PHOSP_HRSVA
ID PHOSP_HRSVA Reviewed; 241 AA.
AC P03421; P90196;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P;
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=6548527; DOI=10.1128/jvi.52.3.991-994.1984;
RA Satake M., Elango N., Venkatesan S.;
RT "Sequence analysis of the respiratory syncytial virus phosphoprotein
RT gene.";
RL J. Virol. 52:991-994(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=8918930; DOI=10.1006/viro.1996.0618;
RA Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R., Crowe J.E. Jr.;
RT "Nucleotide sequence analysis of the respiratory syncytial virus subgroup A
RT cold-passaged (cp) temperature sensitive (ts) cpts-248/404 live attenuated
RT virus vaccine candidate.";
RL Virology 225:419-422(1996).
RN [3]
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 [4]
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 [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 INTERACTION WITH THE NUCLEOPROTEIN, AND MUTAGENESIS OF GLY-172 AND GLU-176.
RX PubMed=11861854; DOI=10.1128/jvi.76.6.2871-2880.2002;
RA Lu B., Brazas R., Ma C.H., Kristoff T., Cheng X., Jin H.;
RT "Identification of temperature-sensitive mutations in the phosphoprotein of
RT respiratory syncytial virus that are likely involved in its interaction
RT with the nucleoprotein.";
RL J. Virol. 76:2871-2880(2002).
RN [7]
RP INTERACTION WITH THE NUCLEOPROTEIN, AND PHOSPHORYLATION AT SER-116;
RP SER-117; SER-119; SER-232 AND SER-237.
RX PubMed=12368320; DOI=10.1128/jvi.76.21.10776-10784.2002;
RA Lu B., Ma C.H., Brazas R., Jin H.;
RT "The major phosphorylation sites of the respiratory syncytial virus
RT phosphoprotein are dispensable for virus replication in vitro.";
RL J. Virol. 76:10776-10784(2002).
RN [8]
RP INTERACTION WITH PROTEIN M2-1, AND MUTAGENESIS OF LEU-101; TYR-102; PHE-109
RP AND PHE-241.
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 [9]
RP DOMAIN, AND SUBUNIT.
RX PubMed=15166449; DOI=10.1099/vir.0.79830-0;
RA Castagne N., Barbier A., Bernard J., Rezaei H., Huet J.C., Henry C.,
RA Da Costa B., Eleouet J.F.;
RT "Biochemical characterization of the respiratory syncytial virus P-P and P-
RT N protein complexes and localization of the P protein oligomerization
RT domain.";
RL J. Gen. Virol. 85:1643-1653(2004).
RN [10]
RP INTERACTION WITH PROTEIN M2-1, AND PHOSPHORYLATION AT THR-108.
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 [11]
RP INTERACTION WITH THE NUCLEOPROTEIN.
RX PubMed=17170452; DOI=10.1099/vir.0.82282-0;
RA Tran T.L., Castagne N., Bhella D., Varela P.F., Bernard J., Chilmonczyk S.,
RA Berkenkamp S., Benhamo V., Grznarova K., Grosclaude J., Nespoulos C.,
RA Rey F.A., Eleouet J.F.;
RT "The nine C-terminal amino acids of the respiratory syncytial virus protein
RT P are necessary and sufficient for binding to ribonucleoprotein complexes
RT in which six ribonucleotides are contacted per N protein protomer.";
RL J. Gen. Virol. 88:196-206(2007).
RN [12]
RP INTERACTION WITH M1-2 PROTEIN, AND SUBUNIT.
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 [13]
RP INTERACTION WITH THE NUCLEOPROTEIN, AND MUTAGENESIS OF ASP-233; LEU-236;
RP GLU-239; 239-GLU-ASP-240 AND PHE-241.
