M21_HRSVA
ID M21_HRSVA Reviewed; 194 AA.
AC P04545; Q77YA8;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Protein M2-1;
DE AltName: Full=Envelope-associated 22 kDa protein;
DE AltName: Full=Transcription antitermination factor M2-1 {ECO:0000303|PubMed:29372904};
DE AltName: Full=Vp24 {ECO:0000303|PubMed:3339328};
GN Name=M2-1;
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=4009789; DOI=10.1128/jvi.55.1.101-110.1985;
RA Elango N., Satake M., Venkatesan S.;
RT "mRNA sequence of three respiratory syncytial virus genes encoding two
RT nonstructural proteins and a 22K structural protein.";
RL J. Virol. 55:101-110(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3838351; DOI=10.1128/jvi.54.1.65-71.1985;
RA Collins P.L., Wertz G.W.;
RT "The envelope-associated 22K protein of human respiratory syncytial virus:
RT nucleotide sequence of the mRNA and a related polytranscript.";
RL J. Virol. 54:65-71(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
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 [5]
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 [6]
RP PHOSPHORYLATION.
RX PubMed=3339328; DOI=10.1099/0022-1317-69-2-313;
RA Lambert D.M., Hambor J., Diebold M., Galinski B.;
RT "Kinetics of synthesis and phosphorylation of respiratory syncytial virus
RT polypeptides.";
RL J. Gen. Virol. 69:313-323(1988).
RN [7]
RP FUNCTION.
RX PubMed=8552680; DOI=10.1073/pnas.93.1.81;
RA Collins P.L., Hill M.G., Cristina J., Grosfeld H.;
RT "Transcription elongation factor of respiratory syncytial virus, a
RT nonsegmented negative-strand RNA virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:81-85(1996).
RN [8]
RP FUNCTION.
RX PubMed=9420254; DOI=10.1128/jvi.72.1.520-526.1998;
RA Hardy R.W., Wertz G.W.;
RT "The product of the respiratory syncytial virus M2 gene ORF1 enhances
RT readthrough of intergenic junctions during viral transcription.";
RL J. Virol. 72:520-526(1998).
RN [9]
RP FUNCTION.
RX PubMed=10364337; DOI=10.1128/jvi.73.7.5852-5864.1999;
RA Fearns R., Collins P.L.;
RT "Role of the M2-1 transcription antitermination protein of respiratory
RT syncytial virus in sequential transcription.";
RL J. Virol. 73:5852-5864(1999).
RN [10]
RP INTERACTION WITH THE NUCLEOPROTEIN, MUTAGENESIS OF CYS-7 AND CYS-15,
RP PHOSPHORYLATION, AND INDUCTION.
RX PubMed=10846068; DOI=10.1128/jvi.74.13.5880-5885.2000;
RA Hardy R.W., Wertz G.W.;
RT "The Cys(3)-His(1) motif of the respiratory syncytial virus M2-1 protein is
RT essential for protein function.";
RL J. Virol. 74:5880-5885(2000).
RN [11]
RP MUTAGENESIS OF CYS-7; CYS-15 AND CYS-21.
RX PubMed=11689613; DOI=10.1128/jvi.75.23.11328-11335.2001;
RA Tang R.S., Nguyen N., Cheng X., Jin H.;
RT "Requirement of cysteines and length of the human respiratory syncytial
RT virus M2-1 protein for protein function and virus viability.";
RL J. Virol. 75:11328-11335(2001).
RN [12]
RP MUTAGENESIS OF SER-58 AND SER-61, AND PHOSPHORYLATION AT SER-58 AND SER-61.
RX PubMed=11711610; DOI=10.1128/jvi.75.24.12188-12197.2001;
RA Cartee T.L., Wertz G.W.;
RT "Respiratory syncytial virus M2-1 protein requires phosphorylation for
RT efficient function and binds viral RNA during infection.";
RL J. Virol. 75:12188-12197(2001).
RN [13]
RP SUBCELLULAR LOCATION.
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 [14]
RP MUTAGENESIS OF LEU-16; ASN-17 AND 16-LEU-ASN-17.
