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Matrix protein 2

 Q2PHN4_9INFA            Unreviewed;        97 AA.
Q2PHN4;
24-JAN-2006, integrated into UniProtKB/TrEMBL.
24-JAN-2006, sequence version 1.
30-AUG-2017, entry version 49.
RecName: Full=Matrix protein 2 {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00395487};
Name=M {ECO:0000313|EMBL:AAZ72692.1};
Influenza A virus (A/duck/Viet Nam/CM-V7/2004(H5N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=340003 {ECO:0000313|EMBL:AAZ72692.1};
[1] {ECO:0000313|EMBL:AAZ72692.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/duck/Viet Nam/CM-V7/2004 {ECO:0000313|EMBL:AAZ72692.1};
Cao V., Hai V.H., Duong L.H., Ngoc N.T., Vu N.P., Chinh N.C.,
Hiep N.T., Long N.T., Hoa D.M.;
"Genetic characterization of H5N1 influenza viruses from the outbreaks
2005 in Vietnam.";
Submitted (JUN-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|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|RuleBase:RU361247}.
-!- SIMILARITY: Belongs to the influenza viruses matrix protein M2
family. {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00581646}.
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EMBL; DQ094269; AAZ72692.1; -; Genomic_RNA.
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:InterPro.
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.
InterPro; IPR002089; Flu_M2.
Pfam; PF00599; Flu_M2; 1.
ProDom; PD001031; Flu_M2; 1.
3: Inferred from homology;
Disulfide bond {ECO:0000256|SAAS:SAAS00108279};
Host cell membrane {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00108156};
Host membrane {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00108156};
Host-virus interaction {ECO:0000256|SAAS:SAAS00108142};
Hydrogen ion transport {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00108569};
Inhibition of host autophagy by virus {ECO:0000256|SAAS:SAAS00108142};
Ion channel {ECO:0000256|SAAS:SAAS00108471};
Ion transport {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00108471, ECO:0000256|SAAS:SAAS00108569};
Membrane {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00108156, ECO:0000256|SAAS:SAAS00108211,
ECO:0000256|SAM:Phobius};
Signal-anchor {ECO:0000256|RuleBase:RU361247};
Transmembrane {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00108211, ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00108211, ECO:0000256|SAM:Phobius};
Transport {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS00108471, ECO:0000256|SAAS:SAAS00108569};
Viral ion channel {ECO:0000256|SAAS:SAAS00108471};
Virion {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108457}.
TRANSMEM 26 48 Helical. {ECO:0000256|SAM:Phobius}.
SEQUENCE 97 AA; 11197 MW; 89EE9C7087928351 CRC64;
MSLLTEVETP TRNEWECRCS DSSDPIVVAA NIIGILHLIL WILDRLFFKC IYRRLKYGLK
RGPATAGVPE SMREEYRQEQ QSAVDVDDGH FVNIELE


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