ID D5FAJ5_9INFA Unreviewed; 65 AA. AC D5FAJ5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 30-AUG-2017, entry version 32. DE RecName: Full=Matrix protein 2 {ECO:0000256|SAAS:SAAS00395487}; DE Flags: Fragment; GN Name=M2 {ECO:0000313|EMBL:ADE48156.1}; OS Influenza A virus (A/Guangxi/1/2005(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=370812 {ECO:0000313|EMBL:ADE48156.1, ECO:0000313|Proteomes:UP000105802}; RN [1] {ECO:0000313|EMBL:ADE48156.1, ECO:0000313|Proteomes:UP000105802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/Guangxi/1/2005 {ECO:0000313|EMBL:ADE48156.1}; RX PubMed=20834097; DOI=10.3851/IMP1656; RA Lan Y., Zhang Y., Dong L., Wang D., Huang W., Xin L., Yang L., RA Zhao X., Li Z., Wang W., Li X., Xu C., Yang L., Guo J., Wang M., RA Peng Y., Gao Y., Guo Y., Wen L., Jiang T., Shu Y.; RT "A comprehensive surveillance of adamantane resistance among human RT influenza A virus isolated from mainland China between 1956 and RT 2009."; RL Antivir. Ther. 15:853-859(2010). RN [2] {ECO:0000313|EMBL:ADE48156.1, ECO:0000313|Proteomes:UP000105802} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A/Guangxi/1/2005 {ECO:0000313|EMBL:ADE48156.1}; RX PubMed=21976646; DOI=10.1128/JVI.05266-11; RA Wan X.F., Dong L., Lan Y., Long L.P., Xu C., Zou S., Li Z., Wen L., RA Cai Z., Wang W., Li X., Yuan F., Sui H., Zhang Y., Dong J., Sun S., RA Gao Y., Wang M., Bai T., Yang L., Li D., Yang W., Yu H., Wang S., RA Feng Z., Wang Y., Guo Y., Webby R.J., Shu Y.; RT "Indications that Live Poultry Markets Are a Major Source of Human RT H5N1 Influenza Virus Infection in China."; RL J. Virol. 85:13432-13438(2011). CC -!- FUNCTION: Forms a proton-selective ion channel that is necessary CC for the efficient release of the viral genome during virus entry. CC After attaching to the cell surface, the virion enters the cell by CC endocytosis. Acidification of the endosome triggers M2 ion channel CC activity. The influx of protons into virion interior is believed CC to disrupt interactions between the viral ribonucleoprotein (RNP), CC matrix protein 1 (M1), and lipid bilayers, thereby freeing the CC viral genome from interaction with viral proteins and enabling RNA CC segments to migrate to the host cell nucleus, where influenza CC virus RNA transcription and replication occur. Also plays a role CC in viral proteins secretory pathway. Elevates the intravesicular CC pH of normally acidic compartments, such as trans-Golgi network, CC preventing newly formed hemagglutinin from premature switching to CC the fusion-active conformation. {ECO:0000256|SAAS:SAAS00108379}. 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|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 -!- SUBCELLULAR LOCATION: Virion membrane CC {ECO:0000256|SAAS:SAAS00581584}. CC -!- SIMILARITY: Belongs to the influenza viruses matrix protein M2 CC family. {ECO:0000256|SAAS:SAAS00581646}. 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; CY060158; ADE48156.1; -; Viral_cRNA. DR Proteomes; UP000105802; Segment 7 sequence. 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:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW. DR GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW. 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 Complete proteome {ECO:0000313|Proteomes:UP000105802}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00108279}; KW Host cell membrane {ECO:0000256|SAAS:SAAS00108156}; KW Host membrane {ECO:0000256|SAAS:SAAS00108238}; KW Host-virus interaction {ECO:0000256|SAAS:SAAS00472422}; KW Hydrogen ion transport {ECO:0000256|SAAS:SAAS00108569}; KW Inhibition of host autophagy by virus {ECO:0000256|SAAS:SAAS00108142}; KW Ion channel {ECO:0000256|SAAS:SAAS00108550}; KW Ion transport {ECO:0000256|SAAS:SAAS00108149}; KW Membrane {ECO:0000256|SAAS:SAAS00108449, ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAAS:SAAS00108343, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00108211, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00108321}; KW Viral ion channel {ECO:0000256|SAAS:SAAS00108471}; KW Virion {ECO:0000256|SAAS:SAAS00108457}. FT TRANSMEM 17 39 Helical. {ECO:0000256|SAM:Phobius}. FT NON_TER 1 1 {ECO:0000313|EMBL:ADE48156.1}. FT NON_TER 65 65 {ECO:0000313|EMBL:ADE48156.1}. SQ SEQUENCE 65 AA; 7537 MW; D1C2532EE3D8D6DF CRC64; PTRNEWECRC SDSSDPLVVA ASIIGILHLI LWILDRLFFK CIYRRLKYGL KRGPSTEGVP ESMRE //