RX PubMed=12692207; DOI=10.1128/jvi.77.9.5046-5053.2003;
RA Zhou H., Cheng X., Jin H.;
RT "Identification of amino acids that are critical to the processivity
RT function of respiratory syncytial virus M2-1 protein.";
RL J. Virol. 77:5046-5053(2003).
RN [15]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=12970453; DOI=10.1128/jvi.77.19.10670-10676.2003;
RA Mason S.W., Aberg E., Lawetz C., DeLong R., Whitehead P., Liuzzi M.;
RT "Interaction between human respiratory syncytial virus (RSV) M2-1 and P
RT proteins is required for reconstitution of M2-1-dependent RSV minigenome
RT activity.";
RL J. Virol. 77:10670-10676(2003).
RN [16]
RP INTERACTION WITH HOST RELA, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15629770; DOI=10.1016/j.virol.2004.10.031;
RA Reimers K., Buchholz K., Werchau H.;
RT "Respiratory syncytial virus M2-1 protein induces the activation of nuclear
RT factor kappa B.";
RL Virology 331:260-268(2005).
RN [17]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=17098979; DOI=10.1099/vir.0.82165-0;
RA Asenjo A., Calvo E., Villanueva N.;
RT "Phosphorylation of human respiratory syncytial virus P protein at
RT threonine 108 controls its interaction with the M2-1 protein in the viral
RT RNA polymerase complex.";
RL J. Gen. Virol. 87:3637-3642(2006).
RN [18]
RP INTERACTION WITH THE MATRIX PROTEIN, 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 [19]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=19386701; DOI=10.1128/jvi.00335-09;
RA Tran T.L., Castagne N., Dubosclard V., Noinville S., Koch E., Moudjou M.,
RA Henry C., Bernard J., Yeo R.P., Eleouet J.F.;
RT "The respiratory syncytial virus M2-1 protein forms tetramers and interacts
RT with RNA and P in a competitive manner.";
RL J. Virol. 83:6363-6374(2009).
RN [20]
RP SUBUNIT, AND INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=22978633; DOI=10.1021/bi300765c;
RA Esperante S.A., Paris G., de Prat-Gay G.;
RT "Modular unfolding and dissociation of the human respiratory syncytial
RT virus phosphoprotein p and its interaction with the m(2-1) antiterminator:
RT a singular tetramer-tetramer interface arrangement.";
RL Biochemistry 51:8100-8110(2012).
RN [21]
RP SUBCELLULAR LOCATION.
RX PubMed=23776214; DOI=10.1073/pnas.1309070110;
RA Liljeroos L., Krzyzaniak M.A., Helenius A., Butcher S.J.;
RT "Architecture of respiratory syncytial virus revealed by electron
RT cryotomography.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11133-11138(2013).
RN [22]
RP SUBCELLULAR LOCATION.
RX PubMed=24760890; DOI=10.1128/jvi.00256-14;
RA Kiss G., Holl J.M., Williams G.M., Alonas E., Vanover D., Lifland A.W.,
RA Gudheti M., Guerrero-Ferreira R.C., Nair V., Yi H., Graham B.S.,
RA Santangelo P.J., Wright E.R.;
RT "Structural analysis of respiratory syncytial virus reveals the position of
RT M2-1 between the matrix protein and the ribonucleoprotein complex.";
RL J. Virol. 88:7602-7617(2014).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF ARG-151.
RX PubMed=27194388; DOI=10.1038/srep25806;
RA Bailly B., Richard C.A., Sharma G., Wang L., Johansen L., Cao J.,
RA Pendharkar V., Sharma D.C., Galloux M., Wang Y., Cui R., Zou G.,
RA Guillon P., von Itzstein M., Eleouet J.F., Altmeyer R.;
RT "Targeting human respiratory syncytial virus transcription anti-termination
RT factor M2-1 to inhibit in vivo viral replication.";
RL Sci. Rep. 6:25806-25806(2016).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=28916773; DOI=10.1038/s41467-017-00655-9;
RA Rincheval V., Lelek M., Gault E., Bouillier C., Sitterlin D.,
RA Blouquit-Laye S., Galloux M., Zimmer C., Eleouet J.F., Rameix-Welti M.A.;
RT "Functional organization of cytoplasmic inclusion bodies in cells infected
RT by respiratory syncytial virus.";
RL Nat. Commun. 8:563-563(2017).
