MATRX_VSNJO
ID MATRX_VSNJO Reviewed; 229 AA.
AC P08325;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Matrix protein;
GN Name=M;
OS Vesicular stomatitis New Jersey virus (strain Ogden subtype Concan)
OS (VSNJV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11283;
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 [MRNA].
RX PubMed=3006343; DOI=10.1016/0042-6822(86)90293-x;
RA Gill D.S., Banerjee A.K.;
RT "Complete nucleotide sequence of the matrix protein mRNA of vesicular
RT stomatitis virus (New Jersey serotype).";
RL Virology 150:308-312(1986).
RN [2]
RP MUTAGENESIS OF MET-48 AND MET-51.
RC STRAIN=Hazelhurst;
RX PubMed=16962155; DOI=10.1016/j.virol.2006.07.022;
RA Kim G.N., Kang C.Y.;
RT "Matrix protein of VSV New Jersey serotype containing methionine to
RT arginine substitutions at positions 48 and 51 allows near-normal host cell
RT gene expression.";
RL Virology 357:41-53(2007).
CC -!- FUNCTION: Plays a major role in assembly and budding of virion.
CC Condensates the ribonucleocapsid core during virus assembly. Shut off
CC cellular transcription by inhibiting mRNA nuclear export through direct
CC interaction with host RAE1-NUP98 complex. This shutoff presumably
CC inhibits interferon signaling and thus establishment of antiviral state
CC in virus infected cells. Induces cell-rounding, cytoskeleton
CC disorganization and apoptosis in infected cell (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer. Interacts with viral nucleocapsid. Interacts
CC with host RAE1-NUP98 complex (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P08325; Q12906: ILF3; Xeno; NbExp=2; IntAct=EBI-15693250, EBI-78756;
CC -!- SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein.
CC Host endomembrane system; Peripheral membrane protein. Host nucleus
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=M;
CC IsoId=P08325-1; Sequence=Displayed;
CC Name=M2;
CC IsoId=P08325-2; Sequence=VSP_025423;
CC Name=M3;
CC IsoId=P08325-3; Sequence=VSP_025422;
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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by host. {ECO:0000250}.
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; M14553; AAA48443.1; -; mRNA.
DR PIR; A27254; MFVNVJ.
DR PDB; 2W2R; X-ray; 1.83 A; A=2-229.
DR PDBsum; 2W2R; -.
DR SMR; P08325; -.
DR IntAct; P08325; 2.
DR EvolutionaryTrace; P08325; -.
DR Proteomes; UP000007626; Genome.
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:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
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;
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_0000222856"
FT REGION 1..35
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_025422"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform M2)"
FT /evidence="ECO:0000305"
FT /id="VSP_025423"
FT MUTAGEN 48
FT /note="M->R: Partial loss of cytopathicity."
FT /evidence="ECO:0000269|PubMed:16962155"
FT MUTAGEN 51
FT /note="M->R: Complete loss of cytopathicity."
FT /evidence="ECO:0000269|PubMed:16962155"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2W2R"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2W2R"
FT STRAND 60..76
FT /evidence="ECO:0007829|PDB:2W2R"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:2W2R"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:2W2R"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2W2R"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:2W2R"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2W2R"
FT STRAND 130..143
FT /evidence="ECO:0007829|PDB:2W2R"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:2W2R"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:2W2R"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:2W2R"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:2W2R"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:2W2R"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2W2R"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2W2R"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2W2R"
SQ SEQUENCE 229 AA; 26229 MW; 6F826255C461C053 CRC64;
MSSFKKILGL SSKSHKKSKK MGLPPPYDES CPMETQPSAP LSNDFFGMED MDLYDKDSLR
YEKFRFMLKM TVRSNKPFRS YDDVTAAVSQ WDNSYIGMVG KRPFYKIIAV IGSSHLQATP
AVLADLNQPE YYATLTGRCF LPHRLGLIPP MFNVQETFRK PFNIGLYKGT LDFTFTVSDD
ESNEKVPHVW DYMNPKYQSQ IQQEGLKFGL ILSKKATGTW VLDQLSPFK
