M1_I34A1
ID M1_I34A1 Reviewed; 252 AA.
AC P03485; A4GXH8; Q20N36; Q77HF4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 155.
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/Puerto Rico/8/1934 H1N1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=211044;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6927841; DOI=10.1093/nar/8.9.1965;
RA Winter G., Fields S.;
RT "Cloning of influenza cDNA into M13: the sequence of the RNA segment
RT encoding the A/PR/8/34 matrix protein.";
RL Nucleic Acids Res. 8:1965-1974(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=A/Puerto Rico/8/34/Mount Sinai;
RX PubMed=11779399; DOI=10.1098/rstb.2001.0979;
RA Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
RA Garcia-Sastre A., Palese P.;
RT "Plasmid-only rescue of influenza A virus vaccine candidates.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
RX PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
RA de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
RA Osterhaus A.D.M.E., Fouchier R.A.M.;
RT "Efficient generation and growth of influenza virus A/PR/8/34 from eight
RT cDNA fragments.";
RL Virus Res. 103:155-161(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
RA Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
RA Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
RA Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT "The NIAID influenza genome sequencing project.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-106.
RX PubMed=7241645; DOI=10.1128/jvi.38.1.1-7.1981;
RA Hall R.M., Air G.M.;
RT "Variation in nucleotide sequences coding for the N-terminal regions of the
RT matrix and nonstructural proteins of influenza A viruses.";
RL J. Virol. 38:1-7(1981).
RN [6]
RP INTERACTION WITH NEP PROTEIN.
RX PubMed=8356796; DOI=10.1006/viro.1993.1473;
RA Yasuda J., Nakada S., Kato A., Toyoda T., Ishihama A.;
RT "Molecular assembly of influenza virus: association of the NS2 protein with
RT virion matrix.";
RL Virology 196:249-255(1993).
RN [7]
RP HOMOMULTIMERIZATION.
RX PubMed=9780049; DOI=10.1099/0022-1317-79-10-2435;
RA Zhao H., Ekstrom M., Garoff H.;
RT "The M1 and NP proteins of influenza A virus form homo- but not
RT heterooligomeric complexes when coexpressed in BHK-21 cells.";
RL J. Gen. Virol. 79:2435-2446(1998).
RN [8]
RP INTERACTION WITH MEMBRANE AND VIRAL RNP.
RX PubMed=11222100; DOI=10.1006/viro.2000.0804;
RA Baudin F., Petit I., Weissenhorn W., Ruigrok R.W.;
RT "In vitro dissection of the membrane and RNP binding activities of
RT influenza virus M1 protein.";
RL Virology 281:102-108(2001).
RN [9]
RP FUNCTION.
RX PubMed=11531417; DOI=10.1006/viro.2001.1067;
RA Huang X., Liu T., Muller J., Levandowski R.A., Ye Z.;
RT "Effect of influenza virus matrix protein and viral RNA on
RT ribonucleoprotein formation and nuclear export.";
RL Virology 287:405-416(2001).
RN [10]
RP REVIEW.
RX PubMed=15567494; DOI=10.1016/j.virusres.2004.08.012;
RA Nayak D.P., Hui E.K., Barman S.;
RT "Assembly and budding of influenza virus.";
RL Virus Res. 106:147-165(2004).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-66.
RX PubMed=1565634; DOI=10.1073/pnas.89.8.3429;
RA Garboczi D.N., Hung D.T., Wiley D.C.;
RT "HLA-A2-peptide complexes: refolding and crystallization of molecules
RT expressed in Escherichia coli and complexed with single antigenic
RT peptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3429-3433(1992).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-158.
RX PubMed=9164466; DOI=10.1038/nsb0397-239;
RA Sha B., Luo M.;
RT "Structure of a bifunctional membrane-RNA binding protein, influenza virus
RT matrix protein M1.";
RL Nat. Struct. Biol. 4:239-244(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-164.
RX PubMed=11162800; DOI=10.1006/viro.2000.0727;
RA Arzt S., Baudin F., Barge A., Timmins P., Burmeister W.P., Ruigrok R.W.;
RT "Combined results from solution studies on intact influenza virus M1
RT protein and from a new crystal form of its N-terminal domain show that M1
RT is an elongated monomer.";
RL Virology 279:439-446(2001).
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, ECO:0000269|PubMed:11531417}.
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 ECO:0000269|PubMed:11531417}.
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, ECO:0000269|PubMed:11222100,
CC ECO:0000269|PubMed:8356796}.
CC -!- INTERACTION:
CC P03485; P03466: NP; NbExp=2; IntAct=EBI-2547543, EBI-2547640;
CC P03485; P03508: NS; NbExp=3; IntAct=EBI-2547543, EBI-2547979;
CC P03485; P03433: PA; NbExp=2; IntAct=EBI-2547543, EBI-2547616;
CC P03485; P11142: HSPA8; Xeno; NbExp=4; IntAct=EBI-2547543, EBI-351896;
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=P03485-1; Sequence=Displayed;
CC Name=M2;
CC IsoId=P06821-1; 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; V01099; CAA24282.1; -; Genomic_RNA.