RN [25]
RP PHOSPHORYLATION, INTERACTION WITH THE PHOSPHOPROTEIN, IDENTIFICATION IN A
RP COMPLEX M2-1/P/PP1, AND SUBCELLULAR LOCATION.
RX PubMed=29489893; DOI=10.1371/journal.ppat.1006920;
RA Richard C.A., Rincheval V., Lassoued S., Fix J., Cardone C., Esneau C.,
RA Nekhai S., Galloux M., Rameix-Welti M.A., Sizun C., Eleouet J.F.;
RT "RSV hijacks cellular protein phosphatase 1 to regulate M2-1
RT phosphorylation and viral transcription.";
RL PLoS Pathog. 14:e1006920-e1006920(2018).
RN [26]
RP INTERACTION WITH HOST PABPC1, AND SUBCELLULAR LOCATION.
RX PubMed=31649314; DOI=10.1038/s41598-019-51746-0;
RA Bouillier C., Cosentino G., Leger T., Rincheval V., Richard C.A.,
RA Desquesnes A., Sitterlin D., Blouquit-Laye S., Eleouet J.F., Gault E.,
RA Rameix-Welti M.A.;
RT "The Interactome analysis of the Respiratory Syncytial Virus protein M2-1
RT suggests a new role in viral mRNA metabolism post-transcription.";
RL Sci. Rep. 9:15258-15258(2019).
RN [27]
RP STRUCTURE BY NMR OF 58-177, FUNCTION, INTERACTION WITH THE PHOSPHOPROTEIN
RP AND NUCLEOPROTEIN, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-92;
RP ARG-126; THR-130; LEU-148; LYS-150; ARG-151; THR-160 AND ASN-163.
RX PubMed=22675274; DOI=10.1371/journal.ppat.1002734;
RA Blondot M.L., Dubosclard V., Fix J., Lassoued S., Aumont-Nicaise M.,
RA Bontems F., Eleouet J.F., Sizun C.;
RT "Structure and functional analysis of the RNA- and viral phosphoprotein-
RT binding domain of respiratory syncytial virus M2-1 protein.";
RL PLoS Pathog. 8:E1002734-E1002734(2012).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH ZINC, AND DOMAIN.
RX PubMed=24434552; DOI=10.1073/pnas.1317262111;
RA Tanner S.J., Ariza A., Richard C.A., Kyle H.F., Dods R.L., Blondot M.L.,
RA Wu W., Trincao J., Trinh C.H., Hiscox J.A., Carroll M.W., Silman N.J.,
RA Eleouet J.F., Edwards T.A., Barr J.N.;
RT "Crystal structure of the essential transcription antiterminator M2-1
RT protein of human respiratory syncytial virus and implications of its
RT phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:1580-1585(2014).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 73-175, AND SUBUNIT.
RX PubMed=29372904; DOI=10.1107/s2053230x17017381;
RA Molina I.G., Josts I., Almeida Hernandez Y., Esperante S., Salgueiro M.,
RA Garcia Alai M.M., de Prat-Gay G., Tidow H.;
RT "RNA-binding core domain reveals a compact and cooperative folding unit.";
RL Acta Crystallogr. F Struct. Biol. Commun. 74:23-30(2018).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ZINC AND RNA,
RP SUBUNIT, RNA-BINDING, AND MUTAGENESIS OF THR-91; LYS-92; LYS-150 AND
RP ARG-151.
RX PubMed=32697936; DOI=10.1016/j.str.2020.07.001;
RA Gao Y., Cao D., Pawnikar S., John K.P., Ahn H.M., Hill S., Ha J.M.,
RA Parikh P., Ogilvie C., Swain A., Yang A., Bell A., Salazar A., Miao Y.,
RA Liang B.;
RT "Structure of the Human Respiratory Syncytial Virus M2-1 Protein in Complex
RT with a Short Positive-Sense Gene-End RNA.";
RL Structure 28:1-12(2020).