RX PubMed=22623798; DOI=10.1128/jvi.00058-12;
RA Galloux M., Tarus B., Blazevic I., Fix J., Duquerroy S., Eleouet J.F.;
RT "Characterization of a viral phosphoprotein binding site on the surface of
RT the respiratory syncytial nucleoprotein.";
RL J. Virol. 86:8375-8387(2012).
RN [14]
RP INTERACTION WITH THE NUCLEOPROTEIN, AND PHOSPHORYLATION AT SER-232 AND
RP SER-237.
RX PubMed=25407889; DOI=10.1186/s12985-014-0191-2;
RA Shapiro A.B., Gao N., O'Connell N., Hu J., Thresher J., Gu R.F.,
RA Overman R., Hardern I.M., Sproat G.G.;
RT "Quantitative investigation of the affinity of human respiratory syncytial
RT virus phosphoprotein C-terminus binding to nucleocapsid protein.";
RL Virol. J. 11:191-191(2014).
RN [15]
RP INTERACTION WITH THE NUCLEOPROTEIN, AND FUNCTION.
RX PubMed=25568210; DOI=10.1128/jvi.03666-14;
RA Galloux M., Gabiane G., Sourimant J., Richard C.A., England P., Moudjou M.,
RA Aumont-Nicaise M., Fix J., Rameix-Welti M.A., Eleouet J.F.;
RT "Identification and characterization of the binding site of the respiratory
RT syncytial virus phosphoprotein to RNA-free nucleoprotein.";
RL J. Virol. 89:3484-3496(2015).
RN [16]
RP INTERACTION WITH RNA-DIRECTED RNA POLYMERASE L.
RX PubMed=25653447; DOI=10.1128/jvi.03619-14;
RA Sourimant J., Rameix-Welti M.A., Gaillard A.L., Chevret D., Galloux M.,
RA Gault E., Eleouet J.F.;
RT "Fine mapping and characterization of the L-polymerase-binding domain of
RT the respiratory syncytial virus phosphoprotein.";
RL J. Virol. 89:4421-4433(2015).
RN [17]
RP PHOSPHORYLATION AT SER-116; SER-117; SER-119; SER-232 AND SER-237,
RP MUTAGENESIS OF 116-SER--SER-119 AND THR-108, INTERACTION WITH THE
RP NUCLEOPROTEIN, INTERACTION WITH RNA-DIRECTED RNA POLYMERASE L, INTERACTION
RP WITH PROTEIN M2-1, FUNCTION, AND DOMAIN.
RX PubMed=26474524; DOI=10.1016/j.virusres.2015.10.011;
RA Asenjo A., Villanueva N.;
RT "Phosphorylation of the human respiratory syncytial virus P protein
RT mediates M2-2 regulation of viral RNA synthesis, a process that involves
RT two P proteins.";
RL Virus Res. 211:117-125(2016).
RN [18]
RP SUBCELLULAR LOCATION.
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 [19]
RP INTERACTION WITH THE NUCLEOPROTEIN.
RX PubMed=28031463; DOI=10.1074/jbc.m116.765958;
RA Pereira N., Cardone C., Lassoued S., Galloux M., Fix J., Assrir N.,
RA Lescop E., Bontems F., Eleouet J.F., Sizun C.;
RT "New Insights into Structural Disorder in Human Respiratory Syncytial Virus
RT Phosphoprotein and Implications for Binding of Protein Partners.";
RL J. Biol. Chem. 292:2120-2131(2017).
RN [20]
RP INTERACTION WITH M1-2 PROTEIN, INTERACTION WITH HOST PHOSPHATASE PP1,
RP IDENTIFICATION IN A COMPLEX PP1/M2-1/P, MUTAGENESIS OF PHE-87; PHE-98;
RP LEU-101; TYR-102; THR-105; ILE-106; THR-108 AND PHE-109, AND FUNCTION.
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 [21]
RP DOMAIN.
