Lipid Modification Database
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
InterPro; IPR002089; Flu_M2
Pfam
Pfam; PF00599; Flu_M2;
SMART
PROSITE
PRINTS