ID B5SN27_9INFA Unreviewed; 96 AA. AC B5SN27; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 05-JUN-2019, entry version 52. DE RecName: Full=Matrix protein 2 {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040803}; 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; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; OC 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 RT China, 1996-2006."; RL Virology 380:243-254(2008). CC -!- FUNCTION: Forms a proton-selective ion channel that is necessary CC for 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 CC is 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 ECO:0000256|SAAS:SAAS01073786}. 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:SAAS01040791}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040793}; CC Single-pass type III membrane protein CC {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040793}. CC Virion membrane {ECO:0000256|RuleBase:RU361247}. 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:SAAS01040773}. 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. DR ProDom; PD001031; Flu_M2; 1. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|SAAS:SAAS01040795}; KW Host cell membrane {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040804}; KW Host membrane {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040762}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS01040805}; KW Hydrogen ion transport {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040774}; KW Inhibition of host autophagy by virus {ECO:0000256|SAAS:SAAS01040755}; KW Ion channel {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040776}; KW Ion transport {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040807}; KW Membrane {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040794, ECO:0000256|SAM:Phobius}; KW Signal-anchor {ECO:0000256|RuleBase:RU361247}; KW Transmembrane {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040784, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040757, ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU361247, KW ECO:0000256|SAAS:SAAS01040788}; KW Viral ion channel {ECO:0000256|SAAS:SAAS01040754}; KW Virion {ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040766}. FT TRANSMEM 25 47 Helical. {ECO:0000256|SAM:Phobius}. FT REGION 60 82 Disordered. {ECO:0000256|MobiDB-lite: FT B5SN27}. FT COMPBIAS 66 82 Polyampholyte. {ECO:0000256|MobiDB-lite: FT B5SN27}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACH85535.1}. FT NON_TER 96 96 {ECO:0000313|EMBL:ACH85535.1}. SQ SEQUENCE 96 AA; 11015 MW; 85D85665BDB61B98 CRC64; SLLTEVETPT RNGWECKCSD SSDPLVTAAS IIGILHLILW ILDRLFFKCI YRRLKYGLKR GPSTEGVPES MREEYRQEQQ SAVDVDDGHF VNIELE //