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Matrix protein 2 (Proton channel protein M2)

 M2_I33A0                Reviewed;          97 AA.
P05780; Q67182;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
07-JUN-2017, entry version 102.
RecName: Full=Matrix protein 2 {ECO:0000255|HAMAP-Rule:MF_04069};
AltName: Full=Proton channel protein M2 {ECO:0000255|HAMAP-Rule:MF_04069};
Name=M {ECO:0000255|HAMAP-Rule:MF_04069};
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus
(strain A/WS/1933 H1N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=381518;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A/WS/33, and A/WSN/33;
PubMed=2701939; DOI=10.1093/nar/17.7.2870;
Zebedee S.L., Lamb R.A.;
"Nucleotide sequences of influenza A virus RNA segment 7: a comparison
of five isolates.";
Nucleic Acids Res. 17:2870-2870(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A/WSN/33;
PubMed=3414185; DOI=10.1016/0168-1702(88)90021-4;
Markushin S., Ghiasi H., Sokolov N., Shilov A., Sinitsin B., Brown D.,
Klimov A., Nayak D.;
"Nucleotide sequence of RNA segment 7 and the predicted amino sequence
of M1 and M2 proteins of FPV/Weybridge (H7N7) and WSN (H1N1) influenza
viruses.";
Virus Res. 10:263-272(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA].
STRAIN=A/NWS/33, and A/WSN/33;
PubMed=7710364; DOI=10.1007/BF01309872;
Ward A.C.;
"Specific changes in the M1 protein during adaptation of influenza
virus to mouse.";
Arch. Virol. 140:383-389(1995).
[4]
TOPOLOGY.
PubMed=3882238; DOI=10.1016/0092-8674(85)90211-9;
Lamb R.A., Zebedee S.L., Richardson C.D.;
"Influenza virus M2 protein is an integral membrane protein expressed
on the infected-cell surface.";
Cell 40:627-633(1985).
[5]
SUBCELLULAR LOCATION.
STRAIN=A/WSN/33;
PubMed=1501289;
Hughey P.G., Compans R.W., Zebedee S.L., Lamb R.A.;
"Expression of the influenza A virus M2 protein is restricted to
apical surfaces of polarized epithelial cells.";
J. Virol. 66:5542-5552(1992).
[6]
DOMAIN, AND MUTAGENESIS OF 74-GLU--LYS-76 AND 77-ARG--GLU-79.
PubMed=16699003; DOI=10.1128/JVI.00049-06;
Iwatsuki-Horimoto K., Horimoto T., Noda T., Kiso M., Maeda J.,
Watanabe S., Muramoto Y., Fujii K., Kawaoka Y.;
"The cytoplasmic tail of the influenza A virus M2 protein plays a role
in viral assembly.";
J. Virol. 80:5233-5240(2006).
[7]
INTERACTION WITH MATRIX PROTEIN 1.
PubMed=16873274; DOI=10.1128/JVI.00627-06;
McCown M.F., Pekosz A.;
"Distinct domains of the influenza a virus M2 protein cytoplasmic tail
mediate binding to the M1 protein and facilitate infectious virus
production.";
J. Virol. 80:8178-8189(2006).
[8]
REVIEW.
PubMed=12972146; DOI=10.1016/S0014-5793(03)00778-6;
Lear J.D.;
"Proton conduction through the M2 protein of the influenza A virus; a
quantitative, mechanistic analysis of experimental data.";
FEBS Lett. 552:17-22(2003).
[9]
REVIEW.
PubMed=12972147; DOI=10.1016/S0014-5793(03)00779-8;
Wu Y., Voth G.A.;
"Computational studies of proton transport through the M2 channel.";
FEBS Lett. 552:23-27(2003).
[10]
REVIEW.
PubMed=15567494; DOI=10.1016/j.virusres.2004.08.012;
Nayak D.P., Hui E.K., Barman S.;
"Assembly and budding of influenza virus.";
Virus Res. 106:147-165(2004).
-!- FUNCTION: 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. {ECO:0000255|HAMAP-Rule:MF_04069}.
-!- ENZYME REGULATION: The M2 protein from most influenza A strains is
inhibited by amantadine and rimantadine, resulting in viral
uncoating incapacity. Emergence of amantadine-resistant variants
is usually rapid.
