M1_I33A0
ID M1_I33A0 Reviewed; 252 AA.
AC P05777;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 126.
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/Wilson-Smith/1933 H1N1) (Influenza A virus
OS (strain A/WS/1933 H1N1)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=381518;
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=2701939; DOI=10.1093/nar/17.7.2870;
RA Zebedee S.L., Lamb R.A.;
RT "Nucleotide sequences of influenza A virus RNA segment 7: a comparison of
RT five isolates.";
RL Nucleic Acids Res. 17:2870-2870(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3414185; DOI=10.1016/0168-1702(88)90021-4;
RA Markushin S., Ghiasi H., Sokolov N., Shilov A., Sinitsin B., Brown D.,
RA Klimov A., Nayak D.;
RT "Nucleotide sequence of RNA segment 7 and the predicted amino sequence of
RT M1 and M2 proteins of FPV/Weybridge (H7N7) and WSN (H1N1) influenza
RT viruses.";
RL Virus Res. 10:263-272(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3354209; DOI=10.1016/0042-6822(88)90303-0;
RA Baylor N.W., Zhiping Y.L., Wagner R.R.;
RT "Transient expression and sequence of the matrix (M1) gene of WSN influenza
RT A virus in a vaccinia vector.";
RL Virology 163:618-621(1988).
RN [4]
RP MUTAGENESIS OF 101-ARG--ARG-105 AND CYS-148.
RX PubMed=10438836; DOI=10.1128/jvi.73.9.7467-7473.1999;
RA Ye Z., Liu T., Offringa D.P., McInnis J., Levandowski R.A.;
RT "Association of influenza virus matrix protein with ribonucleoproteins.";
RL J. Virol. 73:7467-7473(1999).
RN [5]
RP INTERACTION WITH HA AND NA.
RX PubMed=10954572; DOI=10.1128/jvi.74.18.8709-8719.2000;
RA Ali A., Avalos R.T., Ponimaskin E., Nayak D.P.;
RT "Influenza virus assembly: effect of influenza virus glycoproteins on the
RT membrane association of M1 protein.";
RL J. Virol. 74:8709-8719(2000).
RN [6]
RP MUTAGENESIS OF CYS-148; CYS-151; ALA-155; HIS-159 AND HIS-162.
RX PubMed=14573816; DOI=10.1099/vir.0.19389-0;
RA Hui E.K., Ralston K., Judd A.K., Nayak D.P.;
RT "Conserved cysteine and histidine residues in the putative zinc finger
RT motif of the influenza A virus M1 protein are not critical for influenza
RT virus replication.";
RL J. Gen. Virol. 84:3105-3113(2003).
RN [7]
RP FUNCTION.
RX PubMed=12604801; DOI=10.1099/vir.0.18803-0;
RA Bourmakina S.V., Garcia-Sastre A.;
RT "Reverse genetics studies on the filamentous morphology of influenza A
RT virus.";
RL J. Gen. Virol. 84:517-527(2003).
RN [8]
RP RETRACTED PAPER.
RX PubMed=12768027; DOI=10.1128/jvi.77.12.7078-7092.2003;
RA Hui E.K., Barman S., Yang T.Y., Nayak D.P.;
RT "Basic residues of the helix six domain of influenza virus M1 involved in
RT nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly
RT domain motifs.";
RL J. Virol. 77:7078-7092(2003).
RN [9]
RP RETRACTION NOTICE OF PUBMED:12768027.
RX PubMed=17005709; DOI=10.1128/jvi.01632-06;
RA Hui E.K., Barman S., Yang T.Y., Tang D.H., France B., Nayak D.P.;
RT "Retraction.";
RL J. Virol. 80:10289-10289(2006).
RN [10]
RP MUTAGENESIS OF VAL-41; LYS-95 AND THR-218.
RX PubMed=15033573; DOI=10.1016/j.virol.2003.12.009;
RA Elleman C.J., Barclay W.S.;
RT "The M1 matrix protein controls the filamentous phenotype of influenza A
RT virus.";
RL Virology 321:144-153(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 {ECO:0000255|HAMAP-Rule:MF_04068, ECO:0000269|PubMed:12604801}.
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:12604801}.
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:10954572}.
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=P05777-1; Sequence=Displayed;
CC Name=M2;
CC IsoId=P05780-1; 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 -!- CAUTION: An article reported mutagenesis experiments; however, this
CC paper was later retracted. {ECO:0000305|PubMed:17005709}.
