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Matrix M2-1 (Envelope-associated 22 kDa protein)

 M21_HRSVA               Reviewed;         194 AA.
P04545; Q77YA8;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
22-NOV-2017, entry version 81.
RecName: Full=Matrix M2-1;
AltName: Full=Envelope-associated 22 kDa protein;
Name=M2-1;
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=4009789;
Elango N., Satake M., Venkatesan S.;
"mRNA sequence of three respiratory syncytial virus genes encoding two
nonstructural proteins and a 22K structural protein.";
J. Virol. 55:101-110(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3838351;
Collins P.L., Wertz G.W.;
"The envelope-associated 22K protein of human respiratory syncytial
virus: nucleotide sequence of the mRNA and a related polytranscript.";
J. Virol. 54:65-71(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Cold-passage attenuated;
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).
[5]
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).
[6]
PHOSPHORYLATION.
PubMed=3339328; DOI=10.1099/0022-1317-69-2-313;
Lambert D.M., Hambor J., Diebold M., Galinski B.;
"Kinetics of synthesis and phosphorylation of respiratory syncytial
virus polypeptides.";
J. Gen. Virol. 69:313-323(1988).
[7]
FUNCTION.
PubMed=8552680; DOI=10.1073/pnas.93.1.81;
Collins P.L., Hill M.G., Cristina J., Grosfeld H.;
"Transcription elongation factor of respiratory syncytial virus, a
nonsegmented negative-strand RNA virus.";
Proc. Natl. Acad. Sci. U.S.A. 93:81-85(1996).
[8]
FUNCTION.
PubMed=9420254;
Hardy R.W., Wertz G.W.;
"The product of the respiratory syncytial virus M2 gene ORF1 enhances
readthrough of intergenic junctions during viral transcription.";
J. Virol. 72:520-526(1998).
[9]
FUNCTION.
PubMed=10364337;
Fearns R., Collins P.L.;
"Role of the M2-1 transcription antitermination protein of respiratory
syncytial virus in sequential transcription.";
J. Virol. 73:5852-5864(1999).
[10]
INTERACTION WITH N.
PubMed=10846068; DOI=10.1128/JVI.74.13.5880-5885.2000;
Hardy R.W., Wertz G.W.;
"The Cys(3)-His(1) motif of the respiratory syncytial virus M2-1
protein is essential for protein function.";
J. Virol. 74:5880-5885(2000).
[11]
MUTAGENESIS OF CYS-7; CYS-15 AND CYS-21.
PubMed=11689613; DOI=10.1128/JVI.75.23.11328-11335.2001;
Tang R.S., Nguyen N., Cheng X., Jin H.;
"Requirement of cysteines and length of the human respiratory
syncytial virus M2-1 protein for protein function and virus
viability.";
J. Virol. 75:11328-11335(2001).
[12]
MUTAGENESIS OF SER-58 AND SER-61, AND PHOSPHORYLATION AT SER-58 AND
SER-61.
PubMed=11711610; DOI=10.1128/JVI.75.24.12188-12197.2001;
Cartee T.L., Wertz G.W.;
"Respiratory syncytial virus M2-1 protein requires phosphorylation for
efficient function and binds viral RNA during infection.";
J. Virol. 75:12188-12197(2001).
[13]
SUBCELLULAR LOCATION.
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).
[14]
MUTAGENESIS OF LEU-16; ASN-17 AND 16-LEU-ASN-17.
PubMed=12692207; DOI=10.1128/JVI.77.9.5046-5053.2003;
Zhou H., Cheng X., Jin H.;
"Identification of amino acids that are critical to the processivity
function of respiratory syncytial virus M2-1 protein.";
J. Virol. 77:5046-5053(2003).
[15]
INTERACTION WITH HOST RELA.
PubMed=15629770; DOI=10.1016/j.virol.2004.10.031;
Reimers K., Buchholz K., Werchau H.;
"Respiratory syncytial virus M2-1 protein induces the activation of
nuclear factor kappa B.";
Virology 331:260-268(2005).
[16]
INTERACTION WITH P.
PubMed=17098979; DOI=10.1099/vir.0.82165-0;
Asenjo A., Calvo E., Villanueva N.;
"Phosphorylation of human respiratory syncytial virus P protein at
threonine 108 controls its interaction with the M2-1 protein in the
viral RNA polymerase complex.";
J. Gen. Virol. 87:3637-3642(2006).
[17]
INTERACTION WITH M.
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: Acts as a transcriptional elongation factor to prevent
premature termination during transcription thus allowing complete
synthesis of RSV mRNAs. Functions also as a processivity and
antitermination factor to permit transit of the polymerase through
intergenic regions to access promoter distal genes. Plays a role
in the association of the matrix protein with the nucleocapsid,
which initiates assembly and budding. Also, can activate NF-kappa-
B through association with host RELA.
{ECO:0000269|PubMed:10364337, ECO:0000269|PubMed:8552680,
ECO:0000269|PubMed:9420254}.
-!- SUBUNIT: Interacts with protein M; this interaction directs M
localization to cytoplasmic inclusions comprising viral proteins
L, N, P, and M2-1 and mediates M association with the
nucleocapsid. Interacts with protein P; this interaction is
required for protein M2-1 anti-termination and elongation
transcriptional activities. Interacts with protein N. Interacts
with host RELA. {ECO:0000269|PubMed:10846068,
ECO:0000269|PubMed:15629770, ECO:0000269|PubMed:17098979,
ECO:0000269|PubMed:18579594}.
