ID   M1_I02A7                Reviewed;         250 AA.
AC   Q6DPQ6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   29-SEP-2021, entry version 60.
DE   RecName: Full=Matrix protein 1;
DE            Short=M1;
DE   Flags: Fragment;
GN   Name=M;
OS   Influenza A virus (strain A/Teal/China/2978.1/2002 H5N1 genotype W).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=284215;
OH   NCBI_TaxID=8782; Aves.
OH   NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH   NCBI_TaxID=9694; Panthera tigris (Tiger).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15241415; DOI=10.1038/nature02746;
RA   Li K.S., Guan Y., Wang J., Smith G.J.D., Xu K.M., Duan L., Rahardjo A.P.,
RA   Puthavathana P., Buranathai C., Nguyen T.D., Estoepangestie A.T.S.,
RA   Chaisingh A., Auewarakul P., Long H.T., Hanh N.T.H., Webby R.J.,
RA   Poon L.L.M., Chen H., Shortridge K.F., Yuen K.Y., Webster R.G.,
RA   Peiris J.S.M.;
RT   "Genesis of a highly pathogenic and potentially pandemic H5N1 influenza
RT   virus in eastern Asia.";
RL   Nature 430:209-213(2004).
CC   -!- FUNCTION: Plays critical roles in virus replication, from virus entry
CC       and uncoating to assembly and budding of the virus particle. M1 binding
CC       to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral
CC       transcription. Interaction of viral NEP with M1-RNP is thought to
CC       promote nuclear export of the complex, which is targeted to the virion
CC       assembly site at the apical plasma membrane in polarized epithelial
CC       cells. Interactions with NA and HA may bring M1, a non-raft-associated
CC       protein, into lipid rafts. Forms a continuous shell on the inner side
CC       of the lipid bilayer in virion, where it binds the RNP. During virus
CC       entry into cell, the M2 ion channel acidifies the internal virion core,
CC       inducing M1 dissociation from the RNP. M1-free RNPs are transported to
CC       the nucleus, where viral transcription and replication can take place
CC       (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Determines the virion's shape: spherical or filamentous.
CC       Clinical isolates of influenza are characterized by the presence of
CC       significant proportion of filamentous virions, whereas after multiple
CC       passage on eggs or cell culture, virions have only spherical
CC       morphology. Filamentous virions are thought to be important to infect
CC       neighboring cells, and spherical virions more suited to spread through
CC       aerosol between hosts organisms (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP (By
CC       similarity). Binds ribonucleocapsid by both interacting with genomic
CC       RNA and NP protein. May interact with HA and NA (By similarity). Cannot
CC       bind NP without genomic RNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein.
CC       Host nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Only the first 9 residues are shared by the 2 isoforms.;
CC       Name=M1;
CC         IsoId=Q6DPQ6-1; Sequence=Displayed;
CC       Name=M2;
CC         IsoId=Q6DPQ7-1; Sequence=External;
CC   -!- MISCELLANEOUS: Most abundant protein in virion. When expressed alone
CC       can form virus-like particles in transfected cells.
CC   -!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family.
CC       {ECO:0000305}.
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DR   EMBL; AY651417; AAT70587.1; -; Genomic_RNA.
DR   SMR; Q6DPQ6; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.180; -; 1.
DR   Gene3D; 1.20.91.10; -; 1.
DR   InterPro; IPR036039; Flu_matrix_M1.
DR   InterPro; IPR013188; Flu_matrix_M1_C.
DR   InterPro; IPR001561; Flu_matrix_M1_N.
DR   InterPro; IPR015423; Flu_matrix_M1_N_sub1.
DR   InterPro; IPR015799; Flu_matrix_M1_N_sub2.
DR   Pfam; PF00598; Flu_M1; 1.
DR   Pfam; PF08289; Flu_M1_C; 1.
DR   SMART; SM00759; Flu_M1_C; 1.
DR   SUPFAM; SSF48145; SSF48145; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Host nucleus; Membrane; RNA-binding;
KW   Viral matrix protein; Virion.
FT   CHAIN           <1..250
FT                   /note="Matrix protein 1"
FT                   /id="PRO_0000311617"
FT   REGION          <1..162
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          163..250
FT                   /note="RNP-binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           99..103
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   250 AA;  27715 MW;  CEAA3E1D8FA724BD CRC64;
     LLTEVETYVL SIIPSGPLKA EIAQKLEDVF AGKNTDLEAL MEWLKTRPIL SPLTKGILGF
     VFTLTVPSER GLQRRRFVQN ALNGNGDPNN MDRAVKLYKK LKREITFHGA KEVALSYSTG
     ALASCMGLIY NRMGTVTTEV AFGLVCATCE QIADSQHRSH RQMATITNPL IRHENRMVLA
     STTAKAMEQM AGSSEQAAEA MEVANQARQM VQAMRTIGTH PNSSAGLRDN LLENLQAYQK
     RMGVQMQRFK