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; X08088; CAA30882.1; -; Genomic_RNA.
DR EMBL; M23920; AAA43252.1; ALT_SEQ; Genomic_RNA.
DR EMBL; M19374; AAA43352.1; -; Genomic_RNA.
DR EMBL; L25818; AAA91325.1; -; Genomic_RNA.
DR PIR; A28608; MFIVWS.
DR PIR; S07429; S07429.
DR PDB; 4PUS; X-ray; 2.20 A; A/B=2-165.
DR PDB; 5V6G; X-ray; 2.00 A; A/B/C/D=2-165.
DR PDB; 5V7B; X-ray; 2.50 A; A/B=2-165.
DR PDB; 5V7S; X-ray; 2.50 A; A/B/C=2-165.
DR PDB; 5V8A; X-ray; 3.00 A; A=2-165.
DR PDB; 6I3H; X-ray; 1.90 A; A/B=1-158.
DR PDB; 6QZD; X-ray; 2.66 A; CCC/FFF=17-30.
DR PDBsum; 4PUS; -.
DR PDBsum; 5V6G; -.
DR PDBsum; 5V7B; -.
DR PDBsum; 5V7S; -.
DR PDBsum; 5V8A; -.
DR PDBsum; 6I3H; -.
DR PDBsum; 6QZD; -.
DR SMR; P05777; -.
DR Proteomes; UP000000834; 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 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_0000078868"
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 MUTAGEN 41
FT /note="V->A: Induces short filamentous virions."
FT /evidence="ECO:0000269|PubMed:15033573"
FT MUTAGEN 95
FT /note="K->A,R: No effect."
FT /evidence="ECO:0000269|PubMed:15033573"
FT MUTAGEN 100..103
FT /note="YRKL->AAAA,PPPY: Can't be rescued by reverse
FT genetic."
FT MUTAGEN 100..103
FT /note="YRKL->PTAP: No effect."
FT MUTAGEN 101..105
FT /note="RKLKR->SNLNS: 50% loss of RNA binding activity."
FT /evidence="ECO:0000269|PubMed:10438836"
FT MUTAGEN 101..102
FT /note="RK->PD: No effect."
FT MUTAGEN 148
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:10438836,
FT ECO:0000269|PubMed:14573816"
FT MUTAGEN 148
FT /note="C->S: 31% loss of RNA binding activity."
FT /evidence="ECO:0000269|PubMed:10438836,
FT ECO:0000269|PubMed:14573816"
FT MUTAGEN 151
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:14573816"
FT MUTAGEN 155
FT /note="A->G: Complete loss of virus ability to be rescued
FT in a reverse genetic system."
FT /evidence="ECO:0000269|PubMed:14573816"
FT MUTAGEN 159
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:14573816"
FT MUTAGEN 162
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:14573816"
FT MUTAGEN 218
FT /note="T->A: No effect on virion morphology."
FT /evidence="ECO:0000269|PubMed:15033573"
FT CONFLICT 117
FT /note="L -> F (in Ref. 3; AAA43352)"
FT CONFLICT 219
FT /note="I -> V (in Ref. 3; AAA43352)"
FT CONFLICT 231
FT /note="D -> S (in Ref. 2; AAA43252)"
FT HELIX 1..13
FT /evidence="ECO:0007829|PDB:6I3H"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:6I3H"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:6I3H"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5V6G"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:6I3H"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:6I3H"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5V6G"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:6I3H"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:6I3H"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:6I3H"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6I3H"
FT HELIX 140..157
FT /evidence="ECO:0007829|PDB:6I3H"
SQ SEQUENCE 252 AA; 27864 MW; 5F300F18D75BBAD3 CRC64;
MSLLTEVETY VLSIVPSGPL KAEIAQRLED VFAGKNTDLE VLMEWLKTRP ILSPLTKGIL
GFVFTLTVPS ERGLQRRRFV QNALNGNGDP NNMDKAVKLY RKLKREITFH GAKEIALSYS
AGALASCMGL IYNRMGAVTT EVAFGLVCAT CEQIADSQHR SHRQMVTTTN PLIRHENRMV
LASTTAKAME QMAGSSEQAA EAMDIASQAR QMVQAMRTIG THPSSSAGLK DDLLENLQAY
QKRMGVQMQR FK
