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P04876 (MATRX_VSIVG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a major role in assembly and budding of virion. Condensates the ribonucleocapsid core during virus assembly. Shut off cellular transcription by inhibiting mRNA nuclear export through direct interaction with host RAE1-NUP98 complex. This shut off presumably inhibit interferon signaling and thus establishment of antiviral state in virus infected cells. Induces cell-rounding, cytoskeleton disorganization and apoptosis in infected cell By similarity.

Subunit structure

Homomultimer. Interacts with viral nucleocapsid. Interacts with host RAE1-NUP98 complex By similarity.

Subcellular location

Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host nucleus membrane; Peripheral membrane protein By similarity.

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 By similarity.

Post-translational modification

Phosphorylated by host By similarity.

Biotechnological use

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 By similarity.

Sequence similarities

Belongs to the vesiculoviruses matrix protein family.

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]
Isoform M (identifier: P04876-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform M2 (identifier: P04876-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
Isoform M3 (identifier: P04876-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237Matrix protein
PRO_0000222855

Regions

Motif24 – 274PPXY motif
Motif37 – 404PTAP/PSAP motif

Natural variations

Alternative sequence1 – 5050Missing in isoform M3.
VSP_025418
Alternative sequence1 – 3232Missing in isoform M2.
VSP_025419

Experimental info

Sequence conflict321S → N in AAA48444. Ref.2
Sequence conflict641S → F in AAA48444. Ref.2
Sequence conflict2151E → K in AAA48444. Ref.2
Sequence conflict2281S → F in AAA48444. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform M [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: C1DF0CF71510959D

FASTA23726,825
        10         20         30         40         50         60 
MSSLKKILGL KGKGKKSKKL GIAPPPYEED TSMEYAPSAP IDKSYFGVDE MDTHDPNQLR 

        70         80         90        100        110        120 
YEKSFFTVKM TVRSNRPFRT YSDVAAAVSH WDHMYIGMAG KRPFYKILAF LGSSNLKATP 

       130        140        150        160        170        180 
AVLADQGQPE YHAHCEGRAY LPHRMGKTPP MLNVPEHFRR PFNIGLYKGT IELTMTIYDD 

       190        200        210        220        230 
ESLEAAPMIW DHFNSSKFSD FREKALMFGL IVEEEASGAW VLDSVRHSKW ASLASSF 

« Hide

Isoform M2 [UniParc].

Checksum: 4A241ED12D67D81F
Show »

FASTA20523,413
Isoform M3 [UniParc].

Checksum: 01895063A635E892
Show »

FASTA18721,411

References

[1]"Evolution of vesicular stomatitis virus in athymic nude mice: mutations associated with natural killer cell selection."
Vandepol S.B., Holland J.J.
J. Gen. Virol. 67:441-451(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Sequence alterations in temperature-sensitive M-protein mutants (complementation group III) of vesicular stomatitis virus."
Gopalakrishna Y., Lenard J.
J. Virol. 56:655-659(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04452 Genomic RNA. Translation: CAA28051.1.
M11754 Genomic RNA. Translation: AAA48444.1.
PIRMFVNGG. A04112.

3D structure databases

ProteinModelPortalP04876.
SMRP04876. Positions 58-227.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.460.10. 1 hit.
InterProIPR009397. Vesiculo_matrix.
[Graphical view]
PfamPF06326. Vesiculo_matrix. 1 hit.
[Graphical view]
SUPFAMSSF75404. Vesiculo_matrix. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMATRX_VSIVG
AccessionPrimary (citable) accession number: P04876
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families