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Matrix protein

 MATRX_VSIVA             Reviewed;         229 AA.
P03519;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
28-FEB-2018, entry version 94.
RecName: Full=Matrix protein;
Name=M;
Vesicular stomatitis Indiana virus (strain San Juan) (VSIV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Rhabdoviridae; Vesiculovirus.
NCBI_TaxID=11285;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=58271; Culicoides.
NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
NCBI_TaxID=9796; Equus caballus (Horse).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=252607; Lutzomyia.
NCBI_TaxID=7370; Musca domestica (House fly).
NCBI_TaxID=7190; Simuliidae (black flies).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6268840;
Rose J.K., Gallione C.J.;
"Nucleotide sequences of the mRNA's encoding the vesicular stomatitis
virus G and M proteins determined from cDNA clones containing the
complete coding regions.";
J. Virol. 39:519-528(1981).
[2]
SUBCELLULAR LOCATION.
PubMed=1850035;
Rigaut K.D., Birk D.E., Lenard J.;
"Intracellular distribution of input vesicular stomatitis virus
proteins after uncoating.";
J. Virol. 65:2622-2628(1991).
[3]
PHOSPHORYLATION.
STRAIN=Orsay;
PubMed=1323702;
Kaptur P.E., McCreedy B.J. Jr., Lyles D.S.;
"Sites of in vivo phosphorylation of vesicular stomatitis virus matrix
protein.";
J. Virol. 66:5384-5392(1992).
[4]
MUTAGENESIS OF MET-51.
PubMed=9733895;
Ahmed M., Lyles D.S.;
"Effect of vesicular stomatitis virus matrix protein on transcription
directed by host RNA polymerases I, II, and III.";
J. Virol. 72:8413-8419(1998).
[5]
INTERACTION WITH NUP98, AND MUTAGENESIS OF 5-LYS--ILE-7;
28-GLU--ASP-30; 42-ASP--SER-44; 52-ASP--TYR-54 AND 61-TYR--LYS-63.
PubMed=11106761; DOI=10.1016/S1097-2765(00)00120-9;
von Kobbe C., van Deursen J.M., Rodrigues J.P., Sitterlin D.,
Bachi A., Wu X., Wilm M., Carmo-Fonseca M., Izaurralde E.;
"Vesicular stomatitis virus matrix protein inhibits host cell gene
expression by targeting the nucleoporin Nup98.";
Mol. Cell 6:1243-1252(2000).
[6]
ALTERNATIVE INITIATION (ISOFORMS M2 AND M3).
PubMed=12134006; DOI=10.1128/JVI.76.16.8011-8018.2002;
Jayakar H.R., Whitt M.A.;
"Identification of two additional translation products from the matrix
(M) gene that contribute to vesicular stomatitis virus
cytopathology.";
J. Virol. 76:8011-8018(2002).
[7]
FUNCTION.
PubMed=16298982; DOI=10.1099/vir.0.81129-0;
Solon J., Gareil O., Bassereau P., Gaudin Y.;
"Membrane deformations induced by the matrix protein of vesicular
stomatitis virus in a minimal system.";
J. Gen. Virol. 86:3357-3363(2005).
[8]
FUNCTION, AND INTERACTION WITH HOST RAE1-NUP98 COMPLEX.
PubMed=15629720; DOI=10.1016/j.molcel.2004.11.023;
Faria P.A., Chakraborty P., Levay A., Barber G.N., Ezelle H.J.,
Enninga J., Arana C., van Deursen J., Fontoura B.M.;
"VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway.";
Mol. Cell 17:93-102(2005).
[9]
DOMAIN LATE-BUDDING.
PubMed=15220457; DOI=10.1128/JVI.78.14.7823-7827.2004;
Irie T., Licata J.M., Jayakar H.R., Whitt M.A., Bell P., Harty R.N.;
"Functional analysis of late-budding domain activity associated with
the PSAP motif within the vesicular stomatitis virus M protein.";
J. Virol. 78:7823-7827(2004).
[10]
CYTOPATHICITY.
PubMed=12692256; DOI=10.1128/JVI.77.9.5524-5528.2003;
Kopecky S.A., Lyles D.S.;
"The cell-rounding activity of the vesicular stomatitis virus matrix
protein is due to the induction of cell death.";
J. Virol. 77:5524-5528(2003).
[11]
DOMAIN LATE-BUDDING.
