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: -Experimental evidence at protein leveli

Functioni

Miscellaneous

When the channel is activated, one or more imidazole moities of His-37 probably become bi-protonated.UniRule 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei37Essential for channel activity, possibly by being protonated during channel activation, and by forming the channel gate and the selective filterUniRule annotation1
Sitei41Seems to be involved in pH gatingUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIon channel, Viral ion channelUniRule annotationSAAS annotation
Biological processHost-virus interaction, Hydrogen ion transportUniRule annotationSAAS annotation, Inhibition of host autophagy by virusUniRule annotationSAAS annotation, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix protein 2UniRule annotationSAAS annotation
Alternative name(s):
Proton channel protein M2UniRule annotation
Gene namesi
Name:MUniRule annotationImported
OrganismiInfluenza A virus (A/Chiba/5/71(H3N2))Imported
Taxonomic identifieri221020 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

Subcellular locationi

  • Host apical cell membrane SAAS annotation; Single-pass type III membrane protein SAAS annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 22Virion surfaceUniRule annotationAdd BLAST22
Transmembranei25 – 43HelicalSequence analysisAdd BLAST19
Topological domaini44 – 97IntravirionUniRule annotationAdd BLAST54

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi17Interchain (with Cys-17)UniRule annotation
Disulfide bondi19Interchain (with Cys-19)UniRule annotation
Glycosylationi20N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Lipidationi50S-palmitoyl cysteine; by hostUniRule annotation1
Modified residuei64Phosphoserine; by hostUniRule annotation1
Modified residuei82Phosphoserine; by hostUniRule annotation1
Modified residuei93Phosphoserine; by hostUniRule annotation1

Keywords - PTMi

Disulfide bondUniRule annotationSAAS annotation, GlycoproteinUniRule annotation, Lipoprotein, PalmitateUniRule annotation, PhosphoproteinUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LY0NMR-A/B/C/D20-49[»]
ProteinModelPortaliQ6XT21.
SMRiQ6XT21.
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 annotationSAAS annotation

Keywords - Domaini

Signal-anchorUniRule annotation, Transmembrane, Transmembrane helixUniRule annotationSAAS annotation

Family and domain databases

HAMAPiMF_04069. INFV_M2. 1 hit.
InterProiView protein in InterPro
IPR002089. Flu_M2.
PfamiView protein in Pfam
PF00599. Flu_M2. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001031. Flu_M2. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiQ6XT21_9INFA
AccessioniPrimary (citable) accession number: Q6XT21
Entry historyiIntegrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: March 28, 2018
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources