ID B2VM22_9INFA Unreviewed; 97 AA. AC B2VM22; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 12-SEP-2018, entry version 50. DE RecName: Full=Matrix protein 2 {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040803}; DE AltName: Full=Proton channel protein M2 {ECO:0000256|HAMAP-Rule:MF_04069}; GN Name=M2 {ECO:0000313|EMBL:ACD37512.1}; GN Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04069}; OS Influenza A virus (A/Auckland/8/2007(H1N1)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=526895 {ECO:0000313|EMBL:ACD37512.1}; RN [1] {ECO:0000313|EMBL:ACD37512.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/Auckland/8/2007 {ECO:0000313|EMBL:ACD37512.1}; RA Barr I.G., Deng Y.M., Iannello P., Hurt A.C., Komadina N.; RT "Adamantane resistance in influenza A(H1) viruses increased in 2007 in RT South East Asia but decreased in Australia and other countries."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. 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 -!- 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:SAAS01040791}. CC -!- SUBCELLULAR LOCATION: Host apical cell membrane CC {ECO:0000256|SAAS:SAAS01040793}; Single-pass type III membrane CC protein {ECO:0000256|SAAS:SAAS01040793}. 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:SAAS01040773}. 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; CY031389; ACD37512.1; -; 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-UniRule. DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-UniRule. DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:UniProtKB-UniRule. DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-UniRule. DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-UniRule. DR GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-UniRule. 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:SAAS01040795}; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04069}; KW Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040804}; KW Host membrane {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040762}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|SAAS:SAAS01040805}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040774}; KW Inhibition of host autophagy by virus {ECO:0000256|HAMAP- KW Rule:MF_04069, ECO:0000256|SAAS:SAAS01040755}; KW Ion channel {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040776}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040807}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04069}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040794, 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:SAAS01040784, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040788}; KW Viral ion channel {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|SAAS:SAAS01040754}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04069, KW ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040766}. FT TOPO_DOM 1 22 Virion surface. {ECO:0000256|HAMAP-Rule: FT MF_04069}. FT TRANSMEM 25 43 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 MOD_RES 64 64 Phosphoserine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04069}. FT MOD_RES 93 93 Phosphoserine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04069}. FT CARBOHYD 20 20 N-linked (GlcNAc...) asparagine; 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; 11058 MW; 6E71BB310D818DC1 CRC64; MSLLTEVETP IKNEWGCRCN DSSDPLVVAA NIIGIVHLIL WIIDRLFSKS IYRIFKHGLK RGPSTEGVPE SMREEYREEQ QNAVDADDGH FVSIELE //