-!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers
held together by non-covalent interactions. May interact with
matrix protein 1. {ECO:0000255|HAMAP-Rule:MF_04069}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04069, ECO:0000269|PubMed:1501289}. Host apical cell
membrane {ECO:0000255|HAMAP-Rule:MF_04069,
ECO:0000269|PubMed:1501289}; Single-pass type III membrane protein
{ECO:0000255|HAMAP-Rule:MF_04069, ECO:0000269|PubMed:1501289}.
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). {ECO:0000255|HAMAP-Rule:MF_04069}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Only the first 9 residues are shared by the 2 isoforms.;
Name=M2;
IsoId=P05780-1; Sequence=Displayed;
Name=M1;
IsoId=P05777-1; Sequence=External;
-!- DOMAIN: Cytoplasmic tail plays an important role in virion
assembly and morphogenesis. {ECO:0000255|HAMAP-Rule:MF_04069,
ECO:0000269|PubMed:16699003}.
-!- MISCELLANEOUS: When the channel is activated, one or more
imidazole moities of His-37 probably become bi-protonated.
{ECO:0000255|HAMAP-Rule:MF_04069}.
-!- SIMILARITY: Belongs to the influenza viruses matrix protein M2
family. {ECO:0000255|HAMAP-Rule:MF_04069}.
-----------------------------------------------------------------------
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EMBL; X08088; CAA30883.1; -; Genomic_RNA.
EMBL; X08089; CAA30885.1; -; Genomic_RNA.
EMBL; M23922; AAA43274.1; -; Genomic_RNA.
EMBL; L25814; AAA91322.1; -; mRNA.
EMBL; L25818; AAA91324.1; -; Genomic_RNA.
ProteinModelPortal; P05780; -.
SMR; P05780; -.
OrthoDB; VOG090001JK; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW.
HAMAP; MF_04069; INFV_M2; 1.
InterPro; IPR002089; Flu_M2.
Pfam; PF00599; Flu_M2; 1.
ProDom; PD001031; Flu_M2; 1.
1: Evidence at protein level;
Alternative splicing; Disulfide bond; Glycoprotein;
Host cell membrane; Host membrane; Host-virus interaction;
Hydrogen ion transport; Inhibition of host autophagy by virus;
Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Signal-anchor; Transmembrane; Transmembrane helix;
Transport; Viral ion channel; Virion.
CHAIN 1 97 Matrix protein 2.
/FTId=PRO_0000078894.
TOPO_DOM 1 22 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04069}.
TRANSMEM 23 43 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255|HAMAP-
Rule:MF_04069}.
TOPO_DOM 44 97 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04069}.
SITE 37 37 Essential for channel activity, possibly
by being protonated during channel
activation, and by forming the channel
gate and the selective filter.
{ECO:0000255|HAMAP-Rule:MF_04069}.
SITE 41 41 Seems to be involved in pH gating.
{ECO:0000255|HAMAP-Rule:MF_04069}.
MOD_RES 64 64 Phosphoserine; by host.
{ECO:0000255|HAMAP-Rule:MF_04069}.
LIPID 50 50 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04069}.
CARBOHYD 20 20 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04069}.
DISULFID 17 17 Interchain (with C-17).
{ECO:0000255|HAMAP-Rule:MF_04069}.
DISULFID 19 19 Interchain (with C-19).
{ECO:0000255|HAMAP-Rule:MF_04069}.
MUTAGEN 74 76 EEY->AAA: Loss of infectivity, and
modification of virion morphology.
{ECO:0000269|PubMed:16699003}.
MUTAGEN 77 79 RKE->AAA: Loss of infectivity, and
modification of virion morphology.
{ECO:0000269|PubMed:16699003}.
CONFLICT 34 34 G -> E (in Ref. 3; AAA91324).
CONFLICT 55 55 F -> L (in Ref. 2; AAA43274).
SEQUENCE 97 AA; 11313 MW; 1B5A86F9E0CD71DE CRC64;
MSLLTEVETP IRNEWGCRCN DSSDPLVIAA NIIGILHLIL WILDRLFFKC IYRRFKYGLK
RGPSTEGVPE SMREEYRKEQ QNAVDVDDGH FVNIELE


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