CC -!- FUNCTION: Acts as a tetrameric transcription processivity factor that
CC binds in a competitive manner to RNA and the phosphoprotein (P) to
CC prevent premature termination during transcription (PubMed:19386701,
CC PubMed:22675274). Transcription anti-terminator that enhances
CC readthrough of intergenic junctions during viral transcription
CC (PubMed:10364337, PubMed:27194388, PubMed:8552680, PubMed:9420254).
CC Preferentially binds to poly(A)-rich sequences (PubMed:24434552). Plays
CC a role in the association of the matrix protein with the nucleocapsid,
CC which initiates assembly and budding (PubMed:18579594). Also, can
CC activate host NF-kappa-B through association with host RELA
CC (PubMed:15629770). {ECO:0000269|PubMed:10364337,
CC ECO:0000269|PubMed:15629770, ECO:0000269|PubMed:18579594,
CC ECO:0000269|PubMed:19386701, ECO:0000269|PubMed:22675274,
CC ECO:0000269|PubMed:24434552, ECO:0000269|PubMed:27194388,
CC ECO:0000269|PubMed:8552680, ECO:0000269|PubMed:9420254}.
CC -!- SUBUNIT: Homotetramer (PubMed:19386701, PubMed:29372904,
CC PubMed:32697936). The homotetramer interacts with RNA (PubMed:32697936,
CC PubMed:22675274). Interacts with the phosphoprotein (P); this
CC interaction is required for protein M2-1 function, localization in host
CC inclusion bodies (PubMed:12970453, PubMed:17098979, PubMed:19386701,
CC PubMed:22675274, PubMed:29489893, PubMed:22978633). Formation of a
CC complex host PP1/M2-1/P allows P to target host PP1 phosphatase to the
CC M2-1 substrate (PubMed:29489893). Interacts with the nucleoprotein (N)
CC (PubMed:10846068, PubMed:22675274). Interacts with the matrix protein
CC (M); this interaction directs M localization to cytoplasmic inclusions
CC comprising viral proteins L, N, P, and M2-1 and mediates M association
CC with the nucleocapsid (PubMed:18579594). Interacts with host RELA
CC (PubMed:15629770). Interacts with host PABPC1 (via C-terminus)
CC (PubMed:31649314). {ECO:0000269|PubMed:10846068,
CC ECO:0000269|PubMed:12970453, ECO:0000269|PubMed:15629770,
CC ECO:0000269|PubMed:17098979, ECO:0000269|PubMed:18579594,
CC ECO:0000269|PubMed:19386701, ECO:0000269|PubMed:22675274,
CC ECO:0000269|PubMed:22978633, ECO:0000269|PubMed:29372904,
CC ECO:0000269|PubMed:29489893, ECO:0000269|PubMed:31649314,
CC ECO:0000269|PubMed:32697936}.
CC -!- INTERACTION:
CC P04545; P0DOE7: M; NbExp=3; IntAct=EBI-10042927, EBI-10042882;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:23776214,
CC ECO:0000269|PubMed:24760890}. Host cytoplasm
CC {ECO:0000269|PubMed:11907323, ECO:0000269|PubMed:22675274,
CC ECO:0000269|PubMed:27194388, ECO:0000269|PubMed:28916773,
CC ECO:0000269|PubMed:29489893, ECO:0000269|PubMed:31649314}. Host nucleus
CC {ECO:0000269|PubMed:15629770}. Note=Localizes in cytoplasmic inclusion
CC bodies substructures called inclusion bodies associated granules
CC (IBAGs) (PubMed:22675274, PubMed:28916773, PubMed:29489893,
CC PubMed:31649314). Forms a layer between the matrix and nucleocapsid
CC (PubMed:23776214, PubMed:24760890). {ECO:0000269|PubMed:22675274,
CC ECO:0000269|PubMed:23776214, ECO:0000269|PubMed:24760890,
CC ECO:0000269|PubMed:28916773, ECO:0000269|PubMed:29489893,
CC ECO:0000269|PubMed:31649314}.
CC -!- INDUCTION: Down-regulated by cyclopamine (PubMed:27194388). Expressed
CC early in the viral replication cycle (PubMed:10846068).