RX PubMed=31009855; DOI=10.1016/j.virol.2019.04.001;
RA Meshram C.D., Oomens A.G.P.;
RT "Identification of a human respiratory syncytial virus phosphoprotein
RT domain required for virus-like-particle formation.";
RL Virology 532:48-54(2019).
RN [22]
RP INTERACTION WITH THE NUCLEOPROTEIN.
RX PubMed=30626736; DOI=10.1074/jbc.ra118.006453;
RA Esneau C., Raynal B., Roblin P., Brule S., Richard C.A., Fix J.,
RA Eleouet J.F., Galloux M.;
RT "Biochemical characterization of the respiratory syncytial virus N0-P
RT complex in solution.";
RL J. Biol. Chem. 294:3647-3660(2019).
RN [23] {ECO:0007744|PDB:4UCB}
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 235-241.
RX PubMed=26246564; DOI=10.1128/jvi.01612-15;
RA Ouizougun-Oubari M., Pereira N., Tarus B., Galloux M., Lassoued S., Fix J.,
RA Tortorici M.A., Hoos S., Baron B., England P., Desmaele D., Couvreur P.,
RA Bontems F., Rey F.A., Eleouet J.F., Sizun C., Slama-Schwok A.,
RA Duquerroy S.;
RT "A Druggable Pocket at the Nucleocapsid/Phosphoprotein Interaction Site of
RT Human Respiratory Syncytial Virus.";
RL J. Virol. 89:11129-11143(2015).
RN [24] {ECO:0007744|PDB:6PZK}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS), AND INTERACTION WITH
RP RNA-DIRECTED RNA POLYMERASE L.
RX PubMed=31495574; DOI=10.1016/j.cell.2019.08.014;
RA Gilman M.S.A., Liu C., Fung A., Behera I., Jordan P., Rigaux P.,
RA Ysebaert N., Tcherniuk S., Sourimant J., Eleouet J.F., Sutto-Ortiz P.,
RA Decroly E., Roymans D., Jin Z., McLellan J.S.;
RT "Structure of the Respiratory Syncytial Virus Polymerase Complex.";
RL Cell 179:193-204.e14(2019).
RN [25] {ECO:0007744|PDB:6UEN}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.67 ANGSTROMS), INTERACTION WITH
RP RNA-DIRECTED RNA POLYMERASE L, AND IDENTIFICATION IN THE POLYMERASE
RP COMPLEX.
RX PubMed=31953395; DOI=10.1038/s41467-019-14246-3;
RA Cao D., Gao Y., Roesler C., Rice S., D'Cunha P., Zhuang L., Slack J.,
RA Domke M., Antonova A., Romanelli S., Keating S., Forero G., Juneja P.,
RA Liang B.;
RT "Cryo-EM structure of the respiratory syncytial virus RNA polymerase.";
RL Nat. Commun. 11:368-368(2020).
CC -!- FUNCTION: Plays critical roles in regulating RNA replication and
CC transcription through its interactions with multiple proteins
CC (PubMed:26474524, PubMed:25568210). Tethers the RNA-directed RNA
CC polymerase L to the nucleoprotein-RNA complex (PubMed:26474524).
CC Recruits the M2-1 protein, a processivity factor that is required for
CC efficient transcription of viral RNA (PubMed:26474524). Acts as a
CC chaperone for neo-synthesized nucleoprotein by forming an N-P complex
CC that preserves N in a monomeric and RNA-free state and prevents the
CC association of nascent N with host cell RNAs (PubMed:25568210).
CC Recruits the host phosphatase PP1 to inclusion bodies to regulate viral
CC transcription (PubMed:29489893). Together with the nucleoprotein,
CC sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting
CC this host defense pathway (By similarity).
CC {ECO:0000250|UniProtKB:P33454, ECO:0000269|PubMed:25568210,
CC ECO:0000269|PubMed:26474524, ECO:0000269|PubMed:29489893}.
