ID   K7YXX1_9INFA            Unreviewed;        97 AA.
AC   K7YXX1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   28-FEB-2018, entry version 28.
DE   RecName: Full=Matrix protein 2 {ECO:0000256|HAMAP-Rule:MF_04069, ECO:0000256|SAAS:SAAS00395487};
DE   AltName: Full=Proton channel protein M2 {ECO:0000256|HAMAP-Rule:MF_04069};
GN   Name=M2 {ECO:0000313|EMBL:AFX88542.1};
GN   Synonyms=M {ECO:0000256|HAMAP-Rule:MF_04069};
OS   Influenza A virus (A/pintail/Alberta/352/1986(H6N2)).
OC   Viruses; ssRNA viruses; ssRNA negative-strand viruses;
OC   Orthomyxoviridae; Influenzavirus A.
OX   NCBI_TaxID=1261960 {ECO:0000313|EMBL:AFX88542.1};
RN   [1] {ECO:0000313|EMBL:AFX88542.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/pintail/Alberta/352/1986 {ECO:0000313|EMBL:AFX88542.1};
RA   Wentworth D.E., Dugan V., Halpin R., Lin X., Bera J., Ghedin E.,
RA   Fedorova N., Tsitrin T., Stockwell T., Amedeo P., Bishop B.,
RA   Edworthy P., Gupta N., Katzel D., Li K., Schobel S., Shrivastava S.,
RA   Thovarai V., Wang S., van Doorn R., Mai L.Q., Hang N.L., Phuong H.V.,
RA   Cuong V.D., Thanh L., Thach N.C., Quyen P.D., Bao Y., Sanders R.,
RA   Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT   "The NIAID Influenza Genome Sequencing Project.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFX88542.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/pintail/Alberta/352/1986 {ECO:0000313|EMBL:AFX88542.1};
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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|SAAS:SAAS00108524}.
CC   -!- SUBCELLULAR LOCATION: Host apical cell membrane
CC       {ECO:0000256|SAAS:SAAS00581620}; Single-pass type III membrane
CC       protein {ECO:0000256|SAAS:SAAS00581620}.
CC   -!- DOMAIN: Cytoplasmic tail plays an important role in virion
CC       assembly and morphogenesis. {ECO:0000256|HAMAP-Rule:MF_04069}.
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|SAAS:SAAS00581646}.
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; CY126385; AFX88542.1; -; 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:0015078; F:hydrogen ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005216; F:ion channel 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 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:SAAS00108279};
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108156};
KW   Host membrane {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108238};
KW   Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00472422};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108569};
KW   Inhibition of host autophagy by virus {ECO:0000256|HAMAP-
KW   Rule:MF_04069, ECO:0000256|SAAS:SAAS00108142};
KW   Ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108550};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108149};
KW   Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04069};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108449, 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   Transmembrane {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108343, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108211, ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108321};
KW   Viral ion channel {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108471};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04069,
KW   ECO:0000256|SAAS:SAAS00108457}.
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   MOD_RES      82     82       Phosphoserine; 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;  11210 MW;  AB3216314372F2B2 CRC64;
     MSLLTEVETP TRSGWECKCS DSSDPLIFAA SIIGILHLIL WILDRLFFKY IYRRLKYGLK
     RGPSTEGVPK SMREEYQQEQ QSAVDVDDGH FVNIELE
//