Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Matrix protein 2

Gene

M

Organism
Influenza A virus (A/Chiba/5/71(H3N2))
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.SAAS annotation

Enzyme regulationi

The M2 protein from most influenza A strains is inhibited by amantadine and rimantadine, resulting in viral uncoating incapacity. Emergence of amantadine-resistant variants is usually rapid.UniRule annotation

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. suppression by virus of host autophagy Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ion channelUniRule annotationSAAS annotation

Keywords - Biological processi

Host-virus interaction, Hydrogen ion transportUniRule annotationSAAS annotation, Inhibition of host autophagy by virusSAAS annotation, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix protein 2UniRule annotationSAAS annotation
Gene namesi
Name:MImported
OrganismiInfluenza A virus (A/Chiba/5/71(H3N2))Imported
Taxonomic identifieri221020 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

  1. Virion membrane UniRule annotationSAAS annotation
  2. Host apical cell membrane UniRule annotationSAAS annotation; Single-pass type III membrane protein UniRule annotationSAAS annotation

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneUniRule annotationSAAS annotation, Host membrane, Membrane, VirionUniRule annotationSAAS annotation

PTM / Processingi

Keywords - PTMi

Disulfide bondSAAS annotation, PhosphoproteinSAAS annotation

Interactioni

Subunit structurei

Homotetramer; composed of two disulfide-linked dimers held together by non-covalent interactions. May interact with matrix protein 1.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LY0NMR-A/B/C/D19-49[»]
ProteinModelPortaliQ6XT21.
SMRiQ6XT21. Positions 23-60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Cytoplasmic tail plays an important role in virion assembly and morphogenesis.UniRule annotation

Sequence similaritiesi

Belongs to the influenza viruses matrix protein M2 family.UniRule annotation

Keywords - Domaini

Signal-anchorUniRule annotation, Transmembrane, Transmembrane helixUniRule annotationSAAS annotation

Family and domain databases

InterProiIPR002089. Flu_M2.
[Graphical view]
PfamiPF00599. Flu_M2. 1 hit.
[Graphical view]
ProDomiPD001031. Flu_M2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

Q6XT21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLTEVETP IRNEWGCRCN DSSDPLVVAA NIIGILHLIL WILDRLFFKC
60 70 80 90
IYRFFEHGLK RGPSTEGVPE SMREEYRKEQ QSAVDADDSH FVSIELE
Length:97
Mass (Da):11,213
Last modified:July 5, 2004 - v1
Checksum:i3CDD5C08FD6AF754
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY210265 Genomic RNA. Translation: AAO46704.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY210265 Genomic RNA. Translation: AAO46704.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LY0NMR-A/B/C/D19-49[»]
ProteinModelPortaliQ6XT21.
SMRiQ6XT21. Positions 23-60.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR002089. Flu_M2.
[Graphical view]
PfamiPF00599. Flu_M2. 1 hit.
[Graphical view]
ProDomiPD001031. Flu_M2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

  1. "Genetic analysis of human H2N2 and early H3N2 influenza viruses, 1957-1972: evidence for genetic divergence and multiple reassortment events."
    Lindstrom S.E., Cox N.J., Klimov A.
    Virology 328:101-119(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Chiba/5/71Imported.
  2. "Structure and inhibition of the drug-resistant S31N mutant of the M2 ion channel of influenza A virus."
    Wang J., Wu Y., Ma C., Fiorin G., Wang J., Pinto L.H., Lamb R.A., Klein M.L., Degrado W.F.
    Proc. Natl. Acad. Sci. U.S.A. 110:1315-1320(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 19-49.

Entry informationi

Entry nameiQ6XT21_9INFA
AccessioniPrimary (citable) accession number: Q6XT21
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: April 29, 2015
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.