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 27-MAR-2024, entry version 76. 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 Phlebovirus toscanaense. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8BPK; X-ray; 3.60 A; A=2-253. DR PDBsum; 4CSF; -. DR PDBsum; 4CSG; -. DR PDBsum; 4H5L; -. DR PDBsum; 5FVA; -. DR PDBsum; 8BPK; -. 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:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell. DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:1990904; C:ribonucleoprotein complex; 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; Reference proteome; Ribonucleoprotein; KW RNA-binding; 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 //