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Matrix protein 1 (M1)

 M1_I33A0                Reviewed;         252 AA.
P05777;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
22-NOV-2017, entry version 105.
RecName: Full=Matrix protein 1 {ECO:0000255|HAMAP-Rule:MF_04068};
Short=M1 {ECO:0000255|HAMAP-Rule:MF_04068};
Name=M {ECO:0000255|HAMAP-Rule:MF_04068};
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus
(strain A/WS/1933 H1N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=381518;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2701939; DOI=10.1093/nar/17.7.2870;
Zebedee S.L., Lamb R.A.;
"Nucleotide sequences of influenza A virus RNA segment 7: a comparison
of five isolates.";
Nucleic Acids Res. 17:2870-2870(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3414185; DOI=10.1016/0168-1702(88)90021-4;
Markushin S., Ghiasi H., Sokolov N., Shilov A., Sinitsin B., Brown D.,
Klimov A., Nayak D.;
"Nucleotide sequence of RNA segment 7 and the predicted amino sequence
of M1 and M2 proteins of FPV/Weybridge (H7N7) and WSN (H1N1) influenza
viruses.";
Virus Res. 10:263-272(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3354209; DOI=10.1016/0042-6822(88)90303-0;
Baylor N.W., Zhiping Y.L., Wagner R.R.;
"Transient expression and sequence of the matrix (M1) gene of WSN
influenza A virus in a vaccinia vector.";
Virology 163:618-621(1988).
[4]
MUTAGENESIS OF 101-ARG--ARG-105 AND CYS-148.
PubMed=10438836;
Ye Z., Liu T., Offringa D.P., McInnis J., Levandowski R.A.;
"Association of influenza virus matrix protein with
ribonucleoproteins.";
J. Virol. 73:7467-7473(1999).
[5]
INTERACTION WITH HA AND NA.
PubMed=10954572; DOI=10.1128/JVI.74.18.8709-8719.2000;
Ali A., Avalos R.T., Ponimaskin E., Nayak D.P.;
"Influenza virus assembly: effect of influenza virus glycoproteins on
the membrane association of M1 protein.";
J. Virol. 74:8709-8719(2000).
[6]
MUTAGENESIS OF CYS-148; CYS-151; ALA-155; HIS-159 AND HIS-162.
PubMed=14573816; DOI=10.1099/vir.0.19389-0;
Hui E.K., Ralston K., Judd A.K., Nayak D.P.;
"Conserved cysteine and histidine residues in the putative zinc finger
motif of the influenza A virus M1 protein are not critical for
influenza virus replication.";
J. Gen. Virol. 84:3105-3113(2003).
[7]
FUNCTION.
PubMed=12604801; DOI=10.1099/vir.0.18803-0;
Bourmakina S.V., Garcia-Sastre A.;
"Reverse genetics studies on the filamentous morphology of influenza A
virus.";
J. Gen. Virol. 84:517-527(2003).
[8]
MUTAGENESIS OF LYS-95; VAL-97; LYS-98; LEU-99; TYR-100; ARG-101;
LYS-102; LEU-103; LYS-104; ARG-105 AND GLU-106.
PubMed=12768027; DOI=10.1128/JVI.77.12.7078-7092.2003;
Hui E.K., Barman S., Yang T.Y., Nayak D.P.;
"Basic residues of the helix six domain of influenza virus M1 involved
in nuclear translocation of M1 can be replaced by PTAP and YPDL late
assembly domain motifs.";
J. Virol. 77:7078-7092(2003).
[9]
MUTAGENESIS OF VAL-41; LYS-95 AND THR-218.
PubMed=15033573; DOI=10.1016/j.virol.2003.12.009;
Elleman C.J., Barclay W.S.;
"The M1 matrix protein controls the filamentous phenotype of influenza
A virus.";
Virology 321:144-153(2004).
-!- FUNCTION: Plays critical roles in virus replication, from virus
entry and uncoating to assembly and budding of the virus particle.
