NCAP_TOSV
ID NCAP_TOSV Reviewed; 253 AA.
AC P21701;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Toscana virus (Tos).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus;
OC Toscana phlebovirus.
OX NCBI_TaxID=11590;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=13204; Phlebotomus perniciosus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1846496; DOI=10.1016/0042-6822(91)90087-r;
RA Giorgi C., Accardi L., Nicoletti L., Gro M.C., Takehara K., Hilditch C.,
RA Morikawa S., Bishop D.H.L.;
RT "Sequences and coding strategies of the S RNAs of Toscana and Rift Valley
RT fever viruses compared to those of Punta Toro, Sicilian Sandfly fever, and
RT Uukuniemi viruses.";
RL Virology 180:738-753(1991).
RN [2] {ECO:0007744|PDB:4H5L}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), RNA-BINDING, FUNCTION, AND SUBUNIT.
RX PubMed=23129612; DOI=10.1073/pnas.1213553109;
RA Raymond D.D., Piper M.E., Gerrard S.R., Skiniotis G., Smith J.L.;
RT "Phleboviruses encapsidate their genomes by sequestering RNA bases.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19208-19213(2012).
RN [3] {ECO:0007744|PDB:4CSF, ECO:0007744|PDB:4CSG}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH SINGLE-STRANDED RNA,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF TYR-32; LYS-79 AND LYS-204.
RX PubMed=24688060; DOI=10.1093/nar/gku229;
RA Olal D., Dick A., Woods V.L. Jr., Liu T., Li S., Devignot S., Weber F.,
RA Saphire E.O., Daumke O.;
RT "Structural insights into RNA encapsidation and helical assembly of the
RT Toscana virus nucleoprotein.";
RL Nucleic Acids Res. 42:6025-6037(2014).
RN [4] {ECO:0007744|PDB:5FVA}
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 2-253, FUNCTION, AND SUBUNIT.
RX PubMed=28777080; DOI=10.1107/s2059798317008774;
RA Baklouti A., Goulet A., Lichiere J., Canard B., Charrel R.N., Ferron F.,
RA Coutard B., Papageorgiou N.;
RT "Toscana virus nucleoprotein oligomer organization observed in solution.";
RL Acta Crystallogr. D 73:650-659(2017).
CC -!- FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases
CC (PubMed:24688060, PubMed:28777080). Displays high affinity for single-
CC stranded nucleic acid (PubMed:23129612). The encapsidated genomic RNA
CC is termed the nucleocapsid (NC) or ribonucleoprotein (PubMed:24688060,
CC PubMed:28777080). The ribonucleoprotein has a non-helical structure (By
CC similarity). Serves as template for viral transcription and
CC replication. After replication, the nucleocapsid is recruited to the
CC host Golgi apparatus by glycoprotein Gn for packaging into virus
CC particles (By similarity). {ECO:0000250|UniProtKB:D3K5I7,
CC ECO:0000250|UniProtKB:P21700, ECO:0000269|PubMed:23129612,
CC ECO:0000269|PubMed:24688060, ECO:0000269|PubMed:28777080}.
CC -!- SUBUNIT: Homodimer (By similarity). Homohexamer; ring-shaped, necessary
CC to form the nucleocapsid (PubMed:23129612, PubMed:24688060,
CC PubMed:28777080). Homopentamers; opened pentamers in solution
CC (PubMed:28777080). Binds to viral genomic RNA (PubMed:23129612,
CC PubMed:24688060). Interacts with glycoprotein Gn; this interaction
CC allows packaging of nucleocapsids into virions (By similarity).
CC {ECO:0000250|UniProtKB:D3K5I7, ECO:0000250|UniProtKB:P21700,
CC ECO:0000269|PubMed:23129612, ECO:0000269|PubMed:24688060,
CC ECO:0000269|PubMed:28777080}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:D3K5I7}. Host
CC cytoplasm {ECO:0000250|UniProtKB:D3K5I7}. Host nucleus
CC {ECO:0000250|UniProtKB:D3K5I7}. Host endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250|UniProtKB:I6WJ72}. Host Golgi
CC apparatus {ECO:0000250|UniProtKB:I6WJ72}.
CC -!- SIMILARITY: Belongs to the phlebovirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; X53794; CAA37803.1; -; Genomic_RNA.
DR PIR; B38552; VHVUTV.
DR PDB; 4CSF; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-253.
DR PDB; 4CSG; X-ray; 3.32 A; A/B/C/D/E/F/G/H/I/J/K/L=1-253.
DR PDB; 4H5L; X-ray; 2.75 A; A/B/C/D/E/F=1-253.
DR PDB; 5FVA; X-ray; 3.70 A; A/B/C/D/E/F=2-253.
DR PDBsum; 4CSF; -.
DR PDBsum; 4CSG; -.
DR PDBsum; 4H5L; -.
DR PDBsum; 5FVA; -.
DR SMR; P21701; -.
DR DIP; DIP-60331N; -.
DR Proteomes; UP000204292; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR009522; Capsid_Phlebovir/Tenuivir.
DR InterPro; IPR015971; Nucleocapsid_Phlebovirus.
DR Pfam; PF05733; Tenui_N; 1.
DR PIRSF; PIRSF003953; N_PhelboV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Helical capsid protein; Host cytoplasm;
KW Host Golgi apparatus; Host nucleus; Ribonucleoprotein; RNA-binding;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..253
FT /note="Nucleoprotein"
FT /id="PRO_0000221997"
FT SITE 32
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 35
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 68
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 72
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 110
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 111
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 191
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 201
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 204
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT SITE 211
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:24688060"
FT MUTAGEN 32
FT /note="Y->A: Reduced RNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:24688060"
FT MUTAGEN 79
FT /note="K->A: No effect on RNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:24688060"
FT MUTAGEN 204
FT /note="K->A: No effect on RNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:24688060"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 55..69
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:4CSF"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4H5L"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4CSG"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4CSF"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:4CSF"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:4CSF"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:4H5L"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:4CSF"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:4CSF"
SQ SEQUENCE 253 AA; 27704 MW; 33ECBA8444A612D1 CRC64;
MSDENYRDIA LAFLDESADS GTINAWVNEF AYQGFDPKRI VQLVKERGTA KGRDWKKDVK
MMIVLNLVRG NKPEAMMKKM SEKGASIVAN LISVYQLKEG NPGRDTITLS RVSAAFVPWT
VQALRVLSES LPVSGTTMDA IAGVTYPRAM MHPSFAGIID LDLPNGAGAT IADAHGLFMI
EFSKTINPSL RTKQANEVAA TFEKPNMAAM SGRFFTREDK KKLLIAVGII DEDLVLASAV
VRSAEKYRAK VGK
