ID B5SN27_9INFA Unreviewed; 96 AA. AC B5SN27; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 11-DEC-2019, entry version 55. DE RecName: Full=Matrix protein 2 {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199250}; DE Flags: Fragment; GN Name=M2 {ECO:0000313|EMBL:ACH85535.1}; OS Influenza A virus (A/turkey/England/N28/1973(H5N2)). OC Viruses; Riboviria; Negarnaviricota; Polyploviricotina; Insthoviricetes; OC Articulavirales; Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=511839 {ECO:0000313|EMBL:ACH85535.1}; RN [1] {ECO:0000313|EMBL:ACH85535.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/turkey/England/N28/1973 {ECO:0000313|EMBL:ACH85535.1}; RX PubMed=18774155; DOI=10.1016/j.virol.2008.07.038; RA Duan L., Bahl J., Smith G.J., Wang J., Vijaykrishna D., Zhang L.J., RA Zhang J.X., Li K.S., Fan X.H., Cheung C.L., Huang K., Poon L.L., RA Shortridge K.F., Webster R.G., Peiris J.S., Chen H., Guan Y.; RT "The development and genetic diversity of H5N1 influenza virus in China, RT 1996-2006."; RL Virology 380:243-254(2008). CC -!- FUNCTION: Forms a proton-selective ion channel that is necessary for CC the efficient release of the viral genome during virus entry. CC {ECO:0000256|RuleBase:RU361247}. CC -!- ACTIVITY REGULATION: The M2 protein from most influenza A strains is CC inhibited by amantadine and rimantadine, resulting in viral uncoating CC incapacity. Emergence of amantadine-resistant variants is usually CC rapid. {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199254}. CC -!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers held CC together by non-covalent interactions. May interact with matrix protein CC 1. {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199237}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199239}; Single- CC pass type III membrane protein {ECO:0000256|RuleBase:RU361247, CC ECO:0000256|SAAS:SAAS01199239}. Virion membrane CC {ECO:0000256|RuleBase:RU361247}. CC -!- DOMAIN: Cytoplasmic tail plays an important role in virion assembly and CC morphogenesis. {ECO:0000256|RuleBase:RU361247}. CC -!- SIMILARITY: Belongs to the influenza viruses matrix protein M2 family. CC {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199247}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CY030996; ACH85535.1; -; 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:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW. DR GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW. DR HAMAP; MF_04069; INFV_M2; 1. DR InterPro; IPR002089; Flu_M2. DR Pfam; PF00599; Flu_M2; 1. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|SAAS:SAAS01199248}; KW Host cell membrane {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01199252}; KW Host membrane {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01199230}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS01199249}; KW Hydrogen ion transport {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01199235}; KW Inhibition of host autophagy by virus {ECO:0000256|SAAS:SAAS01199229}; KW Ion channel {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199238}; KW Ion transport {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01199246}; KW Membrane {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199251, KW ECO:0000256|SAM:Phobius}; Signal-anchor {ECO:0000256|RuleBase:RU361247}; KW Transmembrane {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01199244, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01199233, ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199253}; KW Viral ion channel {ECO:0000256|SAAS:SAAS01199243}; KW Virion {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01199241}. FT TRANSMEM 25..47 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 60..82 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 66..82 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ACH85535.1" FT NON_TER 96 FT /evidence="ECO:0000313|EMBL:ACH85535.1" SQ SEQUENCE 96 AA; 11015 MW; 85D85665BDB61B98 CRC64; SLLTEVETPT RNGWECKCSD SSDPLVTAAS IIGILHLILW ILDRLFFKCI YRRLKYGLKR GPSTEGVPES MREEYRQEQQ SAVDVDDGHF VNIELE //