ID   Q0A3L8_9INFA            Unreviewed;        97 AA.
AC   Q0A3L8;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   05-JUL-2017, entry version 45.
DE   RecName: Full=Matrix protein 2 {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00395487};
GN   Name=M2 {ECO:0000313|EMBL:ABI84715.1};
OS   Influenza A virus (A/turkey/Minnesota/1012/1990(H13N2)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=402492 {ECO:0000313|EMBL:ABI84715.1};
RN   [1] {ECO:0000313|EMBL:ABI84715.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/turkey/Minnesota/1012/1990 {ECO:0000313|EMBL:ABI84715.1};
RX   PubMed=16439620; DOI=10.1126/science.1121586;
RA   Obenauer J.C., Denson J., Mehta P.K., Su X., Mukatira S.,
RA   Finkelstein D.B., Xu X., Wang J., Ma J., Fan Y., Rakestraw K.M.,
RA   Webster R.G., Hoffmann E., Krauss S., Zheng J., Zhang Z., Naeve C.W.;
RT   "Large-scale sequence analysis of avian influenza isolates.";
RL   Science 311:1576-1580(2006).
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       ECO:0000256|SAAS:SAAS00108524}.
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; CY014800; ABI84715.1; -; Other_RNA.
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:InterPro.
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:SAAS00108279};
KW   Host cell membrane {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108156};
KW   Host membrane {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108238};
KW   Host-virus interaction {ECO:0000256|SAAS:SAAS00472422};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108569};
KW   Inhibition of host autophagy by virus {ECO:0000256|SAAS:SAAS00108142};
KW   Ion channel {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108550};
KW   Ion transport {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108149};
KW   Membrane {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108449, ECO:0000256|SAM:Phobius};
KW   Signal-anchor {ECO:0000256|RuleBase:RU361247};
KW   Transmembrane {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108343, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108211, ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU361247,
KW   ECO:0000256|SAAS:SAAS00108321};
KW   Viral ion channel {ECO:0000256|SAAS:SAAS00108471};
KW   Virion {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108457}.
FT   TRANSMEM     26     48       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   97 AA;  11136 MW;  3F4093895ED46301 CRC64;
     MSLLTEVETH TRSGWECRCS DSSDPLVIAA SIIGILHLIL WILDRLFFKC IYRRFKYGLK
     SGPSTEGVPE SMREEYQQEK QSAVDVDDGH FVNIELE
//