| Tag |
Content |
LipidDB ID |
LipidDB-381518-01056 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
5.12 |
Molecular Weight |
11312.97 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Matrix protein 2 |
Protein Synonyms/Alias |
Proton channel protein M2; |
Gene Name |
M |
Gene Synonyms/Alias |
|
Created Date |
01-NOV-1988 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
50 | Canonical | LDRLFFKCIYRRFKY | [1] | S-Palmitoylation |
|
Organism |
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A viru (strain A/WS/1933 H1N1)) |
NCBI Taxa ID |
381518 |
Reference |
[1] Grantham ML, Wu WH, Lalime EN, Lorenzo ME, Klein SL, Pekosz A. Palmitoylation of the influenza A virus M2 protein is not required for virus replication invitro but contributes to virus virulence. J Virol. 2009 Sep;83(17):8655-61. doi: 10.1128/JVI.01129-09. Epub 2009 Jun 24.[ PMID:19553312]
|
Functional Description |
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 (By similarity). |
Sequence Annotation |
Topological domain: 1 22 Virion surface. Transmembrane: 23 43 Helical; Signal-anchor for type IIImembrane protein. Topological domain: 44 97 Intravirion. Functional site: 37 37 Essential for channel activity, seems tobe protonated during channel activation,and may play a role in the channel gatingand selectivity. Functional site: 41 41 Seems to be involved in pH gating. Modified residue: 64 64 Phosphoserine; by host.
|
Protein Length |
97 AA. |
Protein Sequence (Canonical) |
MSLLTEVETP IRNEWGCRCN DSSDPLVIAA NIIGILHLIL WILDRLFFKC IYRRFKYGLK 60
RGPSTEGVPE SMREEYRKEQ QNAVDVDDGH FVNIELE 97
|
FASTA (Canonical) |
>LipidDB-381518-01056|P05780
MSLLTEVETPIRNEWGCRCNDSSDPLVIAANIIGILHLILWILDRLFFKCIYRRFKYGLK
RGPSTEGVPESMREEYRKEQQNAVDVDDGHFVNIELE
|
Gene Ontology |
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW GO:0055036; C:virion membrane; IEA:InterPro GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro GO:0005216; F:ion channel activity; IEA:UniProtKB-KW GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW |
Interpro |
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Pfam |
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SMART |
|
PROSITE |
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PRINTS |
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