GENTAUR Molecular Products.

 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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 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 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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