GENTAUR Molecular Products.

 B6GV28_9INFA            Unreviewed;        97 AA.
 B6GV28;
 16-DEC-2008, integrated into UniProtKB/TrEMBL.
 16-DEC-2008, sequence version 1.
 13-FEB-2019, entry version 51.
 RecName: Full=Matrix protein 2 {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040803};
 AltName: Full=Proton channel protein M2 {ECO:0000256|HAMAP-Rule:MF_04069};
 Name=M2 {ECO:0000313|EMBL:CAJ43192.1};
 Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04069};
 Influenza A virus (A/mallard/France/710/2002(H1N1)).
 Viruses; ssRNA viruses; ssRNA negative-strand viruses;
 Orthomyxoviridae; Alphainfluenzavirus.
 NCBI_TaxID=356355 {ECO:0000313|EMBL:CAJ43192.1};
 [1] {ECO:0000313|EMBL:CAJ43192.1}
 NUCLEOTIDE SEQUENCE.
 STRAIN=A/mallard/France/710/2002 {ECO:0000313|EMBL:CAJ43192.1};
 Rousset J., Le Gall-Recule G., Ogor K., Bureau E., Hars J., Jestin V.;
 "Characterisation of avian influenza viruses isolated from wild birds
 and sentinel ducks during winter seasons 2000-2001, 2001-2002 and
 2003-2004 in France.";
 Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
 -!- FUNCTION: Forms a proton-selective ion channel that is necessary
     for the efficient release of the viral genome during virus entry.
     After attaching to the cell surface, the virion enters the cell by
     endocytosis. Acidification of the endosome triggers M2 ion channel
     activity. The influx of protons into virion interior is believed
     to disrupt interactions between the viral ribonucleoprotein (RNP),
     matrix protein 1 (M1), and lipid bilayers, thereby freeing the
     viral genome from interaction with viral proteins and enabling RNA
     segments to migrate to the host cell nucleus, where influenza
     virus RNA transcription and replication occur. Also plays a role
     in viral proteins secretory pathway. Elevates the intravesicular
     pH of normally acidic compartments, such as trans-Golgi network,
     preventing newly formed hemagglutinin from premature switching to
     the fusion-active conformation. {ECO:0000256|HAMAP-Rule:MF_04069,
     ECO:0000256|SAAS:SAAS01040783}.
 -!- ACTIVITY REGULATION: The M2 protein from most influenza A strains
     is inhibited by amantadine and rimantadine, resulting in viral
     uncoating incapacity. Emergence of amantadine-resistant variants
     is usually rapid. {ECO:0000256|RuleBase:RU361247,
     ECO:0000256|SAAS:SAAS01073786}.
 -!- SUBUNIT: Homotetramer; composed of two disulfide-linked dimers
     held together by non-covalent interactions. May interact with
     matrix protein 1. {ECO:0000256|HAMAP-Rule:MF_04069,
     ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040791}.
 -!- SUBCELLULAR LOCATION: Host apical cell membrane
     {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|SAAS:SAAS01040793};
     Single-pass type III membrane protein {ECO:0000256|HAMAP-
     Rule:MF_04069, ECO:0000256|SAAS:SAAS01040793}. Virion membrane
     {ECO:0000256|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at
     the apical plasma membrane in infected polarized epithelial cells,
     in close proximity to budding and assembled virions. Minor
     component of virions (only 16-20 molecules/virion).
     {ECO:0000256|HAMAP-Rule:MF_04069}.
 -!- DOMAIN: Cytoplasmic tail plays an important role in virion
     assembly and morphogenesis. {ECO:0000256|HAMAP-Rule:MF_04069,
     ECO:0000256|RuleBase:RU361247}.
 -!- MISCELLANEOUS: When the channel is activated, one or more
     imidazole moities of His-37 probably become bi-protonated.
     {ECO:0000256|HAMAP-Rule:MF_04069}.
 -!- SIMILARITY: Belongs to the influenza viruses matrix protein M2
     family. {ECO:0000256|HAMAP-Rule:MF_04069,
     ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040773}.
 -!- CAUTION: Lacks conserved residue(s) required for the propagation
     of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04069}.
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 EMBL; AM157388; CAJ43192.1; -; Genomic_RNA.
 SMR; B6GV28; -.
 GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
 GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-UniRule.
 GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
 GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-UniRule.
 GO; GO:0015078; F:proton transmembrane transporter activity; IEA:UniProtKB-UniRule.
 GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-UniRule.
 GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-UniRule.
 GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-UniRule.
 HAMAP; MF_04069; INFV_M2; 1.
 InterPro; IPR002089; Flu_M2.
 Pfam; PF00599; Flu_M2; 1.
 ProDom; PD001031; Flu_M2; 1.
 3: Inferred from homology;
 Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|SAAS:SAAS01040795};
 Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040804};
 Host membrane {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040804};
 Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|SAAS:SAAS01040755};
 Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040774};
 Inhibition of host autophagy by virus {ECO:0000256|HAMAP-
 Rule:MF_04069, ECO:0000256|SAAS:SAAS01040755};
 Ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|SAAS:SAAS01040754};
 Ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040754,
 ECO:0000256|SAAS:SAAS01040774};
 Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
 Membrane {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
 ECO:0000256|SAAS:SAAS01040804, ECO:0000256|SAM:Phobius};
 Palmitate {ECO:0000256|HAMAP-Rule:MF_04069};
 Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
 Signal-anchor {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247};
 Transmembrane {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
 ECO:0000256|SAM:Phobius};
 Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040757,
 ECO:0000256|SAM:Phobius};
 Transport {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040754,
 ECO:0000256|SAAS:SAAS01040774};
 Viral ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|SAAS:SAAS01040754};
 Virion {ECO:0000256|HAMAP-Rule:MF_04069,
 ECO:0000256|RuleBase:RU361247, ECO:0000256|SAAS:SAAS01040766}.
 TOPO_DOM      1     22       Virion surface. {ECO:0000256|HAMAP-
                              Rule:MF_04069}.
 TRANSMEM     26     48       Helical. {ECO:0000256|SAM:Phobius}.
 TOPO_DOM     44     97       Intravirion. {ECO:0000256|HAMAP-
                              Rule:MF_04069}.
 SITE         37     37       Essential for channel activity, possibly
                              by being protonated during channel
                              activation, and by forming the channel
                              gate and the selective filter.
                              {ECO:0000256|HAMAP-Rule:MF_04069}.
 SITE         41     41       Seems to be involved in pH gating.
                              {ECO:0000256|HAMAP-Rule:MF_04069}.
 MOD_RES      64     64       Phosphoserine; by host.
                              {ECO:0000256|HAMAP-Rule:MF_04069}.
 MOD_RES      82     82       Phosphoserine; by host.
                              {ECO:0000256|HAMAP-Rule:MF_04069}.
 LIPID        50     50       S-palmitoyl cysteine; by host.
                              {ECO:0000256|HAMAP-Rule:MF_04069}.
 DISULFID     17     17       Interchain (with Cys-17).
                              {ECO:0000256|HAMAP-Rule:MF_04069}.
 DISULFID     19     19       Interchain (with Cys-19).
                              {ECO:0000256|HAMAP-Rule:MF_04069}.
 SEQUENCE   97 AA;  11158 MW;  FF12EFFCB4370398 CRC64;
 MSLLTEVETP TRNGWECKCS DSSDPLVIAA SIIGILHLIL WILDRLFFKC IYRRLKYGLK
 RGPSTEGVPE SMREEYRQEQ QSAVDVDDGH FVNIELE

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