CC -!- SUBUNIT: Homotetramer (PubMed:22978633, PubMed:15166449). Interacts
CC with protein M2-1; the interaction between the two tetramers is
CC required for the anti-termination and elongation transcriptional
CC activities of protein M2-1 (PubMed:17098979, PubMed:22978633,
CC PubMed:29489893, PubMed:26474524, PubMed:12970453). Interacts with host
CC phosphatase PP1; this interaction recruits PP1 to the inclusion bodies
CC (PubMed:29489893). Formation of a complex PP1/M2-1/P allows P to target
CC host PP1 phosphatase to the M2-1 substrate (PubMed:29489893). Interacts
CC (via C-terminus) with the nucleoprotein N (via N-terminus); the
CC phosphorylated phosphoprotein P binds to N-RNA complex
CC (PubMed:26474524, PubMed:17170452, PubMed:22623798, PubMed:25407889,
CC PubMed:11861854, PubMed:12368320). Interacts (via N-terminus) with the
CC monomeric RNA-free nucleoprotein N (PubMed:25568210, PubMed:28031463,
CC PubMed:30626736). Interacts (via C-terminus) with RNA-directed RNA
CC polymerase L; the association of P and L forms the polymerase complex
CC (PubMed:26474524, PubMed:25653447, PubMed:31953395).
CC {ECO:0000269|PubMed:11861854, ECO:0000269|PubMed:12368320,
CC ECO:0000269|PubMed:12970453, ECO:0000269|PubMed:15166449,
CC ECO:0000269|PubMed:17098979, ECO:0000269|PubMed:17170452,
CC ECO:0000269|PubMed:22623798, ECO:0000269|PubMed:22978633,
CC ECO:0000269|PubMed:25407889, ECO:0000269|PubMed:25568210,
CC ECO:0000269|PubMed:25653447, ECO:0000269|PubMed:26474524,
CC ECO:0000269|PubMed:28031463, ECO:0000269|PubMed:29489893,
CC ECO:0000269|PubMed:30626736, ECO:0000269|PubMed:31953395}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27654298}. Host
CC cytoplasm {ECO:0000269|PubMed:27654298}. Note=Localizes in cytoplasmic
CC inclusion bodies. {ECO:0000269|PubMed:27654298}.
CC -!- DOMAIN: The N-terminus is important for viral particle assembly
CC (PubMed:31009855). The oligomerization region is central
CC (PubMed:15166449). The C-terminus part contains binding regions for the
CC RNA-directed RNA polymerase L and the nucleoprotein (PubMed:26474524).
CC {ECO:0000269|PubMed:15166449, ECO:0000269|PubMed:26474524,
CC ECO:0000269|PubMed:31009855}.
CC -!- PTM: Constitutively phosphorylated by host (PubMed:17098979).
CC Phosphorylation at S-116, S-117, S-119, S-232 and S-237 is required for
CC transcription inhibition by M2-2 and viral particle egress
CC (PubMed:26474524). Phosphorylation at S-232 and S-237 increases the
CC affinity of the binding to the nucleoprotein (PubMed:25407889).
CC {ECO:0000269|PubMed:17098979, ECO:0000269|PubMed:25407889,
CC ECO:0000269|PubMed:26474524}.
CC -!- SIMILARITY: Belongs to the pneumoviridae phosphoprotein P family.
CC {ECO:0000305}.
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DR EMBL; M11486; AAB59853.1; -; Genomic_RNA.
DR EMBL; U50362; AAB86659.1; -; Genomic_RNA.
DR EMBL; U50363; AAB86671.1; -; Genomic_RNA.
DR EMBL; AF035006; AAC14897.1; -; Genomic_RNA.
DR EMBL; U63644; AAC55965.1; -; Genomic_RNA.
DR PIR; A04037; RRNZ.
DR PDB; 4UCB; X-ray; 2.79 A; C/D=235-241.
DR PDB; 6G0Y; X-ray; 2.42 A; G/H/I/J=90-110.
