Reviewed
Aves [TaxID: 8782]; Homo Sapiens (Human) [TaxID: 9606]; Sus Scrofa (Pig) [TaxID: 9823]
M[Gene ID: 956528 ]
Matrix protein 2 (Proton channel protein M2)
Influenza A Virus (strain A/Puerto Rico/8/1934 H1N1)
Viruses> SsRNA Viruses> SsRNA Negative-strand Viruses> Orthomyxoviridae> Alphainfluenzavirus> Influenza A Virus> H1N1 Subtype> Influenza A Virus (strain A/Puerto Rico/8/1934 H1N1)
Not Available
Various pathway(s) in which protein is involved
MSLLTEVETPIRNEWGCRCNGSSDPLAIAANIIGILHLILWILDRLFFKCIYRRFKYGLKGGPSTEGVPKSMREEYRKEQQSAVDADDGHFVSIELE
97
Not Available
Not Available
01-11-1988
Evidence at protein level
| Amino Acid | Count | % Frequency | Amino Acid | Count | % Frequency |
|---|---|---|---|---|---|
| Alanine (A) | Leucine (L) | ||||
| Arginine (R) | Lysine (K) | ||||
| Asparagine (N) | Methionine (M) | ||||
| Aspartic Acid (D) | Phenylalanine (F) | ||||
| Cysteine (C) | Proline (P) | ||||
| Glutamine (Q) | Serine (S) | ||||
| Glutamic Acid (E) | Threonine (T) | ||||
| Glycine (G) | Tryptophan (W) | ||||
| Histidine (H) | Tyrosine (Y) | ||||
| Isoleucine (I) | Valine (V) |
| % Number of Residues in Helices | % Number of Residues in Strands | % Number of Residues in Coils |
|---|---|---|
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.
Not Available
GO:0000139 ; GO:0005215 ; GO:0005216 ; GO:0005576 ; GO:0005789 ;
GO:0005829 ; GO:0005886 ; GO:0015078 ; GO:0016021 ; GO:0019060 ;
GO:0019061 ; GO:0019062 ; GO:0019064 ; GO:0019065 ; GO:0019068 ;
GO:0019072 ; GO:0020002 ; GO:0030666 ; GO:0031904 ; GO:0039521 ;
GO:0039707 ; GO:0044385 ; GO:0046761 ; GO:0051259 ; GO:0055036
GO:0005829 ; GO:0005886 ; GO:0015078 ; GO:0016021 ; GO:0019060 ;
GO:0019061 ; GO:0019062 ; GO:0019064 ; GO:0019065 ; GO:0019068 ;
GO:0019072 ; GO:0020002 ; GO:0030666 ; GO:0031904 ; GO:0039521 ;
GO:0039707 ; GO:0044385 ; GO:0046761 ; GO:0051259 ; GO:0055036
♦ Virion membrane . Host apical cell membrane
♦ Single-pass type III membrane protein . Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). .
♦ Single-pass type III membrane protein . Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). .
Not Available
Not Available
X-ray crystallography (1)
Not Available
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.