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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
 
 
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