Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-392810-00062
Entry Name
UniProt Accession
Theoretical PI
5.1
Molecular Weight
11225.84
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
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
50
Canonical
LNRLFFKCIYRRLKY
[1]
S-Palmitoylation
Organism
Influenza A virus (strain A/Fowl plague virus/Rostock/8/1934 H7N1)
NCBI Taxa ID
392810
Reference
[1] Sugrue RJ, Belshe RB, Hay AJ. Palmitoylation of the influenza A virus M2protein. Virology. 1990 Nov;179(1):51-6.[PMID:2219738]
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.
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.
Modified residue: 82 82 Phosphoserine; by host.
Protein Length
97 AA.
Protein Sequence
(Canonical)
MSLLTEVETP TRNGWECRCN DSSDPLIIAA SIIGILHLIL WILNRLFFKC IYRRLKYGLK  60
RGPSTEGVPE SMREEYRQEQ QSAVDVDDGH FVNIELE                           97
FASTA
(Canonical)
>LipidDB-392810-00062|P03492
MSLLTEVETPTRNGWECRCNDSSDPLIIAASIIGILHLILWILNRLFFKCIYRRLKYGLK
RGPSTEGVPESMREEYRQEQQSAVDVDDGHFVNIELE
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