ID A0A2P0VFC5_9INFA Unreviewed; 97 AA. AC A0A2P0VFC5; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 20-JUN-2018, entry version 2. 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:ASW34431.1}; GN Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04069}; OS Influenza A virus (A/chicken/Jordan/70/2004(H9N2)). OC Viruses; ssRNA viruses; ssRNA negative-strand viruses; OC Orthomyxoviridae; Alphainfluenzavirus. OX NCBI_TaxID=2027238 {ECO:0000313|EMBL:ASW34431.1}; RN [1] {ECO:0000313|EMBL:ASW34431.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A/chicken/Jordan/70/2004 {ECO:0000313|EMBL:ASW34431.1}; RX PubMed=29524835; DOI=.1016/j.virol.2018.02.016; RA Chrzastek K., Lee D.H., Gharaibeh S., Zsak A., Kapczynski D.R.; RT "Characterization of H9N2 avian influenza viruses from the Middle East RT demonstrates heterogeneity at amino acid position 226 in the RT hemagglutinin and potential for transmission to mammals."; RL Virology 518:195-201(2018). 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: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; MF673314; ASW34431.1; -; Viral_cRNA. 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 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 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 MOD_RES 64 64 Phosphoserine; by host. 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; 11092 MW; 62A6D2FF6D732856 CRC64; MSLLTEVETL TRNAWGCRCS DSSDPLVVAA SIIGILHLIL WILDRLFFKC IYRRFKYGLK GGPSTEGVPE SMREEYRQEQ QNAVDVDDGH FVNIELE //