PubMed=16188963; DOI=10.1128/JVI.79.20.12617-12622.2005;
Irie T., Harty R.N.;
"L-domain flanking sequences are important for host interactions and
efficient budding of vesicular stomatitis virus recombinants.";
J. Virol. 79:12617-12622(2005).
[12]
MUTAGENESIS OF 121-ALA--ALA-124.
PubMed=16571787; DOI=10.1128/JVI.80.8.3701-3711.2006;
Connor J.H., McKenzie M.O., Lyles D.S.;
"Role of residues 121 to 124 of vesicular stomatitis virus matrix
protein in virus assembly and virus-host interaction.";
J. Virol. 80:3701-3711(2006).
[13]
FUNCTION, AND INTERACTION WITH HOST DYNAMIN.
PubMed=20943988; DOI=10.1128/JVI.01400-10;
Raux H., Obiang L., Richard N., Harper F., Blondel D., Gaudin Y.;
"The matrix protein of vesicular stomatitis virus binds dynamin for
efficient viral assembly.";
J. Virol. 84:12609-12618(2010).
[14]
INTERACTION WITH HOST NEDD4 AND TSG101, AND MUTAGENESIS OF LEU-4;
TYR-27 AND PRO-40.
STRAIN=Indiana (Orsay);
PubMed=22190013; DOI=10.1099/vir.0.039800-0;
Obiang L., Raux H., Ouldali M., Blondel D., Gaudin Y.;
"Phenotypes of vesicular stomatitis virus mutants with mutations in
the PSAP motif of the matrix protein.";
J. Gen. Virol. 93:857-865(2012).
-!- FUNCTION: Plays a major role in assembly and budding of virion, by
recruiting cellular partners of the ESCRT complexes that play a
key role in releasing the budding particle from the host membrane.
Condensates the ribonucleocapsid core during virus assembly.
{ECO:0000269|PubMed:16298982, ECO:0000269|PubMed:20943988}.
-!- FUNCTION: Shut off cellular protein expression by inhibiting mRNA
nuclear export through direct interaction with host RAE1-NUP98
complex. This shutoff presumably inhibits interferon signaling and
thus establishment of antiviral state in virus infected cells.
Induces cell-rounding, cytoskeleton disorganization and apoptosis
in infected cell. {ECO:0000269|PubMed:15629720}.
-!- SUBUNIT: Homomultimer. Interacts with viral nucleocapsid.
Interacts with host NEDD4 and TSG101 (PubMed:22190013). Interacts
with host dynamin (PubMed:20943988). Interacts with host RAE1-
NUP98 complex (PubMed:11106761, PubMed:15629720).
{ECO:0000269|PubMed:11106761, ECO:0000269|PubMed:15629720,
ECO:0000269|PubMed:20943988, ECO:0000269|PubMed:22190013}.
-!- SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein
{ECO:0000269|PubMed:1850035}. Host endomembrane system; Peripheral
membrane protein. Host nucleus membrane; Peripheral membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=3;
Name=M;
IsoId=P03519-1; Sequence=Displayed;
Name=M2 {ECO:0000303|PubMed:12134006};
IsoId=P03519-2; Sequence=VSP_025421;
Name=M3 {ECO:0000303|PubMed:12134006};
IsoId=P03519-3; Sequence=VSP_025420;
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle budding. They recruit proteins of the
host ESCRT machinery (Endosomal Sorting Complex Required for
Transport) or ESCRT-associated proteins. M contains two
overlapping L domains: a PPXY motif which interacts with the WW
domain 3 of NEDD4 and a PTAP/PSAP motif, which interacts with the
UEV domain of TSG101. {ECO:0000269|PubMed:15220457,
ECO:0000269|PubMed:16188963}.
-!- PTM: Phosphorylated by host. {ECO:0000269|PubMed:1323702}.
-!- BIOTECHNOLOGY: VSV is used as an oncolytic agent for cancer
therapy, because of his wide host range, rapid replication and
mild pathogenicity in humans. VSV used are mutated at M51R in
their matrix protein. These mutated viruses cannot successfully
infect normal cells, being unable to counteract the antiviral
state induced by interferon-alpha in normal cells. Cancer cells
are impeded with responsiveness to interferon, and then can be
successfully infected and lysed by the virus.