M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit
viral transcription. Interaction of viral NEP with M1-RNP is
thought to promote nuclear export of the complex, which is
targeted to the virion assembly site at the apical plasma membrane
in polarized epithelial cells. Interactions with NA and HA may
bring M1, a non-raft-associated protein, into lipid rafts. Forms a
continuous shell on the inner side of the lipid bilayer in virion,
where it binds the RNP. During virus entry into cell, the M2 ion
channel acidifies the internal virion core, inducing M1
dissociation from the RNP. M1-free RNPs are transported to the
nucleus, where viral transcription and replication can take place.
{ECO:0000255|HAMAP-Rule:MF_04068, ECO:0000269|PubMed:12604801}.
-!- FUNCTION: Determines the virion's shape: spherical or filamentous.
Clinical isolates of influenza are characterized by the presence
of significant proportion of filamentous virions, whereas after
multiple passage on eggs or cell culture, virions have only
spherical morphology. Filamentous virions are thought to be
important to infect neighboring cells, and spherical virions more
suited to spread through aerosol between hosts organisms.
{ECO:0000255|HAMAP-Rule:MF_04068, ECO:0000269|PubMed:12604801}.
-!- SUBUNIT: Homodimer and homomultimer. Interacts with NEP. Binds
ribonucleocapsid by both interacting with genomic RNA and NP
protein. May interact with HA and NA. Cannot bind NP without
genomic RNA. {ECO:0000255|HAMAP-Rule:MF_04068,
ECO:0000269|PubMed:10954572}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04068}; Peripheral membrane protein {ECO:0000255|HAMAP-
Rule:MF_04068}; Cytoplasmic side {ECO:0000255|HAMAP-
Rule:MF_04068}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04068}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Only the first 9 residues are shared by the 2 isoforms.;
Name=M1;
IsoId=P05777-1; Sequence=Displayed;
Name=M2;
IsoId=P05780-1; Sequence=External;
-!- MISCELLANEOUS: Most abundant protein in virion. When expressed
alone can form virus-like particles in transfected cells.
{ECO:0000255|HAMAP-Rule:MF_04068}.
-!- SIMILARITY: Belongs to the influenza viruses Matrix protein M1
family. {ECO:0000255|HAMAP-Rule:MF_04068}.
-----------------------------------------------------------------------
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EMBL; X08088; CAA30882.1; -; Genomic_RNA.
EMBL; M23920; AAA43252.1; ALT_SEQ; Genomic_RNA.
EMBL; M19374; AAA43352.1; -; Genomic_RNA.
EMBL; L25818; AAA91325.1; -; Genomic_RNA.
PIR; A28608; MFIVWS.
PIR; S07429; S07429.
PDB; 4PUS; X-ray; 2.20 A; A/B=2-165.
PDB; 5V6G; X-ray; 2.00 A; A/B/C/D=2-165.
PDB; 5V7B; X-ray; 2.50 A; A/B=2-165.
PDB; 5V7S; X-ray; 2.50 A; A/B/C=2-165.
PDB; 5V8A; X-ray; 3.00 A; A=2-165.
PDBsum; 4PUS; -.
PDBsum; 5V6G; -.
PDBsum; 5V7B; -.
PDBsum; 5V7S; -.
PDBsum; 5V8A; -.
ProteinModelPortal; P05777; -.
SMR; P05777; -.
OrthoDB; VOG090000KZ; -.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
Gene3D; 1.10.10.180; -; 1.
HAMAP; MF_04068; INFV_M1; 1.
InterPro; IPR036039; Flu_matrix_M1.
InterPro; IPR013188; Flu_matrix_M1_C.
InterPro; IPR001561; Flu_matrix_M1_N.
InterPro; IPR015799; Flu_matrix_M1_N_sub2.
Pfam; PF00598; Flu_M1; 1.
Pfam; PF08289; Flu_M1_C; 1.
ProDom; PD596253; Flu_matrix_M1_C; 1.
ProDom; PD001061; Flu_matrix_M1_N; 1.
SMART; SM00759; Flu_M1_C; 1.
SUPFAM; SSF48145; SSF48145; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Host nucleus; Membrane;
RNA-binding; Viral matrix protein; Virion.