CC {ECO:0000269|PubMed:10846068, ECO:0000269|PubMed:27194388}.
CC -!- DOMAIN: Contains a zinc-finger domain on its N-terminus essential for
CC its anti-termination function (PubMed:24434552). Contains an
CC oligomerization domain (PubMed:22675274). The central globular core is
CC responsible for binding to RNA and phosphoprotein (PubMed:22675274).
CC {ECO:0000269|PubMed:22675274, ECO:0000269|PubMed:24434552}.
CC -!- PTM: Phosphorylated by host in infected cells (PubMed:11711610,
CC PubMed:3339328, PubMed:10846068, PubMed:29489893). Only
CC dephosphorylated M2-1 is competent for viral mRNA binding
CC (PubMed:29489893). Cyclic turnover of phosphorylation-dephosphorylation
CC of M2-1 is required for efficient viral transcription
CC (PubMed:29489893). {ECO:0000269|PubMed:10846068,
CC ECO:0000269|PubMed:11711610, ECO:0000269|PubMed:29489893,
CC ECO:0000269|PubMed:3339328}.
CC -!- SIMILARITY: Belongs to the pneumoviridae M2-1 protein family.
CC {ECO:0000305}.
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DR EMBL; M11486; AAB59860.1; -; Genomic_RNA.
DR EMBL; U50362; AAB86665.1; -; Genomic_RNA.
DR EMBL; U50363; AAB86677.1; -; Genomic_RNA.
DR EMBL; U63644; AAC55971.1; -; Genomic_RNA.
DR EMBL; AF035006; AAC14903.1; -; Genomic_RNA.
DR PIR; B93010; WMNZ22.
DR PDB; 2L9J; NMR; -; A=58-177.
DR 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.
DR PDB; 4C3D; X-ray; 2.52 A; A/B=1-194.
DR 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.
DR PDB; 5NOH; X-ray; 1.80 A; A/B=73-175.
DR PDB; 6G0Y; X-ray; 2.42 A; A/C/E/F=1-194.
DR PDB; 6PZQ; X-ray; 2.70 A; A/B/C/D=1-194.
DR PDBsum; 2L9J; -.
DR PDBsum; 4C3B; -.
DR PDBsum; 4C3D; -.
DR PDBsum; 4C3E; -.
DR PDBsum; 5NOH; -.
DR PDBsum; 6G0Y; -.
DR PDBsum; 6PZQ; -.
DR BMRB; P04545; -.
DR SMR; P04545; -.
DR IntAct; P04545; 2.
DR BindingDB; P04545; -.
DR ChEMBL; CHEMBL4105717; -.
DR iPTMnet; P04545; -.
DR PRIDE; P04545; -.
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; IDA:AgBase.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0046782; P:regulation of viral transcription; IEA:InterPro.
DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-KW.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR InterPro; IPR009452; Pneumovirus_M2-1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF06436; Pneumovirus_M2; 1.
DR PIRSF; PIRSF003913; Matrix_glycop-M2_paramyxo; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host NF-kappa-B by virus; Host cytoplasm;
KW Host nucleus; Host-virus interaction; Metal-binding; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription;
KW Transcription antitermination; Transcription regulation;
KW Viral transcription; Virion; Zinc; Zinc-finger.
FT CHAIN 1..194
FT /note="Protein M2-1"
FT /id="PRO_0000142840"
FT ZN_FING 1..28
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723,
FT ECO:0000269|PubMed:24434552, ECO:0000269|PubMed:32697936"
FT REGION 32..49
FT /note="Oligomerization"
FT /evidence="ECO:0000269|PubMed:22675274"
FT REGION 76..171
FT /note="Globular core"
FT /evidence="ECO:0000269|PubMed:22675274"
FT REGION 126..163
FT /note="Binding to the phosphoprotein"
FT /evidence="ECO:0000269|PubMed:32697936"
FT REGION 172..194
FT /note="Disordered"
FT /evidence="ECO:0000269|PubMed:22675274"
FT SITE 8
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000269|PubMed:32697936"
FT SITE 9
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000269|PubMed:32697936"
FT SITE 23
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000269|PubMed:32697936"
FT SITE 92
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000269|PubMed:32697936"
FT SITE 151
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000269|PubMed:32697936"
FT MOD_RES 58
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:11711610"
FT MOD_RES 61
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:11711610"
FT MUTAGEN 7
FT /note="C->G: More than 95% loss of processivity function."
