Mutation detail:
| Mutation site | D21G |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | M2 |
| Gene ID | 23308108 |
| Country | Brazil |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | clade 6 |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | FJ966085.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Matrix Protein 2 |
| Uniprot protein ID | C3W5X3 |
| Protein length | 97 amino acids |
| Protein description | The M2 protein channel consists of 97 residues: (1) an ectodomain (residues 1-24); (2) the pore-forming TM helix (residues 25-43); (3) an amphiphilic C-terminal helix (residues 47-60); and (4)a cytoplasmic tail (residues 61-97). The influenza A virus M2 protein, a tetrameric type III integral transmembrane (TM) protein, is known to play an essential role in viral replication by mediating the acidification and uncoating of endosomally entrapped virus. The tetrameric M2 in the viral membrane functions as pH-dependent proton channels to equilibrate pH across the viral membrane during entry and across the trans-Golgi membrane of infected cells during viral maturation. |
Literature information:
| Pubmed ID | 24114147 |
| Clinical information | No |
| Disease | - |
| Published year | 2014 |
| Journal | Archives of Virology |
| Title | Genomic analysis of pandemic and post-pandemic influenza A pH1N1 viruses isolated in Rio Grande do Sul, Brazil |
| Author | F H Sant'Anna,L G A Borges,P R V Fallavena,T S Gregianini,F Matias |
| Evidence | Table 5 |