ID   K7YXX1_9INFA            Unreviewed;        97 AA.
AC   K7YXX1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   03-APR-2013, entry version 3.
DE   SubName: Full=Matrix protein 2;
GN   Name=M2;
OS   Influenza A virus (A/pintail/Alberta/352/1986(H6N2)).
OC   Viruses; ssRNA negative-strand viruses; Orthomyxoviridae;
OC   Influenzavirus A.
OX   NCBI_TaxID=1261960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/pintail/Alberta/352/1986;
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]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/pintail/Alberta/352/1986;
RG   The NIAID Influenza Genome Sequencing Consortium;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms a proton-selective ion channel that is necessary
CC       for the efficient release of the viral genome during virus entry.
CC       After attaching to the cell surface, the virion enters the cell by
CC       endocytosis. Acidification of the endosome triggers M2 ion channel
CC       activity. The influx of protons into virion interior is believed
CC       to disrupt interactions between the viral ribonucleoprotein (RNP),
CC       matrix protein 1 (M1), and lipid bilayers, thereby freeing the
CC       viral genome from interaction with viral proteins and enabling RNA
CC       segments to migrate to the host cell nucleus, where influenza
CC       virus RNA transcription and replication occur. Also plays a role
CC       in viral proteins secretory pathway. Elevates the intravesicular
CC       pH of normally acidic compartments, such as trans-Golgi network,
CC       preventing newly formed hemagglutinin from premature switching to
CC       the fusion-active conformation (By similarity).
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DR   EMBL; CY126385; AFX88542.1; -; Viral_cRNA.
DR   GO; GO:0033644; C:host cell membrane; IEA:InterPro.
DR   GO; GO:0055036; C:virion membrane; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
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; Host cell membrane; Host membrane;
KW   Hydrogen ion transport; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport; Virion.
SQ   SEQUENCE   97 AA;  11210 MW;  AB3216314372F2B2 CRC64;
     MSLLTEVETP TRSGWECKCS DSSDPLIFAA SIIGILHLIL WILDRLFFKY IYRRLKYGLK
     RGPSTEGVPK SMREEYQQEQ QSAVDVDDGH FVNIELE
//