MATRX_HRSVA
ID MATRX_HRSVA Reviewed; 256 AA.
AC P0DOE7; P03419; Q77YB3;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Matrix protein;
DE AltName: Full=M protein {ECO:0000303|PubMed:18579594};
GN Name=M;
OS Human respiratory syncytial virus A (strain A2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11259;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6699948; DOI=10.1128/jvi.50.1.92-99.1984;
RA Satake M., Venkatesan S.;
RT "Nucleotide sequence of the gene encoding respiratory syncytial virus
RT matrix protein.";
RL J. Virol. 50:92-99(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7747420; DOI=10.1006/viro.1995.1178;
RA Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.;
RT "A cold-passaged, attenuated strain of human respiratory syncytial virus
RT contains mutations in the F and L genes.";
RL Virology 208:478-484(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9035372; DOI=10.1007/bf00366988;
RA Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R.;
RT "Acquisition of the ts phenotype by a chemically mutagenized cold-passaged
RT human respiratory syncytial virus vaccine candidate results from the
RT acquisition of a single mutation in the polymerase (L) gene.";
RL Virus Genes 13:269-273(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=9557743; DOI=10.1128/jvi.72.5.4467-4471.1998;
RA Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.;
RT "Recombinant respiratory syncytial virus (RSV) bearing a set of mutations
RT from cold-passaged RSV is attenuated in chimpanzees.";
RL J. Virol. 72:4467-4471(1998).
RN [5]
RP FUNCTION.
RX PubMed=11907323; DOI=10.1099/0022-1317-83-4-753;
RA Ghildyal R., Mills J., Murray M., Vardaxis N., Meanger J.;
RT "Respiratory syncytial virus matrix protein associates with nucleocapsids
RT in infected cells.";
RL J. Gen. Virol. 83:753-757(2002).
RN [6]
RP SUBCELLULAR LOCATION, ASSOCIATION WITH LIPID RAFTS, AND FUNCTION.
RX PubMed=12350355; DOI=10.1006/viro.2002.1540;
RA Henderson G., Murray J., Yeo R.P.;
RT "Sorting of the respiratory syncytial virus matrix protein into detergent-
RT resistant structures is dependent on cell-surface expression of the
RT glycoproteins.";
RL Virology 300:244-254(2002).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12827470; DOI=10.1007/s00705-003-0112-y;
RA Ghildyal R., Baulch-Brown C., Mills J., Meanger J.;
RT "The matrix protein of Human respiratory syncytial virus localises to the
RT nucleus of infected cells and inhibits transcription.";
RL Arch. Virol. 148:1419-1429(2003).
RN [8]
RP INTERACTION WITH G, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15958665; DOI=10.1099/vir.0.80829-0;
RA Ghildyal R., Li D., Peroulis I., Shields B., Bardin P.G., Teng M.N.,
RA Collins P.L., Meanger J., Mills J.;
RT "Interaction between the respiratory syncytial virus G glycoprotein
RT cytoplasmic domain and the matrix protein.";
RL J. Gen. Virol. 86:1879-1884(2005).
RN [9]
RP INTERACTION WITH HOST KPNB1, AND SUBCELLULAR LOCATION.
RX PubMed=16171404; DOI=10.1021/bi050701e;
RA Ghildyal R., Ho A., Wagstaff K.M., Dias M.M., Barton C.L., Jans P.,
RA Bardin P.G., Jans D.A.;
RT "Nuclear import of the respiratory syncytial virus matrix protein is
RT mediated by importin beta1 independent of importin alpha.";
RL Biochemistry 44:12887-12895(2005).
RN [10]
RP INTERACTION WITH M2-1, AND FUNCTION.
RX PubMed=18579594; DOI=10.1128/jvi.00343-08;
RA Li D., Jans D.A., Bardin P.G., Meanger J., Mills J., Ghildyal R.;
RT "Association of respiratory syncytial virus M protein with viral
RT nucleocapsids is mediated by the M2-1 protein.";
RL J. Virol. 82:8863-8870(2008).
RN [11]
RP FUNCTION, NUCLEAR EXPORT SIGNAL, AND SUBCELLULAR LOCATION.
