;
MSSLKKILGL KGKGKKSKKL GIAPPPYEED TSMEYAPSAP IDKSYFGVDE MDTHDPNQLR
YEKFFFTVKM TVRSNRPFRT YSDVAAAVSH WDHMYIGMAG KRPFYKILAF LGSSNLKATP
AVLADQGQPE YHAHCEGRAY LPHRMGKTPP MLNVPEHFRR PFNIGLYKGT IELTMTIYDD
ESLEAAPMIW DHFNSSKFSD FREKALMFGL IVEKKASGAW VLDSVSHFK
