Database: UniProt
Entry: A0A0J1IM29_BACCI
Original site: A0A0J1IM29_BACCI 
hibited 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}.
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DR   EMBL; JX309207; AFP35084.1; -; Viral_cRNA.
DR   ProteinModelPortal; I7F0J1; -.
DR   SMR; I7F0J1; -.
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   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:SAAS0104077
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