RX PubMed=19297465; DOI=10.1128/jvi.02374-08;
RA Ghildyal R., Ho A., Dias M., Soegiyono L., Bardin P.G., Tran K.C.,
RA Teng M.N., Jans D.A.;
RT "The respiratory syncytial virus matrix protein possesses a Crm1-mediated
RT nuclear export mechanism.";
RL J. Virol. 83:5353-5362(2009).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23903836; DOI=10.1128/jvi.03086-12;
RA Baviskar P.S., Hotard A.L., Moore M.L., Oomens A.G.;
RT "The respiratory syncytial virus fusion protein targets to the perimeter of
RT inclusion bodies and facilitates filament formation by a cytoplasmic tail-
RT dependent mechanism.";
RL J. Virol. 87:10730-10741(2013).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF THR-205, AND
RP PHOSPHORYLATION AT THR-205.
RX PubMed=24672034; DOI=10.1128/jvi.03856-13;
RA Bajorek M., Caly L., Tran K.C., Maertens G.N., Tripp R.A., Bacharach E.,
RA Teng M.N., Ghildyal R., Jans D.A.;
RT "The Thr205 phosphorylation site within respiratory syncytial virus matrix
RT (M) protein modulates M oligomerization and virus production.";
RL J. Virol. 88:6380-6393(2014).
RN [14]
RP INTERACTION WITH HOST CAV1, INTERACTION WITH HOST CFL1, AND INTERACTION
RP WITH HOST ZNF502.
RX PubMed=25556234; DOI=10.1074/mcp.m114.044107;
RA Kipper S., Hamad S., Caly L., Avrahami D., Bacharach E., Jans D.A.,
RA Gerber D., Bajorek M.;
RT "New host factors important for respiratory syncytial virus (RSV)
RT replication revealed by a novel microfluidics screen for interactors of
RT matrix (M) protein.";
RL Mol. Cell. Proteomics 14:532-543(2015).
RN [15]
RP FUNCTION.
RX PubMed=27654298; DOI=10.1128/jvi.01193-16;
RA Meshram C.D., Baviskar P.S., Ognibene C.M., Oomens A.G.P.;
RT "The Respiratory Syncytial Virus Phosphoprotein, Matrix Protein, and Fusion
RT Protein Carboxy-Terminal Domain Drive Efficient Filamentous Virus-Like
RT Particle Formation.";
RL J. Virol. 90:10612-10628(2016).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH HOST AP3M1.
RX PubMed=29028839; DOI=10.1371/journal.pone.0184629;
RA Ward C., Maselko M., Lupfer C., Prescott M., Pastey M.K.;
RT "Interaction of the Human Respiratory Syncytial Virus matrix protein with
RT cellular adaptor protein complex 3 plays a critical role in trafficking.";
RL PLoS ONE 12:E0184629-E0184629(2017).
RN [17]
RP SUBUNIT.
RX PubMed=29510513; DOI=10.3390/v10030109;
RA Trevisan M., Di Antonio V., Radeghieri A., Palu G., Ghildyal R., Alvisi G.;
RT "Molecular Requirements for Self-Interaction of the Respiratory Syncytial
RT Virus Matrix Protein in Living Mammalian Cells.";
RL Viruses 10:0-0(2018).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-170 AND LYS-172.
RX PubMed=34685766; DOI=10.3390/cells10102786;
RA Li H.M., Ghildyal R., Hu M., Tran K.C., Starrs L.M., Mills J., Teng M.N.,
RA Jans D.A.;
RT "Respiratory Syncytial Virus Matrix Protein-Chromatin Association Is Key to
RT Transcriptional Inhibition in Infected Cells.";
RL Cells 10:0-0(2021).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), SUBUNIT, AND FUNCTION.