DR PDB; 6PZK; EM; 3.20 A; B/C/D/E=1-241.
DR PDB; 6UEN; EM; 3.67 A; B/C/D/E=1-241.
DR PDB; 6YP5; NMR; -; A/B/C/D=127-163.
DR PDBsum; 4UCB; -.
DR PDBsum; 6G0Y; -.
DR PDBsum; 6PZK; -.
DR PDBsum; 6UEN; -.
DR PDBsum; 6YP5; -.
DR SMR; P03421; -.
DR IntAct; P03421; 22.
DR BindingDB; P03421; -.
DR ChEMBL; CHEMBL4105718; -.
DR PRIDE; P03421; -.
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:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR DisProt; DP00895; -.
DR InterPro; IPR003487; Pprotein_pneumovir.
DR Pfam; PF02478; Pneumo_phosprot; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host-virus interaction;
KW Inhibition of host NF-kappa-B by virus; Phosphoprotein; Reference proteome;
KW Viral RNA replication; Virion.
FT CHAIN 1..241
FT /note="Phosphoprotein"
FT /id="PRO_0000142723"
FT REGION 1..30
FT /note="Binding to monomeric RNA-free nucleoprotein"
FT /evidence="ECO:0000269|PubMed:25568210"
FT REGION 39..57
FT /note="Important for viral particle assembly"
FT /evidence="ECO:0000269|PubMed:31009855"
FT REGION 58..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..87
FT /note="Binding to host phosphatase PP1"
FT /evidence="ECO:0000269|PubMed:29489893"
FT REGION 90..110
FT /note="Binding to protein M2-1"
FT /evidence="ECO:0000269|PubMed:29489893"
FT REGION 120..160
FT /note="Oligomerization and binding to RNA-directed RNA
FT polymerase L"
FT /evidence="ECO:0000269|PubMed:12970453"
FT REGION 201..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..232
FT /note="Binding to RNA-directed RNA polymerase L"
FT /evidence="ECO:0000269|PubMed:25653447,
FT ECO:0000269|PubMed:26474524"
FT REGION 232..241
FT /note="Binding to the N-RNA complex"
FT /evidence="ECO:0000269|PubMed:17170452,
FT ECO:0000269|PubMed:25407889, ECO:0000269|PubMed:26474524"
FT COMPBIAS 58..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 108
FT /note="Interaction with protein M2-1"
FT MOD_RES 108
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:17098979"
FT MOD_RES 116
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:12368320,
FT ECO:0000269|PubMed:26474524"
FT MOD_RES 117
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:12368320,
FT ECO:0000269|PubMed:26474524"
FT MOD_RES 119
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:12368320,
FT ECO:0000269|PubMed:26474524"
FT MOD_RES 232
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:12368320,
FT ECO:0000269|PubMed:26474524"
FT MOD_RES 237
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:12368320,
FT ECO:0000269|PubMed:26474524"
FT VARIANT 171
FT /note="I -> V"
FT MUTAGEN 87
FT /note="F->A: Almost complete loss of viral transcription.
FT Complete loss of interaction with host phospatase PP1."
FT /evidence="ECO:0000269|PubMed:29489893"
FT MUTAGEN 98
FT /note="F->A: Complete loss of interaction with protein M2-
FT 1. Almost complete loss of viral transcription and loss of
FT localization of protein M2-1 in inclusion bodies."
FT /evidence="ECO:0000269|PubMed:29489893"
FT MUTAGEN 101
FT /note="L->A: Complete loss of interaction with protein M2-
FT 1. Almost complete loss of viral transcription and loss of
FT localization of protein M2-1 in inclusion bodies."
FT /evidence="ECO:0000269|PubMed:12970453,
FT ECO:0000269|PubMed:29489893"
FT MUTAGEN 102
FT /note="Y->A: Complete loss of interaction with protein M2-
FT 1. Almost complete loss of viral transcription and loss of
FT localization of protein M2-1 in inclusion bodies."