-!- INTERACTION:
P0DOE7:M; NbExp=3; IntAct=EBI-10042927, EBI-10042882;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
{ECO:0000269|PubMed:11907323}.
-!- DOMAIN: Contains a zinc-finger domain on its N-terminus essential
for its antitermination function.
-!- PTM: Phosphorylated by host in infected cells.
{ECO:0000269|PubMed:11711610, ECO:0000269|PubMed:3339328}.
-----------------------------------------------------------------------
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EMBL; M11486; AAB59860.1; -; Genomic_RNA.
EMBL; U50362; AAB86665.1; -; Genomic_RNA.
EMBL; U50363; AAB86677.1; -; Genomic_RNA.
EMBL; U63644; AAC55971.1; -; Genomic_RNA.
EMBL; AF035006; AAC14903.1; -; Genomic_RNA.
PIR; B93010; WMNZ22.
PDB; 2L9J; NMR; -; A=58-177.
PDB; 4C3B; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-194.
PDB; 4C3D; X-ray; 2.52 A; A/B=1-194.
PDB; 4C3E; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-194.
PDBsum; 2L9J; -.
PDBsum; 4C3B; -.
PDBsum; 4C3D; -.
PDBsum; 4C3E; -.
SMR; P04545; -.
IntAct; P04545; 2.
iPTMnet; P04545; -.
PRIDE; P04545; -.
OrthoDB; VOG090000TG; -.
Proteomes; UP000007678; Genome.
Proteomes; UP000134464; Genome.
Proteomes; UP000181145; Genome.
Proteomes; UP000181262; Genome.
Proteomes; UP000181559; Genome.
GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039652; P:activation by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW.
GO; GO:0046782; P:regulation of viral transcription; IEA:InterPro.
Gene3D; 4.10.1000.10; -; 1.
InterPro; IPR009452; Pneumovirus_M2.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF06436; Pneumovirus_M2; 1.
PIRSF; PIRSF003913; Matrix_glycop-M2_paramyxo; 1.
SMART; SM00356; ZnF_C3H1; 1.
SUPFAM; SSF90229; SSF90229; 1.
PROSITE; PS50103; ZF_C3H1; 1.
1: Evidence at protein level;
3D-structure; Activation of host NF-kappa-B by virus;
Complete proteome; Host cytoplasm; Host-virus interaction;
Metal-binding; Phosphoprotein; Virion; Zinc; Zinc-finger.
CHAIN 1 194 Matrix M2-1.
/FTId=PRO_0000142840.
ZN_FING 1 28 C3H1-type. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
MOD_RES 58 58 Phosphoserine; by host.
{ECO:0000269|PubMed:11711610}.
MOD_RES 61 61 Phosphoserine; by host.
{ECO:0000269|PubMed:11711610}.
MUTAGEN 7 7 C->G: More than 95% loss of processivity
function. {ECO:0000269|PubMed:11689613}.
MUTAGEN 15 15 C->G: About 80% loss of processivity
function. {ECO:0000269|PubMed:11689613}.
MUTAGEN 16 17 LN->SR: 99% loss of processivity
function. {ECO:0000269|PubMed:12692207}.
MUTAGEN 16 16 L->S: 97% loss of processivity function.
{ECO:0000269|PubMed:12692207}.
MUTAGEN 17 17 N->R: 94% loss of processivity function.
{ECO:0000269|PubMed:12692207}.
MUTAGEN 21 21 C->G: About 80% loss of processivity
function. {ECO:0000269|PubMed:11689613}.
MUTAGEN 58 58 S->A: Complete loss of phosphorylation.
{ECO:0000269|PubMed:11711610}.
MUTAGEN 61 61 S->A: About 50% loss of phosphorylation.
{ECO:0000269|PubMed:11711610}.
HELIX 8 11 {ECO:0000244|PDB:4C3E}.
HELIX 18 20 {ECO:0000244|PDB:4C3E}.
HELIX 27 29 {ECO:0000244|PDB:4C3E}.
HELIX 32 48 {ECO:0000244|PDB:4C3E}.
HELIX 54 57 {ECO:0000244|PDB:4C3B}.
TURN 61 63 {ECO:0000244|PDB:4C3E}.
HELIX 64 67 {ECO:0000244|PDB:4C3E}.
HELIX 69 84 {ECO:0000244|PDB:4C3E}.
HELIX 92 105 {ECO:0000244|PDB:4C3E}.
HELIX 108 116 {ECO:0000244|PDB:4C3E}.
HELIX 124 140 {ECO:0000244|PDB:4C3E}.
HELIX 142 151 {ECO:0000244|PDB:4C3E}.
HELIX 154 172 {ECO:0000244|PDB:4C3E}.
SEQUENCE 194 AA; 22154 MW; CA5B397FE2707EF9 CRC64;
MSRRNPCKFE IRGHCLNGKR CHFSHNYFEW PPHALLVRQN FMLNRILKSM DKSIDTLSEI
SGAAELDRTE EYALGVVGVL ESYIGSINNI TKQSACVAMS KLLTELNSDD IKKLRDNEEL
NSPKIRVYNT VISYIESNRK NNKQTIHLLK RLPADVLKKT IKNTLDIHKS ITINNPKEST
VSDTNDHAKN NDTT


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