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Matrix protein

 MATRX_HRSVA             Reviewed;         256 AA.
P0DOE7; P03419; Q77YB3;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
12-APR-2017, sequence version 1.
22-NOV-2017, entry version 8.
RecName: Full=Matrix protein;
Name=M;
Human respiratory syncytial virus A (strain A2).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Pneumoviridae; Orthopneumovirus.
NCBI_TaxID=11259;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6699948;
Satake M., Venkatesan S.;
"Nucleotide sequence of the gene encoding respiratory syncytial virus
matrix protein.";
J. Virol. 50:92-99(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7747420; DOI=10.1006/viro.1995.1178;
Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.;
"A cold-passaged, attenuated strain of human respiratory syncytial
virus contains mutations in the F and L genes.";
Virology 208:478-484(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=9035372; DOI=10.1007/BF00366988;
Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L.,
Murphy B.R.;
"Acquisition of the ts phenotype by a chemically mutagenized cold-
passaged human respiratory syncytial virus vaccine candidate results
from the acquisition of a single mutation in the polymerase (L)
gene.";
Virus Genes 13:269-273(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
PubMed=9557743;
Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.;
"Recombinant respiratory syncytial virus (RSV) bearing a set of
mutations from cold-passaged RSV is attenuated in chimpanzees.";
J. Virol. 72:4467-4471(1998).
[5]
FUNCTION, AND INTERACTION WITH N.
PubMed=11907323;
Ghildyal R., Mills J., Murray M., Vardaxis N., Meanger J.;
"Respiratory syncytial virus matrix protein associates with
nucleocapsids in infected cells.";
J. Gen. Virol. 83:753-757(2002).
[6]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH LIPID RAFTS.
PubMed=12350355; DOI=10.1006/viro.2002.1540;
Henderson G., Murray J., Yeo R.P.;
"Sorting of the respiratory syncytial virus matrix protein into
detergent-resistant structures is dependent on cell-surface expression
of the glycoproteins.";
Virology 300:244-254(2002).
[7]
INTERACTION WITH G.
PubMed=15958665; DOI=10.1099/vir.0.80829-0;
Ghildyal R., Li D., Peroulis I., Shields B., Bardin P.G., Teng M.N.,
Collins P.L., Meanger J., Mills J.;
"Interaction between the respiratory syncytial virus G glycoprotein
cytoplasmic domain and the matrix protein.";
J. Gen. Virol. 86:1879-1884(2005).
[8]
INTERACTION WITH HOST KPNB1.
PubMed=16171404; DOI=10.1021/bi050701e;
Ghildyal R., Ho A., Wagstaff K.M., Dias M.M., Barton C.L., Jans P.,
Bardin P.G., Jans D.A.;
"Nuclear import of the respiratory syncytial virus matrix protein is
mediated by importin beta1 independent of importin alpha.";
Biochemistry 44:12887-12895(2005).
[9]
INTERACTION WITH M2-1.
PubMed=18579594; DOI=10.1128/JVI.00343-08;
Li D., Jans D.A., Bardin P.G., Meanger J., Mills J., Ghildyal R.;
"Association of respiratory syncytial virus M protein with viral
nucleocapsids is mediated by the M2-1 protein.";
J. Virol. 82:8863-8870(2008).
-!- FUNCTION: Has a crucial role in virus assembly and budding. The
matrix interacts with the RNP complex and this association serves
two functions: facilitate virion assembly and inhibit the viral
transcriptase activity. Early in infection, M is localized to the
nucleus and may inhibit host cell transcription. Later on, M can
associate with lipid rafts supposely by interacting with the
cytoskeleton and with the cytoplasmic tail of glycoprotein G. The
binding of M to host membrane is stabilized by the surface
expression of the viral glycoproteins. These interactions may
allow virus formation by mediating association of the nucleocapsid
with the nascent envelop. {ECO:0000269|PubMed:11907323}.
-!- SUBUNIT: Interacts with glycoprotein G (via N-terminus), and
protein N. Interacts with protein M2-1; this interaction mediates
the association between proteins M and N. Interacts with host
KPNB1; this interaction mediates nuclear import of M early during
infection. {ECO:0000269|PubMed:11907323,
ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:16171404,
ECO:0000269|PubMed:18579594}.
