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Matrix protein 2 (Fragment)

 B0LX17_9INFA            Unreviewed;        95 AA.
B0LX17;
18-MAR-2008, integrated into UniProtKB/TrEMBL.
18-MAR-2008, sequence version 1.
10-OCT-2018, entry version 49.
RecName: Full=Matrix protein 2 {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040803};
Flags: Fragment;
Name=M2 {ECO:0000313|EMBL:ABY86175.1};
Influenza A virus (A/Hong Kong/CUHK7546/2005(H3N2)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=499510 {ECO:0000313|EMBL:ABY86175.1};
[1] {ECO:0000313|EMBL:ABY86175.1}
NUCLEOTIDE SEQUENCE.
STRAIN=A/Hong Kong/CUHK7546/2005 {ECO:0000313|EMBL:ABY86175.1};
PubMed=18360910; DOI=10.1002/jmv.21155;
Tang J.W., Ngai K.L., Wong J.C., Lam W.Y., Chan P.K.;
"Emergence of adamantane-resistant influenza A(H3N2) viruses in Hong
Kong between 1997 and 2006.";
J. Med. Virol. 80:895-901(2008).
-!- ACTIVITY 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,
ECO:0000256|SAAS:SAAS01073786}.
-!- 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: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|RuleBase:RU361247}.
-!- SIMILARITY: Belongs to the influenza viruses matrix protein M2
family. {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040773}.
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EMBL; EU384534; ABY86175.1; -; Viral_cRNA.
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:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex 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.
3: Inferred from homology;
Disulfide bond {ECO:0000256|SAAS:SAAS01040795};
Host cell membrane {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040804};
Host membrane {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040804};
Host-virus interaction {ECO:0000256|SAAS:SAAS01040755};
Hydrogen ion transport {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040774};
Inhibition of host autophagy by virus {ECO:0000256|SAAS:SAAS01040755};
Ion channel {ECO:0000256|SAAS:SAAS01040754};
Ion transport {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040754, ECO:0000256|SAAS:SAAS01040774};
Membrane {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040757, ECO:0000256|SAAS:SAAS01040804,
ECO:0000256|SAM:Phobius};
Signal-anchor {ECO:0000256|RuleBase:RU361247};
Transmembrane {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040757, ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040757, ECO:0000256|SAM:Phobius};
Transport {ECO:0000256|RuleBase:RU361247,
ECO:0000256|SAAS:SAAS01040754, ECO:0000256|SAAS:SAAS01040774};
Viral ion channel {ECO:0000256|SAAS:SAAS01040754};
Virion {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040766}.
TRANSMEM 28 48 Helical. {ECO:0000256|SAM:Phobius}.
NON_TER 95 95 {ECO:0000313|EMBL:ABY86175.1}.
SEQUENCE 95 AA; 10876 MW; B1B603C86C64C3C5 CRC64;
MSLLTEVETP IRNEWGCRCN DSSDPLVVAA NIIGILHLIL WILDRLFFKC VYRLFKHGLK
RGPSTGGVPE SMREEYRKEQ QNAVDADDSH FVSIE


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