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M1_I96A0
ID   M1_I96A0                Reviewed;         252 AA.
AC   Q9Q0L8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-SEP-2021, entry version 100.
DE   RecName: Full=Matrix protein 1 {ECO:0000255|HAMAP-Rule:MF_04068};
DE            Short=M1 {ECO:0000255|HAMAP-Rule:MF_04068};
GN   Name=M {ECO:0000255|HAMAP-Rule:MF_04068};
OS   Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX   NCBI_TaxID=93838;
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.
RX   PubMed=10484749; DOI=10.1006/viro.1999.9820;
RA   Xu X., Subbarao K., Cox N.J., Guo Y.;
RT   "Genetic characterization of the pathogenic influenza
RT   A/Goose/Guangdong/1/96 (H5N1) virus: similarity of its hemagglutinin gene
RT   to those of H5N1 viruses from the 1997 outbreaks in Hong Kong.";
RL   Virology 261:15-19(1999).
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       {ECO:0000255|HAMAP-Rule:MF_04068}.
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. {ECO:0000255|HAMAP-Rule:MF_04068}.
CC   -!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP. Binds
CC       ribonucleocapsid by both interacting with genomic RNA and NP protein.
CC       May interact with HA and NA. Cannot bind NP without genomic RNA.
CC       {ECO:0000255|HAMAP-Rule:MF_04068}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04068}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04068}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04068}.
CC       Host nucleus {ECO:0000255|HAMAP-Rule:MF_04068}.
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=Q9Q0L8-1; Sequence=Displayed;
CC       Name=M2;
CC         IsoId=Q9Q0L9-1; Sequence=External;
CC   -!- MISCELLANEOUS: Most abundant protein in virion. When expressed alone
CC       can form virus-like particles in transfected cells. {ECO:0000255|HAMAP-
CC       Rule:MF_04068}.
CC   -!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_04068}.
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DR   EMBL; AF144306; AAD51928.1; -; Genomic_RNA.
DR   RefSeq; YP_308671.1; NC_007363.1. [Q9Q0L8-1]
DR   SMR; Q9Q0L8; -.
DR   GeneID; 8656647; -.
DR   KEGG; vg:8656647; -.
DR   Proteomes; UP000131152; Genome.
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-UniRule.
DR   GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-UniRule.
DR   GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.180; -; 1.
DR   Gene3D; 1.20.91.10; -; 1.
DR   HAMAP; MF_04068; INFV_M1; 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   InterPro; IPR037533; INFV_M1.
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; Reference proteome;
KW   RNA-binding; Viral matrix protein; Virion.
FT   CHAIN           1..252
FT                   /note="Matrix protein 1"
FT                   /id="PRO_0000078856"
FT   REGION          1..164
FT                   /note="Membrane-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04068"
FT   REGION          165..252
FT                   /note="RNP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04068"
FT   MOTIF           101..105
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04068"
SQ   SEQUENCE   252 AA;  27853 MW;  2A482C994E664043 CRC64;
     MSLLTEVETY VLSIVPSGPL KAEIAQRLED VFAGKNTDLE ALMEWLKTRP ILSPLTKGIL
     GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDRAVKLY KKLKREITFH GAKEVALSYS
     TGALASCMGL IYNRMGTVTT EVAFGLVCAT CEQIADSQHR SHRQMATTTN PLIRHENRMV
     LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRTIG THPSSSAGLK DNLLENLQAY
     QKRMGVQMQR FK
 
 
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