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Matrix protein 2 (Proton channel protein M2)

 Q20QB8_9INFA            Unreviewed;        97 AA.
Q20QB8;
18-APR-2006, integrated into UniProtKB/TrEMBL.
18-APR-2006, sequence version 1.
23-MAY-2018, entry version 54.
RecName: Full=Matrix protein 2 {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040803};
AltName: Full=Proton channel protein M2 {ECO:0000256|HAMAP-Rule:MF_04069};
Name=M2 {ECO:0000313|EMBL:ABB20143.1};
Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04069};
Influenza A virus (A/semi-palmated sandpiper/Brazil/43/1990(H2N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=352559 {ECO:0000313|EMBL:ABB20143.1, ECO:0000313|Proteomes:UP000137073};
[1] {ECO:0000313|EMBL:ABB20143.1, ECO:0000313|Proteomes:UP000137073}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=A/semi-palmated sandpiper/Brazil/43/1990
{ECO:0000313|EMBL:ABB20143.1};
PubMed=16439620; DOI=10.1126/science.1121586;
Obenauer J.C., Denson J., Mehta P.K., Su X., Mukatira S.,
Finkelstein D.B., Xu X., Wang J., Ma J., Fan Y., Rakestraw K.M.,
Webster R.G., Hoffmann E., Krauss S., Zheng J., Zhang Z., Naeve C.W.;
"Large-scale sequence analysis of avian influenza isolates.";
Science 311:1576-1580(2006).
-!- 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. {ECO:0000256|RuleBase:RU361247}.
-!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers
held together by non-covalent interactions. May interact with
matrix protein 1. {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040791}.
-!- SUBCELLULAR LOCATION: Host apical cell membrane
{ECO:0000256|SAAS:SAAS01040793}; Single-pass type III membrane
protein {ECO:0000256|SAAS:SAAS01040793}.
-!- DOMAIN: Cytoplasmic tail plays an important role in virion
assembly and morphogenesis. {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247}.
-!- MISCELLANEOUS: When the channel is activated, one or more
imidazole moities of His-37 probably become bi-protonated.
{ECO:0000256|HAMAP-Rule:MF_04069}.
-!- SIMILARITY: Belongs to the influenza viruses matrix protein M2
family. {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040773}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04069}.
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EMBL; CY005414; ABB20143.1; -; Other_RNA.
Proteomes; UP000137073; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-UniRule.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-UniRule.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-UniRule.
GO; GO:0015078; F:proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-UniRule.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-UniRule.
GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-UniRule.
HAMAP; MF_04069; INFV_M2; 1.
InterPro; IPR002089; Flu_M2.
Pfam; PF00599; Flu_M2; 1.
ProDom; PD001031; Flu_M2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000137073};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040795};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040804};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040804};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040755};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040774};
Inhibition of host autophagy by virus {ECO:0000256|HAMAP-
Rule:MF_04069, ECO:0000256|SAAS:SAAS01040755};
Ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040754};
Ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040754,
ECO:0000256|SAAS:SAAS01040774};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
Membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
ECO:0000256|SAAS:SAAS01040804, ECO:0000256|SAM:Phobius};
Palmitate {ECO:0000256|HAMAP-Rule:MF_04069};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
ECO:0000256|SAM:Phobius};
Transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040754,
ECO:0000256|SAAS:SAAS01040774};
Viral ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS01040754};
Virion {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040766}.
TOPO_DOM 1 22 Virion surface. {ECO:0000256|HAMAP-
Rule:MF_04069}.
TRANSMEM 26 48 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 44 97 Intravirion. {ECO:0000256|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:0000256|HAMAP-Rule:MF_04069}.
SITE 41 41 Seems to be involved in pH gating.
{ECO:0000256|HAMAP-Rule:MF_04069}.
MOD_RES 64 64 Phosphoserine; by host.
{ECO:0000256|HAMAP-Rule:MF_04069}.
MOD_RES 82 82 Phosphoserine; by host.
{ECO:0000256|HAMAP-Rule:MF_04069}.
LIPID 50 50 S-palmitoyl cysteine; by host.
{ECO:0000256|HAMAP-Rule:MF_04069}.
DISULFID 17 17 Interchain (with Cys-17).
{ECO:0000256|HAMAP-Rule:MF_04069}.
DISULFID 19 19 Interchain (with Cys-19).
{ECO:0000256|HAMAP-Rule:MF_04069}.
SEQUENCE 97 AA; 11230 MW; 8D30EFFF0161E02D CRC64;
MSLLTEVETP TRNEWECKCS DSSDPLVIAA SIIGILHLIL WILDRLFFKC IYRRLKYGLK
RGPSTEGVPE SMREEYRQEQ QSAVDVDDGH FVNIELE


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