ID Q77MD4_9INFA Unreviewed; 97 AA. AC Q77MD4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 20-DEC-2017, entry version 57. DE RecName: Full=Matrix protein 2 {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00395487}; DE AltName: Full=Proton channel protein M2 {ECO:0000256|HAMAP-Rule:MF_04069}; GN Name=M {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000313|EMBL:AAK49257.1}; OS Influenza A virus (A/Hong Kong/488/97(H5N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Influenzavirus A. OX NCBI_TaxID=155222 {ECO:0000313|EMBL:AAK49257.1}; RN [1] {ECO:0000313|EMBL:AAK49257.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/488/97 {ECO:0000313|EMBL:AAK49257.1}; RA Shaw M.W., Cooper L.A., Xu X., Thompson W.W., Krauss S.L., Guan Y., RA Zhou N.N., Klimov A., Cox N.J., Webster R.G., Lim W., Shortridge K.F., RA Subbarao K.; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAK49257.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Hong Kong/488/97 {ECO:0000313|EMBL:AAK49257.1}; RX PubMed=11748666; DOI=10.1002/jmv.2118; RA Shaw M., Cooper L., Xu X., Thompson W., Krauss S., Guan Y., Zhou N., RA Klimov A., Cox N., Webster R., Lim W., Shortridge K., Subbarao K.; RT "Molecular changes associated with the transmission of avian influenza RT a H5N1 and H9N2 viruses to humans."; RL J. Med. Virol. 66:107-114(2002). 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|HAMAP-Rule:MF_04069, CC ECO:0000256|RuleBase:RU361247, 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|HAMAP-Rule:MF_04069, CC ECO:0000256|RuleBase:RU361247}. CC -!- MISCELLANEOUS: When the channel is activated, one or more CC imidazole moities of His-37 probably become bi-protonated. CC {ECO:0000256|HAMAP-Rule:MF_04069}. CC -!- SIMILARITY: Belongs to the influenza viruses matrix protein M2 CC family. {ECO:0000256|HAMAP-Rule:MF_04069, CC ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00581646}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04069}. 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; AH010697; AAK49257.1; -; Viral_cRNA. DR EMBL; AF255377; AAK49257.1; JOINED; Genomic_RNA. DR ProteinModelPortal; Q77MD4; -. 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:InterPro. 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 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|HAMAP-Rule:MF_04069, KW ECO:0000256|SAAS:SAAS00108279}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108156}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108238}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|SAAS:SAAS00472422}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108569}; KW Inhibition of host autophagy by virus {ECO:0000256|HAMAP- KW Rule:MF_04069, ECO:0000256|SAAS:SAAS00108142}; KW Ion channel {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108550}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108149}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04069}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108449, KW ECO:0000256|SAM:Phobius}; KW Palmitate {ECO:0000256|HAMAP-Rule:MF_04069}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04069}; KW Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108343, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108211, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108321}; KW Viral ion channel {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|SAAS:SAAS00108471}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS00108457}. FT TOPO_DOM 1 22 Virion surface. {ECO:0000256|HAMAP-Rule: FT MF_04069}. FT TRANSMEM 26 48 Helical. {ECO:0000256|SAM:Phobius}. FT TOPO_DOM 44 97 Intravirion. {ECO:0000256|HAMAP-Rule: FT MF_04069}. FT SITE 37 37 Essential for channel activity, possibly FT by being protonated during channel FT activation, and by forming the channel FT gate and the selective filter. FT {ECO:0000256|HAMAP-Rule:MF_04069}. FT SITE 41 41 Seems to be involved in pH gating. FT {ECO:0000256|HAMAP-Rule:MF_04069}. FT LIPID 50 50 S-palmitoyl cysteine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04069}. FT DISULFID 17 17 Interchain (with Cys-17). FT {ECO:0000256|HAMAP-Rule:MF_04069}. FT DISULFID 19 19 Interchain (with Cys-19). FT {ECO:0000256|HAMAP-Rule:MF_04069}. SQ SEQUENCE 97 AA; 11203 MW; F4C22FD462FF0BF9 CRC64; MSLLTEVETL TRNGWGCRCS DSSDPLVVAA SIIGILHLIL WILDRLFFKC IYRRFKYGLK RGPPTEGVLE SMREEYRQEQ QNAVDVDDGH FVNIELE //