M1_I82A9
ID M1_I82A9 Reviewed; 252 AA.
AC Q8QV58; Q8QV56;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 29-SEP-2021, entry version 79.
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/Philippines/2/1982 H3N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=382825;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9721; Cetacea (whales).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate mouse-adapted, and Isolate wild-type;
RA Brown E.G., Liu H., Baird S., Chang Kit L., Nesrallah M.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate A/Philippines/2/82/BS;
RA Ward A.C.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
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=Q8QV58-1; Sequence=Displayed;
CC Name=M2;
CC IsoId=Q8QV59-1; 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}.
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; AF348912; AAM09296.1; -; Genomic_RNA.
DR EMBL; AF348913; AAM09298.1; -; Genomic_RNA.
DR EMBL; U08863; AAC79577.1; -; mRNA.
DR SMR; Q8QV58; -.
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 2: Evidence at transcript level;
KW Alternative splicing; Host nucleus; Membrane; RNA-binding;
KW Viral matrix protein; Virion.
FT CHAIN 1..252
FT /note="Matrix protein 1"
FT /id="PRO_0000223623"
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"
FT VARIANT 15
FT /note="V -> I (in strain: Isolate A/Philippines/2/82/BS)"
FT VARIANT 41
FT /note="A -> V (in strain: Isolate A/Philippines/2/82/BS and
FT Isolate mouse-adapted)"
FT VARIANT 43
FT /note="T -> M (in strain: Isolate A/Philippines/2/82/BS)"
FT VARIANT 95
FT /note="R -> K (in strain: Isolate A/Philippines/2/82/BS)"
FT VARIANT 116
FT /note="A -> S (in strain: Isolate A/Philippines/2/82/BS)"
FT VARIANT 144
FT /note="F -> L (in strain: Isolate mouse-adapted)"
FT VARIANT 167
FT /note="A -> T (in strain: Isolate A/Philippines/2/82/BS)"
FT VARIANT 218
FT /note="A -> T (in strain: Isolate A/Philippines/2/82/BS)"
FT VARIANT 231
FT /note="D -> N (in strain: Isolate A/Philippines/2/82/BS)"
FT VARIANT 239
FT /note="T -> A (in strain: Isolate A/Philippines/2/82/BS)"
SQ SEQUENCE 252 AA; 27804 MW; 13C990FA49267F08 CRC64;
MSLLTEVETY VLSIVPSGPL KAEIAQRLED VFAGKNTDLE ALTEWLKTRP ILSPLTKGIL
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDRAVKLY RKLKREITFH GAKEIALSYS
AGALASCMGL IYNRMGAVTT EVAFGLVCAT CEQIADSQHR SHRQMVATTN PLIRHENRMV
LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRAIG THPSSSAGLK DDLLENLQTY
QKRMGVQMQR FK