DR EMBL; AF389121; AAM75161.1; -; Genomic_RNA.
DR EMBL; EF467824; ABO21712.1; -; Viral_cRNA.
DR EMBL; CY009445; ABD77676.1; -; Genomic_RNA.
DR RefSeq; NP_040978.1; NC_002016.1. [P03485-1]
DR PDB; 1AA7; X-ray; 2.08 A; A/B=1-158.
DR PDB; 1EA3; X-ray; 2.30 A; A/B=1-164.
DR PDB; 1HHI; X-ray; 2.50 A; C/F=58-66.
DR PDB; 2VLL; X-ray; 1.60 A; C/F=58-66.
DR PDB; 2VLR; X-ray; 2.30 A; C/H=58-66.
DR PDB; 3VDX; X-ray; 3.00 A; A/B/C=3-164.
DR PDB; 4D9J; X-ray; 3.92 A; A/B/C/D/E/F/G/H/I/J/K/L=3-164.
DR PDB; 4IQ4; X-ray; 3.50 A; A/B/C/D/E/F=3-164.
DR PDB; 4ITV; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=3-164.
DR PDB; 4IVJ; X-ray; 7.35 A; A/B/C=3-164.
DR PDB; 4QES; X-ray; 4.19 A; A/B/C=3-164.
DR PDB; 4QF0; X-ray; 6.49 A; A/B/C/D/E/F=3-164.
DR PDB; 4QFF; X-ray; 7.81 A; A/B/C/D/E/F/G/H/I/J/K/L=3-164.
DR PDB; 5CQE; X-ray; 2.10 A; A/B=1-164.
DR PDB; 5E6I; X-ray; 4.00 A; E/K/O/T=58-66.
DR PDB; 5EUO; X-ray; 2.10 A; I/J=58-66.
DR PDB; 5ISZ; X-ray; 2.06 A; C=58-66.
DR PDB; 5JHD; X-ray; 2.46 A; C/H=58-66.
DR PDB; 5TEZ; X-ray; 1.70 A; C=58-66.
DR PDB; 6Z5L; EM; 3.80 A; A=1-252.
DR PDB; 7JM3; EM; 3.40 A; C=2-252.
DR PDBsum; 1AA7; -.
DR PDBsum; 1EA3; -.
DR PDBsum; 1HHI; -.
DR PDBsum; 2VLL; -.
DR PDBsum; 2VLR; -.
DR PDBsum; 3VDX; -.
DR PDBsum; 4D9J; -.
DR PDBsum; 4IQ4; -.
DR PDBsum; 4ITV; -.
DR PDBsum; 4IVJ; -.
DR PDBsum; 4QES; -.
DR PDBsum; 4QF0; -.
DR PDBsum; 4QFF; -.
DR PDBsum; 5CQE; -.
DR PDBsum; 5E6I; -.
DR PDBsum; 5EUO; -.
DR PDBsum; 5ISZ; -.
DR PDBsum; 5JHD; -.
DR PDBsum; 5TEZ; -.
DR PDBsum; 6Z5L; -.
DR PDBsum; 7JM3; -.
DR SMR; P03485; -.
DR IntAct; P03485; 50.
DR MINT; P03485; -.
DR GeneID; 956527; -.
DR KEGG; vg:956527; -.
DR Reactome; R-HSA-168255; Influenza Infection.
DR Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
DR Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
DR Reactome; R-HSA-168298; Release.
DR Reactome; R-HSA-168302; Budding.
DR Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
DR Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site.
DR Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR EvolutionaryTrace; P03485; -.
DR Proteomes; UP000009255; Genome.
DR Proteomes; UP000116373; Genome.
DR Proteomes; UP000170967; Genome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Host nucleus; Membrane;
KW Reference proteome; RNA-binding; Viral matrix protein; Virion.
FT CHAIN 1..252
FT /note="Matrix protein 1"
FT /id="PRO_0000078864"
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 CONFLICT 207..208
FT /note="SQ -> IR (in Ref. 4; ABD77676)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1AA7"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:1AA7"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:1AA7"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1AA7"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:1AA7"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:7JM3"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1AA7"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1AA7"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:1AA7"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:1AA7"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1AA7"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1EA3"
FT HELIX 140..157
FT /evidence="ECO:0007829|PDB:1AA7"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:7JM3"
FT HELIX 171..194
FT /evidence="ECO:0007829|PDB:7JM3"
FT HELIX 202..219
FT /evidence="ECO:0007829|PDB:7JM3"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:7JM3"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:7JM3"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:7JM3"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7JM3"
SQ SEQUENCE 252 AA; 27893 MW; 2A54EEC87C3D4638 CRC64;
MSLLTEVETY VLSIIPSGPL KAEIAQRLED VFAGKNTDLE VLMEWLKTRP ILSPLTKGIL
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDKAVKLY RKLKREITFH GAKEISLSYS
AGALASCMGL IYNRMGAVTT EVAFGLVCAT CEQIADSQHR SHRQMVTTTN PLIRHENRMV
LASTTAKAME QMAGSSEQAA EAMEVASQAR QMVQAMRTIG THPSSSAGLK NDLLENLQAY
QKRMGVQMQR FK