-!- INTERACTION:
Q03135:CAV1 (xeno); NbExp=2; IntAct=EBI-10042882, EBI-603614;
P56539:CAV3 (xeno); NbExp=2; IntAct=EBI-10042882, EBI-3905936;
P23528:CFL1 (xeno); NbExp=2; IntAct=EBI-10042882, EBI-352733;
P04545:M2-1; NbExp=3; IntAct=EBI-10042882, EBI-10042927;
P06748:NPM1 (xeno); NbExp=3; IntAct=EBI-10042882, EBI-78579;
Q9NS69:TOMM22 (xeno); NbExp=2; IntAct=EBI-10042882, EBI-1047508;
Q8TBZ5:ZNF502 (xeno); NbExp=3; IntAct=EBI-10042882, EBI-10273699;
-!- SUBCELLULAR LOCATION: Virion. Host cytoplasm. Host nucleus
{ECO:0000269|PubMed:9557743}. Host cell membrane {ECO:0000305};
Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
{ECO:0000305}. Note=During bud formation, associates at the inner
side of the plasma membrane of infected cells. {ECO:0000305}.
-!- SIMILARITY: Belongs to the pneumovirinae M protein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M11486; AAB59854.1; -; Genomic_RNA.
EMBL; U50362; AAB86660.1; -; Genomic_RNA.
EMBL; U50363; AAB86672.1; -; Genomic_RNA.
EMBL; U63644; AAC55966.1; -; Genomic_RNA.
EMBL; AF035006; AAC14898.1; -; Genomic_RNA.
PIR; A04030; MFNZ.
PDB; 2VQP; X-ray; 1.60 A; A=1-256.
PDB; 2YKD; X-ray; 1.86 A; A=1-256.
PDB; 4D4T; X-ray; 1.90 A; A=1-256.
PDB; 4V23; X-ray; 1.70 A; A=1-256.
PDBsum; 2VQP; -.
PDBsum; 2YKD; -.
PDBsum; 4D4T; -.
PDBsum; 4V23; -.
SMR; P0DOE7; -.
IntAct; P0DOE7; 29.
Proteomes; UP000007678; Genome.
Proteomes; UP000134464; Genome.
Proteomes; UP000181145; Genome.
Proteomes; UP000181262; Genome.
Proteomes; UP000181559; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0019068; P:virion assembly; IEA:InterPro.
InterPro; IPR005056; Pneu_matrix.
Pfam; PF03393; Pneumo_matrix; 1.
ProDom; PD008590; Pneu_matrix; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Host cell membrane; Host cytoplasm;
Host membrane; Host nucleus; Host-virus interaction; Membrane;
Viral matrix protein; Virion.
CHAIN 1 256 Matrix protein.
/FTId=PRO_0000142748.
STRAND 2 7 {ECO:0000244|PDB:2VQP}.
STRAND 12 28 {ECO:0000244|PDB:2VQP}.
STRAND 31 35 {ECO:0000244|PDB:2VQP}.
STRAND 39 41 {ECO:0000244|PDB:2VQP}.
HELIX 45 52 {ECO:0000244|PDB:2VQP}.
STRAND 56 64 {ECO:0000244|PDB:2VQP}.
STRAND 67 75 {ECO:0000244|PDB:2VQP}.
HELIX 79 83 {ECO:0000244|PDB:2VQP}.
STRAND 86 91 {ECO:0000244|PDB:2VQP}.
HELIX 92 95 {ECO:0000244|PDB:2VQP}.
STRAND 108 120 {ECO:0000244|PDB:2VQP}.
HELIX 123 125 {ECO:0000244|PDB:2VQP}.
STRAND 126 128 {ECO:0000244|PDB:2VQP}.
HELIX 129 132 {ECO:0000244|PDB:2VQP}.
STRAND 140 151 {ECO:0000244|PDB:2VQP}.
TURN 152 154 {ECO:0000244|PDB:2VQP}.
STRAND 157 167 {ECO:0000244|PDB:2VQP}.
HELIX 171 174 {ECO:0000244|PDB:2VQP}.
TURN 178 180 {ECO:0000244|PDB:2VQP}.
HELIX 183 190 {ECO:0000244|PDB:2VQP}.
STRAND 193 205 {ECO:0000244|PDB:2VQP}.
HELIX 211 213 {ECO:0000244|PDB:2VQP}.
STRAND 221 225 {ECO:0000244|PDB:2VQP}.
HELIX 227 229 {ECO:0000244|PDB:2VQP}.
HELIX 235 241 {ECO:0000244|PDB:2VQP}.
STRAND 242 253 {ECO:0000244|PDB:2VQP}.
SEQUENCE 256 AA; 28714 MW; 1E70706D65416BA0 CRC64;
METYVNKLHE GSTYTAAVQY NVLEKDDDPA SLTIWVPMFQ SSMPADLLIK ELANVNILVK
QISTPKGPSL RVMINSRSAV LAQMPSKFTI CANVSLDERS KLAYDVTTPC EIKACSLTCL
KSKNMLTTVK DLTMKTLNPT HDIIALCEFE NIVTSKKVII PTYLRSISVR NKDLNTLENI
TTTEFKNAIT NAKIIPYSGL LLVITVTDNK GAFKYIKPQS QFIVDLGAYL EKESIYYVTT
NWKHTATRFA IKPMED


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