RX PubMed=25673702; DOI=10.1128/jvi.03500-14;
RA Foerster A., Maertens G.N., Farrell P.J., Bajorek M.;
RT "Dimerization of matrix protein is required for budding of respiratory
RT syncytial virus.";
RL J. Virol. 89:4624-4635(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RX PubMed=19251668; DOI=10.1073/pnas.0805740106;
RA Money V.A., McPhee H.K., Mosely J.A., Sanderson J.M., Yeo R.P.;
RT "Surface features of a Mononegavirales matrix protein indicate sites of
RT membrane interaction.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4441-4446(2009).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RX PubMed=21141948; DOI=10.1021/la104041n;
RA McPhee H.K., Carlisle J.L., Beeby A., Money V.A., Watson S.M., Yeo R.P.,
RA Sanderson J.M.;
RT "Influence of lipids on the interfacial disposition of respiratory
RT syncytical virus matrix protein.";
RL Langmuir 27:304-311(2011).
CC -!- FUNCTION: Plays a crucial role in virus assembly into filaments and
CC budding (PubMed:25673702, PubMed:27654298, PubMed:23903836,
CC PubMed:24672034). Early in infection, localizes in the nucleus where it
CC inhibits host cell transcription through direct binding to host
CC chromatin (PubMed:12827470, PubMed:34685766). Later in infection,
CC traffics to the cytoplasm through the action of host CRM1 to associate
CC with inclusion bodies, the site of viral transcription and replication
CC (PubMed:19297465, PubMed:23903836). During virus assembly and budding,
CC acts as a bridge between the nucleocapsid and the lipid bilayer
CC (PubMed:11907323, PubMed:12350355, PubMed:15958665, PubMed:18579594).
CC {ECO:0000269|PubMed:11907323, ECO:0000269|PubMed:12350355,
CC ECO:0000269|PubMed:12827470, ECO:0000269|PubMed:15958665,
CC ECO:0000269|PubMed:18579594, ECO:0000269|PubMed:19297465,
CC ECO:0000269|PubMed:23903836, ECO:0000269|PubMed:24672034,
CC ECO:0000269|PubMed:25673702, ECO:0000269|PubMed:27654298,
CC ECO:0000269|PubMed:34685766, ECO:0000269|PubMed:9035372}.
CC -!- SUBUNIT: Forms dimers (PubMed:29510513, PubMed:25673702). Forms higher-
CC order oligomers (PubMed:24672034). Interacts with glycoprotein G (via
CC N-terminus) (PubMed:15958665). Interacts with protein M2-1; this
CC interaction directs the matrix protein localization to cytoplasmic
CC inclusions comprising viral proteins L, N, P, and M2-1 and mediates the
CC matrix protein association with the nucleocapsid (PubMed:18579594).
CC Interacts with host importin KPNB1; this interaction mediates nuclear
CC import of the matrix protein early during infection (PubMed:16171404).
CC Interacts with host AP3M1; this interaction plays an essential role in
CC trafficking the matrix protein in host cells (PubMed:29028839).
CC Interacts with host CAV1; this interaction probably facilitates viral
CC budding (PubMed:25556234). Interacts with host CFL1; this interaction
CC probably facilitates viral replication (PubMed:25556234). Interacts
CC with host ZNF502; this interaction probably facilitates viral release
CC (PubMed:25556234). {ECO:0000269|PubMed:15958665,
CC ECO:0000269|PubMed:16171404, ECO:0000269|PubMed:18579594,
CC ECO:0000269|PubMed:24672034, ECO:0000269|PubMed:25556234,
CC ECO:0000269|PubMed:25673702, ECO:0000269|PubMed:29028839,
CC ECO:0000269|PubMed:29510513}.
CC -!- INTERACTION:
CC P0DOE7; P04545: M2-1; NbExp=3; IntAct=EBI-10042882, EBI-10042927;
CC P0DOE7; Q03135: CAV1; Xeno; NbExp=2; IntAct=EBI-10042882, EBI-603614;
CC P0DOE7; P56539: CAV3; Xeno; NbExp=2; IntAct=EBI-10042882, EBI-3905936;
CC P0DOE7; P23528: CFL1; Xeno; NbExp=2; IntAct=EBI-10042882, EBI-352733;
CC P0DOE7; P06748: NPM1; Xeno; NbExp=3; IntAct=EBI-10042882, EBI-78579;
CC P0DOE7; Q9NS69: TOMM22; Xeno; NbExp=2; IntAct=EBI-10042882, EBI-1047508;
CC P0DOE7; Q8TBZ5: ZNF502; Xeno; NbExp=3; IntAct=EBI-10042882, EBI-10273699;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24672034}. Host
CC cytoplasm {ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:19297465,
CC ECO:0000269|PubMed:24672034, ECO:0000269|PubMed:29028839}. Host nucleus
CC {ECO:0000269|PubMed:12827470, ECO:0000269|PubMed:15958665,
CC ECO:0000269|PubMed:16171404, ECO:0000269|PubMed:19297465,
CC ECO:0000269|PubMed:34685766}. Host cell membrane
CC {ECO:0000269|PubMed:12350355}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=In the cytoplasm,
CC associates with inclusion bodies (PubMed:23903836). During bud
CC formation, associates at the inner side of the plasma membrane of
CC infected cells. {ECO:0000269|PubMed:23903836, ECO:0000305}.