FT /evidence="ECO:0000269|PubMed:11689613"
FT MUTAGEN 7
FT /note="C->S: Complete loss of binding to N protein. Loss of
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:10846068"
FT MUTAGEN 10
FT /note="E->G: Complete loss of binding to N protein."
FT /evidence="ECO:0000269|PubMed:10846068"
FT MUTAGEN 15
FT /note="C->G: About 80% loss of processivity function."
FT /evidence="ECO:0000269|PubMed:11689613"
FT MUTAGEN 15
FT /note="C->S: Complete loss of binding to N protein."
FT /evidence="ECO:0000269|PubMed:10846068"
FT MUTAGEN 16..17
FT /note="LN->SR: 99% loss of processivity function."
FT /evidence="ECO:0000269|PubMed:12692207"
FT MUTAGEN 16
FT /note="L->S: 97% loss of processivity function."
FT /evidence="ECO:0000269|PubMed:12692207"
FT MUTAGEN 17
FT /note="N->R: 94% loss of processivity function."
FT /evidence="ECO:0000269|PubMed:12692207"
FT MUTAGEN 21
FT /note="C->G: About 80% loss of processivity function."
FT /evidence="ECO:0000269|PubMed:11689613"
FT MUTAGEN 58
FT /note="S->A: Complete loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:11711610"
FT MUTAGEN 61
FT /note="S->A: About 50% loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:11711610"
FT MUTAGEN 91
FT /note="T->D: Slight loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:32697936"
FT MUTAGEN 92
FT /note="K->A: Loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:32697936"
FT MUTAGEN 92
FT /note="K->D: Loss of RNA-binding. No effect on M2-1
FT association with inclusion bodies."
FT /evidence="ECO:0000269|PubMed:22675274"
FT MUTAGEN 126
FT /note="R->D: Loss of M2-1 association with inclusion
FT bodies. No effect on RNA-binding."
FT /evidence="ECO:0000269|PubMed:22675274"
FT MUTAGEN 130
FT /note="T->D: Loss of M2-1 association with inclusion
FT bodies. No effect on RNA-binding."
FT /evidence="ECO:0000269|PubMed:22675274"
FT MUTAGEN 148
FT /note="L->A: Loss of M2-1 association with inclusion
FT bodies. No effect on of RNA-binding."
FT /evidence="ECO:0000269|PubMed:22675274"
FT MUTAGEN 150
FT /note="K->A: Almost no loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:22675274"
FT MUTAGEN 150
FT /note="K->D: Loss of RNA-binding. No effect on M2-1
FT association with inclusion bodies."
FT /evidence="ECO:0000269|PubMed:22675274"
FT MUTAGEN 151
FT /note="R->D: Reduced RNA-binding. No effect on M2-1
FT association with inclusion bodies."
FT /evidence="ECO:0000269|PubMed:22675274,
FT ECO:0000269|PubMed:32697936"
FT MUTAGEN 151
FT /note="R->K: Confers virus resistance to cyclopamine in
FT vitro."
FT /evidence="ECO:0000269|PubMed:27194388"
FT MUTAGEN 160
FT /note="T->D: Loss of M2-1 association with inclusion
FT bodies. No effect on RNA-binding."
FT /evidence="ECO:0000269|PubMed:22675274"
FT MUTAGEN 163
FT /note="N->D: Loss of M2-1 association with inclusion
FT bodies. No effect on RNA-binding."
FT /evidence="ECO:0000269|PubMed:22675274"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:4C3E"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4C3E"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4C3E"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:4C3E"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:6G0Y"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6G0Y"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:4C3E"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4C3E"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:6G0Y"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:5NOH"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:5NOH"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:5NOH"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:5NOH"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:5NOH"
FT HELIX 154..173
FT /evidence="ECO:0007829|PDB:5NOH"
SQ 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
