ID D5FAJ5_9INFA Unreviewed; 65 AA. AC D5FAJ5; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 19-FEB-2014, entry version 14. DE SubName: Full=Matrix protein 2; DE Flags: Fragment; GN Name=M2; OS Influenza A virus (A/Guangxi/1/2005(H5N1)). OC Viruses; ssRNA negative-strand viruses; Orthomyxoviridae; OC Influenzavirus A. OX NCBI_TaxID=370812; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Guangxi/1/2005; 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] RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Guangxi/1/2005; 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 (By similarity). CC -!- SUBCELLULAR LOCATION: Virion membrane. Host apical cell membrane; CC Single-pass type III membrane protein (By similarity). 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 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:0034220; P:ion transmembrane transport; IEA:GOC. 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; Host cell membrane; Host membrane; KW Hydrogen ion transport; Ion channel; Ion transport; Membrane; KW Phosphoprotein; Transmembrane; Transmembrane helix; Transport; Virion. FT NON_TER 1 1 FT NON_TER 65 65 SQ SEQUENCE 65 AA; 7537 MW; D1C2532EE3D8D6DF CRC64; PTRNEWECRC SDSSDPLVVA ASIIGILHLI LWILDRLFFK CIYRRLKYGL KRGPSTEGVP ESMRE //