CC -!- PTM: Phosphorylation is important for oligomerization.
CC {ECO:0000269|PubMed:24672034}.
CC -!- SIMILARITY: Belongs to the pneumovirinae M protein family.
CC {ECO:0000305}.
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DR EMBL; M11486; AAB59854.1; -; Genomic_RNA.
DR EMBL; U50362; AAB86660.1; -; Genomic_RNA.
DR EMBL; U50363; AAB86672.1; -; Genomic_RNA.
DR EMBL; U63644; AAC55966.1; -; Genomic_RNA.
DR EMBL; AF035006; AAC14898.1; -; Genomic_RNA.
DR PIR; A04030; MFNZ.
DR PDB; 2VQP; X-ray; 1.60 A; A=1-256.
DR PDB; 2YKD; X-ray; 1.86 A; A=1-256.
DR PDB; 4D4T; X-ray; 1.90 A; A=1-256.
DR PDB; 4V23; X-ray; 1.70 A; A=1-256.
DR PDBsum; 2VQP; -.
DR PDBsum; 2YKD; -.
DR PDBsum; 4D4T; -.
DR PDBsum; 4V23; -.
DR SMR; P0DOE7; -.
DR IntAct; P0DOE7; 29.
DR iPTMnet; P0DOE7; -.
DR Proteomes; UP000007678; Genome.
DR Proteomes; UP000134464; Genome.
DR Proteomes; UP000181145; Genome.
DR Proteomes; UP000181262; Genome.
DR Proteomes; UP000181559; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR GO; GO:0019068; P:virion assembly; IEA:InterPro.
DR Gene3D; 2.70.20.30; -; 1.
DR InterPro; IPR005056; Pneu_matrix.
DR InterPro; IPR043062; Pneu_matrix_N.
DR Pfam; PF03393; Pneumo_matrix; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cell membrane; Host cytoplasm; Host membrane;
KW Host nucleus; Host-virus interaction; Membrane; Phosphoprotein;
KW Reference proteome; Viral matrix protein; Virion.
FT CHAIN 1..256
FT /note="Matrix protein"
FT /id="PRO_0000142748"
FT REGION 1..110
FT /note="Interaction with M2-1"
FT /evidence="ECO:0000269|PubMed:18579594"
FT REGION 110..183
FT /note="Nuclear targeting and binding to host importin
FT KPNB1"
FT /evidence="ECO:0000269|PubMed:16171404"
FT MOTIF 194..206
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:19297465"
FT MOD_RES 205
FT /note="Phosphothreonine; by host CK2"
FT /evidence="ECO:0000269|PubMed:24672034"
FT MUTAGEN 170
FT /note="R->A: About 80% loss of host transcriptional
FT inhibition activity; when associated with A-172."
FT /evidence="ECO:0000269|PubMed:34685766"
FT MUTAGEN 172
FT /note="K->A: About 80% loss of host transcriptional
FT inhibition activity; when associated with A-170."
FT /evidence="ECO:0000269|PubMed:34685766"
FT MUTAGEN 205
FT /note="T->A: Loss of higher-order oligomer assembly."
FT /evidence="ECO:0000269|PubMed:24672034"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 12..28
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 108..120
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 140..151
FT /evidence="ECO:0007829|PDB:2VQP"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2VQP"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 193..205
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2VQP"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:2VQP"
FT STRAND 242..253
FT /evidence="ECO:0007829|PDB:2VQP"
SQ 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
