GENTAUR Molecular Products.

 B6GV28_9INFA            Unreviewed;        97 AA.
 B6GV28;
 16-DEC-2008, integrated into UniProtKB/TrEMBL.
 16-DEC-2008, sequence version 1.
 23-MAY-2018, entry version 47.
 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.
 -!- ENZYME 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}.
 -!- 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|SAAS:SAAS01040793}; Single-pass type III membrane
     protein {ECO:0000256|SAAS:SAAS01040793}.
 -!- 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}.
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution-NoDerivs License
 -----------------------------------------------------------------------
 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-UniRule.
 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

Related products :