-!- MISCELLANEOUS: Most abundant protein in the virion.
-!- SIMILARITY: Belongs to the vesiculoviruses matrix protein family.
{ECO:0000305}.
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EMBL; J02428; AAA48369.1; -; Genomic_RNA.
RefSeq; NP_041714.1; NC_001560.1.
ProteinModelPortal; P03519; -.
SMR; P03519; -.
ELM; P03519; -.
IntAct; P03519; 3.
MINT; P03519; -.
GeneID; 1489833; -.
KEGG; vg:1489833; -.
OrthoDB; VOG090000OM; -.
Proteomes; UP000002327; Genome.
GO; GO:0044200; C:host cell nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IDA:UniProtKB.
GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
Gene3D; 3.10.460.10; -; 1.
InterPro; IPR009397; Vesiculo_matrix.
InterPro; IPR036711; VSV_matrix_sf.
Pfam; PF06326; Vesiculo_matrix; 1.
SUPFAM; SSF75404; SSF75404; 1.
1: Evidence at protein level;
Alternative initiation; Apoptosis; Complete proteome;
Eukaryotic host gene expression shutoff by virus;
Host gene expression shutoff by virus; Host membrane;
Host mRNA suppression by virus; Host nucleus; Host-virus interaction;
Inhibition of host mRNA nuclear export by virus; Membrane;
Phosphoprotein; Reference proteome; Viral budding;
Viral budding via the host ESCRT complexes; Viral matrix protein;
Viral release from host cell; Virion.
CHAIN 1 229 Matrix protein.
/FTId=PRO_0000222857.
MOTIF 2 4 dynamin binding.
{ECO:0000269|PubMed:20943988}.
MOTIF 24 27 PPXY motif.
MOTIF 37 40 PTAP/PSAP motif.
VAR_SEQ 1 50 Missing (in isoform M3). {ECO:0000305}.
/FTId=VSP_025420.
VAR_SEQ 1 32 Missing (in isoform M2). {ECO:0000305}.
/FTId=VSP_025421.
MUTAGEN 4 4 L->A: No effect on host NEDD4 or TSG101
binding. {ECO:0000269|PubMed:11106761}.
MUTAGEN 5 7 KKI->AAA: No effect on mRNA nuclear
export inhibition.
{ECO:0000269|PubMed:11106761}.
MUTAGEN 27 27 Y->A: Partial loss of host NEDD4 binding.
{ECO:0000269|PubMed:22190013}.
MUTAGEN 28 30 EED->AAA: No effect on mRNA nuclear
export inhibition.
{ECO:0000269|PubMed:11106761}.
MUTAGEN 40 40 P->A: Partial loss of host TSG101
binding. {ECO:0000269|PubMed:22190013}.
MUTAGEN 42 44 DKS->AAA: No effect on mRNA nuclear
export inhibition.
{ECO:0000269|PubMed:11106761}.
MUTAGEN 51 51 M->R: Complete loss of mRNA nuclear
export inhibition.
{ECO:0000269|PubMed:9733895}.
MUTAGEN 52 54 DTY->AAA: Complete loss of mRNA nuclear
export inhibition.
{ECO:0000269|PubMed:11106761}.
MUTAGEN 61 63 YEK->AAA: No effect on mRNA nuclear
export inhibition.
{ECO:0000269|PubMed:11106761}.
MUTAGEN 121 124 AVLA->DKQQ: No effect on virion budding.
Increase viral-mRNA translation.
{ECO:0000269|PubMed:16571787}.
SEQUENCE 229 AA; 26094 MW; C89E2ACA4365B847 CRC64;
MSSLKKILGL KGKGKKSKKL GIAPPPYEED TSMEYAPSAP IDKSYFGVDE MDTYDPNQLR
YEKFFFTVKM TVRSNRPFRT YSDVAAAVSH WDHMYIGMAG KRPFYKILAF LGSSNLKATP
AVLADQGQPE YHTHCEGRAY LPHRMGKTPP MLNVPEHFRR PFNIGLYKGT IELTMTIYDD
ESLEAAPMIW DHFNSSKFSD FREKALMFGL IVEKKASGAW VLDSISHFK


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