CHAIN 1 252 Matrix protein 1.
/FTId=PRO_0000078868.
REGION 1 164 Membrane-binding. {ECO:0000255|HAMAP-
Rule:MF_04068}.
REGION 165 252 RNP-binding. {ECO:0000255|HAMAP-
Rule:MF_04068}.
MOTIF 101 105 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04068}.
MUTAGEN 41 41 V->A: Induces short filamentous virions.
{ECO:0000269|PubMed:15033573}.
MUTAGEN 95 95 K->A,R: No effect.
{ECO:0000269|PubMed:12768027,
ECO:0000269|PubMed:15033573}.
MUTAGEN 97 97 V->A: No effect.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 98 98 K->A,R: No effect.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 99 99 L->A: No effect.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 100 103 YRKL->AAAA,PPPY: Can't be rescued by
reverse genetic.
MUTAGEN 100 103 YRKL->PTAP: No effect.
MUTAGEN 100 100 Y->A,F,S: No effect.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 101 105 RKLKR->SNLNS: 50% loss of RNA binding
activity. {ECO:0000269|PubMed:10438836}.
MUTAGEN 101 102 RK->PD: No effect.
MUTAGEN 101 101 R->A: Reduced growth and small-plaque
morphology. Virions have an elongated
filamentous morphology.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 101 101 R->K: No effect.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 102 102 K->A,R: No effect.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 103 103 L->A,I,V: No effect.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 104 104 K->A: Can't be rescued by reverse
genetic. {ECO:0000269|PubMed:12768027}.
MUTAGEN 104 104 K->R: No effect.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 105 105 R->A: Can't be rescued by reverse
genetic. {ECO:0000269|PubMed:12768027}.
MUTAGEN 105 105 R->K: Reduced growth and small-plaque
morphology.
{ECO:0000269|PubMed:12768027}.
MUTAGEN 106 106 E->A: Can't be rescued by reverse
genetic. {ECO:0000269|PubMed:12768027}.
MUTAGEN 148 148 C->A: No effect.
{ECO:0000269|PubMed:10438836,
ECO:0000269|PubMed:14573816}.
MUTAGEN 148 148 C->S: 31% loss of RNA binding activity.
{ECO:0000269|PubMed:10438836,
ECO:0000269|PubMed:14573816}.
MUTAGEN 151 151 C->A: No effect.
{ECO:0000269|PubMed:14573816}.
MUTAGEN 155 155 A->G: Complete loss of virus ability to
be rescued in a reverse genetic system.
{ECO:0000269|PubMed:14573816}.
MUTAGEN 159 159 H->A: No effect.
{ECO:0000269|PubMed:14573816}.
MUTAGEN 162 162 H->A: No effect.
{ECO:0000269|PubMed:14573816}.
MUTAGEN 218 218 T->A: No effect on virion morphology.
{ECO:0000269|PubMed:15033573}.
CONFLICT 117 117 L -> F (in Ref. 3; AAA43352).
CONFLICT 219 219 I -> V (in Ref. 3; AAA43352).
CONFLICT 231 231 D -> S (in Ref. 2; AAA43252).
HELIX 3 13 {ECO:0000244|PDB:5V6G}.
HELIX 19 33 {ECO:0000244|PDB:5V6G}.
HELIX 39 47 {ECO:0000244|PDB:5V6G}.
STRAND 50 52 {ECO:0000244|PDB:5V6G}.
HELIX 54 67 {ECO:0000244|PDB:5V6G}.
HELIX 78 83 {ECO:0000244|PDB:5V6G}.
HELIX 86 88 {ECO:0000244|PDB:5V6G}.
HELIX 90 103 {ECO:0000244|PDB:5V6G}.
HELIX 109 116 {ECO:0000244|PDB:5V6G}.
HELIX 121 132 {ECO:0000244|PDB:5V6G}.
HELIX 133 137 {ECO:0000244|PDB:4PUS}.
HELIX 140 157 {ECO:0000244|PDB:5V6G}.
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


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