ID   B2VM22_9INFA            Unreviewed;        97 AA.
AC   B2VM22;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   06-JUL-2016, entry version 39.
DE   RecName: Full=Matrix protein 2 {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108407};
GN   Name=M2 {ECO:0000313|EMBL:ACD37512.1};
OS   Influenza A virus (A/Auckland/8/2007(H1N1)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=526895 {ECO:0000313|EMBL:ACD37512.1};
RN   [1] {ECO:0000313|EMBL:ACD37512.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/Auckland/8/2007 {ECO:0000313|EMBL:ACD37512.1};
RA   Barr I.G., Deng Y.M., Iannello P., Hurt A.C., Komadina N.;
RT   "Adamantane resistance in influenza A(H1) viruses increased in 2007 in
RT   South East Asia but decreased in Australia and other countries.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- ENZYME REGULATION: The M2 protein from most influenza A strains is
CC       inhibited by amantadine and rimantadine, resulting in viral
CC       uncoating incapacity. Emergence of amantadine-resistant variants
CC       is usually rapid. {ECO:0000256|RuleBase:RU361247}.
CC   -!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers
CC       held together by non-covalent interactions. May interact with
CC       matrix protein 1. {ECO:0000256|RuleBase:RU361247}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|SAAS:SAAS00581620}; Single-pass type III membrane
CC       protein {ECO:0000256|SAAS:SAAS00581620}.
CC   -!- DOMAIN: Cytoplasmic tail plays an important role in virion
CC       assembly and morphogenesis. {ECO:0000256|RuleBase:RU361247}.
CC   -!- SIMILARITY: Belongs to the influenza viruses matrix protein M2
CC       family. {ECO:0000256|RuleBase:RU361247,
CC       ECO:0000256|SAAS:SAAS00581646}.
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DR   EMBL; CY031389; ACD37512.1; -; Viral_cRNA.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW.
DR   InterPro; IPR002089; Flu_M2.
DR   Pfam; PF00599; Flu_M2; 1.
DR   ProDom; PD001031; Flu_M2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00472286};
KW   Host cell membrane {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472401};
KW   Host membrane {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472469};
KW   Host-virus interaction {ECO:0000256|SAAS:SAAS00472422};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472663};
KW   Inhibition of host autophagy by virus {ECO:0000256|SAAS:SAAS00472519};
KW   Ion channel {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472701};
KW   Ion transport {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472370};
KW   Membrane {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472180, ECO:0000256|SAM:Phobius};
KW   Signal-anchor {ECO:0000256|RuleBase:RU361247};
KW   Transmembrane {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472769, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472741, ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00472097};
KW   Virion {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00472621}.
FT   TRANSMEM     25     43       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   97 AA;  11058 MW;  6E71BB310D818DC1 CRC64;
     MSLLTEVETP IKNEWGCRCN DSSDPLVVAA NIIGIVHLIL WIIDRLFSKS IYRIFKHGLK
     RGPSTEGVPE SMREEYREEQ QNAVDADDGH FVSIELE
//