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Matrix protein 2 (Proton channel protein M2)

 B6GV14_9INFA            Unreviewed;        97 AA.
B6GV14;
16-DEC-2008, integrated into UniProtKB/TrEMBL.
16-DEC-2008, sequence version 1.
31-JAN-2018, entry version 43.
RecName: Full=Matrix protein 2 {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00395487};
AltName: Full=Proton channel protein M2 {ECO:0000256|HAMAP-Rule:MF_04069};
Name=M2 {ECO:0000313|EMBL:CAJ43178.1};
Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04069};
Influenza A virus (A/teal/France/2546/2001(H1N3)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=298322 {ECO:0000313|EMBL:CAJ43178.1};
[1] {ECO:0000313|EMBL:CAJ43178.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/teal/France/2546/2001 {ECO:0000313|EMBL:CAJ43178.1};
Rousset J., Le Gall-Recule G., Ogor K., Bureau E., Hars J., Jestin V.;
"Characterisation of avian influenza viruses isolated from wild birds
and sentinel ducks during winter seasons 2000-2001, 2001-2002 and
2003-2004 in France.";
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
-!- 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:SAAS00108524}.
-!- SUBCELLULAR LOCATION: Host apical cell membrane
{ECO:0000256|SAAS:SAAS00581620}; Single-pass type III membrane
protein {ECO:0000256|SAAS:SAAS00581620}.
-!- 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:SAAS00581646}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04069}.
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EMBL; AM157381; CAJ43178.1; -; Genomic_RNA.
SMR; B6GV14; -.
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:0015078; F:hydrogen ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
GO; GO:0005216; F:ion channel 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 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;
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS00108279};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108156};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108156};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS00108142};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108569};
Inhibition of host autophagy by virus {ECO:0000256|HAMAP-
Rule:MF_04069, ECO:0000256|SAAS:SAAS00108142};
Ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS00108471};
Ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108471,
ECO:0000256|SAAS:SAAS00108569};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
Membrane {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108156,
ECO:0000256|SAAS:SAAS00108211, 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:SAAS00108211,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108211,
ECO:0000256|SAM:Phobius};
Transport {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108471,
ECO:0000256|SAAS:SAAS00108569};
Viral ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|SAAS:SAAS00108471};
Virion {ECO:0000256|HAMAP-Rule:MF_04069,
ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108457}.
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; 11158 MW; FF12EFFCB4370398 CRC64;
MSLLTEVETP TRNGWECKCS DSSDPLVIAA SIIGILHLIL WILDRLFFKC IYRRLKYGLK
RGPSTEGVPE SMREEYRQEQ QSAVDVDDGH FVNIELE


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