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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.
12-SEP-2018, entry version 87.
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, FUNCTION, AND SUBCELLULAR LOCATION.
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).
[18]
FUNCTION, SUBUNIT, AND INTERACTION WITH PROTEIN P.
PubMed=19386701; DOI=10.1128/JVI.00335-09;
Tran T.L., Castagne N., Dubosclard V., Noinville S., Koch E.,
Moudjou M., Henry C., Bernard J., Yeo R.P., Eleouet J.F.;
"The respiratory syncytial virus M2-1 protein forms tetramers and
interacts with RNA and P in a competitive manner.";
J. Virol. 83:6363-6374(2009).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=27194388; DOI=10.1038/srep25806;
Bailly B., Richard C.A., Sharma G., Wang L., Johansen L., Cao J.,
Pendharkar V., Sharma D.C., Galloux M., Wang Y., Cui R., Zou G.,
Guillon P., von Itzstein M., Eleouet J.F., Altmeyer R.;
"Targeting human respiratory syncytial virus transcription anti-
termination factor M2-1 to inhibit in vivo viral replication.";
Sci. Rep. 6:25806-25806(2016).
[20]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 73-175.
PubMed=29372904; DOI=10.1107/S2053230X17017381;
Molina I.G., Josts I., Almeida Hernandez Y., Esperante S.,
Salgueiro M., Garcia Alai M.M., de Prat-Gay G., Tidow H.;
"RNA-binding core domain reveals a compact and cooperative folding
unit.";
Acta Crystallogr. F Struct. Biol. Commun. 74:23-30(2018).
[21]
STRUCTURE BY NMR OF 58-177, FUNCTION, INTERACTION WITH PROTEIN P AND
PROTEIN N, AND SUBCELLULAR LOCATION.
PubMed=22675274; DOI=10.1371/journal.ppat.1002734;
Blondot M.L., Dubosclard V., Fix J., Lassoued S., Aumont-Nicaise M.,
Bontems F., Eleouet J.F., Sizun C.;
"Structure and functional analysis of the RNA- and viral
phosphoprotein-binding domain of respiratory syncytial virus M2-1
protein.";
PLoS Pathog. 8:E1002734-E1002734(2012).
[22]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC.
PubMed=24434552; DOI=10.1073/pnas.1317262111;
Tanner S.J., Ariza A., Richard C.A., Kyle H.F., Dods R.L.,
Blondot M.L., Wu W., Trincao J., Trinh C.H., Hiscox J.A.,
Carroll M.W., Silman N.J., Eleouet J.F., Edwards T.A., Barr J.N.;
"Crystal structure of the essential transcription antiterminator M2-1
protein of human respiratory syncytial virus and implications of its
phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 111:1580-1585(2014).
-!- FUNCTION: Acts as a tetrameric transcription processivity factor
that binds in a competitive manner to RNA and P. Acts also as an
antitermination factor to prevent premature termination of
transcription. Plays a role in the association of the matrix
protein with the nucleocapsid, which initiates assembly and
budding. Also, can activate host NF-kappa-B through association
with host RELA. {ECO:0000269|PubMed:10364337,
ECO:0000269|PubMed:15629770, ECO:0000269|PubMed:19386701,
ECO:0000269|PubMed:22675274, ECO:0000269|PubMed:27194388,
ECO:0000269|PubMed:8552680, ECO:0000269|PubMed:9420254}.
-!- SUBUNIT: Forms homotetramers (PubMed:19386701). 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
(PubMed:19386701, PubMed:17098979). Interacts with protein N.
Interacts with host RELA (PubMed:15629770).
{ECO:0000269|PubMed:10846068, ECO:0000269|PubMed:15629770,
ECO:0000269|PubMed:17098979, ECO:0000269|PubMed:18579594,
ECO:0000269|PubMed:19386701, ECO:0000269|PubMed:22675274}.
-!- INTERACTION:
P0DOE7:M; NbExp=3; IntAct=EBI-10042927, EBI-10042882;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
{ECO:0000269|PubMed:11907323, ECO:0000269|PubMed:22675274,
ECO:0000269|PubMed:27194388}. Host nucleus
{ECO:0000269|PubMed:15629770}.
-!- DOMAIN: Contains a zinc-finger domain on its N-terminus essential
for its antitermination function. {ECO:0000269|PubMed:24434552}.
-!- 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.
PDB; 5NOH; X-ray; 1.80 A; A/B=73-175.
PDBsum; 2L9J; -.
PDBsum; 4C3B; -.
PDBsum; 4C3D; -.
PDBsum; 4C3E; -.
PDBsum; 5NOH; -.
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.
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 nucleus;
Host-virus interaction; Metal-binding; Phosphoprotein;
Reference proteome; 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 76 85 {ECO:0000244|PDB:5NOH}.
HELIX 92 105 {ECO:0000244|PDB:5NOH}.
HELIX 108 116 {ECO:0000244|PDB:5NOH}.
HELIX 124 140 {ECO:0000244|PDB:5NOH}.
HELIX 142 151 {ECO:0000244|PDB:5NOH}.
HELIX 154 173 {ECO:0000244|PDB:5NOH}.
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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