FT /evidence="ECO:0000269|PubMed:12970453,
FT ECO:0000269|PubMed:29489893"
FT MUTAGEN 105
FT /note="T->A,D: Complete loss of interaction with protein
FT M2-1. Almost complete loss of viral transcription and loss
FT of localization of protein M2-1 in inclusion bodies."
FT /evidence="ECO:0000269|PubMed:29489893"
FT MUTAGEN 106
FT /note="I->A: Complete loss of interaction with protein M2-
FT 1. Almost complete loss of viral transcription and loss of
FT localization of protein M2-1 in inclusion bodies."
FT /evidence="ECO:0000269|PubMed:29489893"
FT MUTAGEN 108
FT /note="T->D: Loss of interaction with protein M2-1 and loss
FT of localization of protein M2-1 in inclusion bodies."
FT /evidence="ECO:0000269|PubMed:26474524,
FT ECO:0000269|PubMed:29489893"
FT MUTAGEN 109
FT /note="F->A: Complete loss of interaction with protein M2-
FT 1. Almost complete loss of viral transcription and loss of
FT localization of protein M2-1 in inclusion bodies."
FT /evidence="ECO:0000269|PubMed:12970453,
FT ECO:0000269|PubMed:29489893"
FT MUTAGEN 116..119
FT /note="SSYS->DDYD: 60% loss of transcription inhibition by
FT M2-2."
FT /evidence="ECO:0000269|PubMed:26474524"
FT MUTAGEN 116..119
FT /note="SSYS->LRYL: 60% loss of transcription inhibition by
FT M2-2."
FT /evidence="ECO:0000269|PubMed:26474524"
FT MUTAGEN 172
FT /note="G->S: Almost complete loss of interaction with the
FT nucleoprotein."
FT /evidence="ECO:0000269|PubMed:11861854"
FT MUTAGEN 176
FT /note="E->G: Complete loss of interaction with the
FT nucleoprotein."
FT /evidence="ECO:0000269|PubMed:11861854"
FT MUTAGEN 233
FT /note="D->A: Complete loss of interaction with the N-RNA
FT complex; when associated with A-239."
FT /evidence="ECO:0000269|PubMed:22623798"
FT MUTAGEN 236
FT /note="L->P: No effect on the interaction with the N-RNA
FT complex."
FT /evidence="ECO:0000269|PubMed:22623798"
FT MUTAGEN 239..240
FT /note="ED->AA: Complete loss of interaction with the N-RNA
FT complex."
FT /evidence="ECO:0000269|PubMed:22623798"
FT MUTAGEN 239
FT /note="E->A: Complete loss of interaction with the N-RNA
FT complex; when associated with A-233."
FT /evidence="ECO:0000269|PubMed:22623798"
FT MUTAGEN 241
FT /note="F->A: Complete loss of interaction with N and viral
FT RNA synthesis."
FT /evidence="ECO:0000269|PubMed:12970453,
FT ECO:0000269|PubMed:22623798"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:6G0Y"
FT HELIX 132..149
FT /evidence="ECO:0007829|PDB:6PZK"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6PZK"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6PZK"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6PZK"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:6PZK"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:6PZK"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:6PZK"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:6PZK"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:6PZK"
SQ SEQUENCE 241 AA; 27148 MW; 21A9E45CA2DFD50C CRC64;
MEKFAPEFHG EDANNRATKF LESIKGKFTS PKDPKKKDSI ISVNSIDIEV TKESPITSNS
TIINPTNETD DTAGNKPNYQ RKPLVSFKED PTPSDNPFSK LYKETIETFD NNEEESSYSY
EEINDQTNDN ITARLDRIDE KLSEILGMLH TLVVASAGPT SARDGIRDAM IGLREEMIEK
IRTEALMTND RLEAMARLRN EESEKMAKDT SDEVSLNPTS EKLNNLLEGN DSDNDLSLED
F
