ID NCAP_RVFVZ Reviewed; 245 AA. AC P21700; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1991, sequence version 1. DT 08-NOV-2023, entry version 85. DE RecName: Full=Nucleoprotein; DE AltName: Full=Nucleocapsid protein; DE Short=Protein N; GN Name=N; OS Rift valley fever virus (strain ZH-548 M12) (RVFV). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus; OC Phlebovirus riftense. OX NCBI_TaxID=11589; OH NCBI_TaxID=7158; Aedes. OH NCBI_TaxID=9913; Bos taurus (Bovine). OH NCBI_TaxID=297284; Bos taurus x Bison bison (beefalo). OH NCBI_TaxID=9837; Camelus bactrianus (Bactrian camel). OH NCBI_TaxID=9925; Capra hircus (Goat). OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9940; Ovis aries (Sheep). OH NCBI_TaxID=29031; Phlebotomus papatasi (Sandfly). 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] RP FUNCTION. RC STRAIN=MP12; RX PubMed=7769655; DOI=10.1128/jvi.69.7.3972-3979.1995; RA Lopez N., Muller R., Prehaud C., Bouloy M.; RT "The L protein of Rift Valley fever virus can rescue viral RT ribonucleoproteins and transcribe synthetic genome-like RNA molecules."; RL J. Virol. 69:3972-3979(1995). RN [3] RP SUBUNIT, AND REGION. RC STRAIN=MP12; RX PubMed=16140773; DOI=10.1128/jvi.79.18.11974-11980.2005; RA Le May N., Gauliard N., Billecocq A., Bouloy M.; RT "The N terminus of Rift Valley fever virus nucleoprotein is essential for RT dimerization."; RL J. Virol. 79:11974-11980(2005). RN [4] RP INTERACTION WITH GLYCOPROTEIN GN, AND FUNCTION. RX PubMed=21445316; DOI=10.1371/journal.pone.0018070; RA Piper M.E., Sorenson D.R., Gerrard S.R.; RT "Efficient cellular release of Rift Valley fever virus requires genomic RT RNA."; RL PLoS ONE 6:E18070-E18070(2011). RN [5] {ECO:0007744|PDB:3OUO, ECO:0007744|PDB:3OV9} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF ARG-64; RP LYS-67 AND LYS-74. RC STRAIN=Smithburn; RX PubMed=21589902; DOI=10.1371/journal.ppat.1002030; RA Ferron F., Li Z., Danek E.I., Luo D., Wong Y., Coutard B., Lantez V., RA Charrel R., Canard B., Walz T., Lescar J.; RT "The hexamer structure of Rift Valley fever virus nucleoprotein suggests a RT mechanism for its assembly into ribonucleoprotein complexes."; RL PLoS Pathog. 7:e1002030-e1002030(2011). CC -!- FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases CC (By similarity). Displays high affinity for single-stranded nucleic CC acid (By similarity). The encapsidated genomic RNA is termed the CC nucleocapsid (NC) (By similarity). The ribonucleoprotein has a non- CC helical structure (By similarity). Serves as template for viral CC transcription and replication (PubMed:7769655). After replication, the CC nucleocapsid is recruited to the host Golgi apparatus by glycoprotein CC Gn for packaging into virus particles (PubMed:21445316). CC {ECO:0000250|UniProtKB:D3K5I7, ECO:0000269|PubMed:21445316, CC ECO:0000269|PubMed:7769655}. CC -!- SUBUNIT: Homodimer (PubMed:16140773). Homohexamer; ring-shaped, CC necessary to form the nucleocapsid (PubMed:16140773, PubMed:21589902). CC Homopentamers; opened pentamers in solution (By similarity). Binds to CC viral genomic RNA (By similarity). Interacts with glycoprotein Gn; this CC interaction allows packaging of nucleocapsids into virions CC (PubMed:21445316). {ECO:0000250|UniProtKB:D3K5I7, CC ECO:0000250|UniProtKB:P21701, ECO:0000269|PubMed:16140773, CC ECO:0000269|PubMed:21445316, ECO:0000269|PubMed:21589902}. CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm CC {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; X53771; CAA37789.1; -; Genomic_RNA. DR PIR; D38552; VHVURV. DR PDB; 3OUO; X-ray; 2.30 A; A/B/C=1-245. DR PDB; 3OV9; X-ray; 1.60 A; A/B/C=1-245. DR PDBsum; 3OUO; -. DR PDBsum; 3OV9; -. DR SMR; P21700; -. DR EvolutionaryTrace; P21700; -. DR Proteomes; UP000002477; 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..245 FT /note="Nucleoprotein" FT /id="PRO_0000221995" FT REGION 1..71 FT /note="Essential for oligomerization" FT /evidence="ECO:0000269|PubMed:16140773" FT SITE 30 FT /note="RNA-binding" FT /evidence="ECO:0000250|UniProtKB:D3K5I7" FT SITE 33 FT /note="RNA-binding" FT /evidence="ECO:0000250|UniProtKB:D3K5I7" FT SITE 66 FT /note="RNA-binding" FT /evidence="ECO:0000250|UniProtKB:D3K5I7" FT SITE 67 FT /note="RNA-binding" FT /evidence="ECO:0000250|UniProtKB:D3K5I7" FT SITE 70 FT /note="RNA-binding" FT /evidence="ECO:0000250|UniProtKB:D3K5I7" FT SITE 99 FT /note="RNA-binding" FT /evidence="ECO:0000250|UniProtKB:D3K5I7" FT SITE 106 FT /note="RNA-binding" FT /evidence="ECO:0000250|UniProtKB:D3K5I7" FT SITE 125 FT /note="Important for dimerization" FT /evidence="ECO:0000250|UniProtKB:D3K5I7" FT MUTAGEN 64 FT /note="R->D: Complete loss of RNA-binding; when associated FT with A-67 and A-74." FT /evidence="ECO:0000269|PubMed:21589902" FT MUTAGEN 67 FT /note="K->D: Complete loss of RNA-binding; when associated FT with A-64 and A-74." FT /evidence="ECO:0000269|PubMed:21589902" FT MUTAGEN 74 FT /note="K->D: Complete loss of RNA-binding; when associated FT with A-64 and A-67." FT /evidence="ECO:0000269|PubMed:21589902" FT HELIX 4..13 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 18..28 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 35..46 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 50..63 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 68..71 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 77..90 FT /evidence="ECO:0007829|PDB:3OV9" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 104..110 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 112..122 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:3OV9" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 147..152 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 159..180 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:3OUO" FT HELIX 189..204 FT /evidence="ECO:0007829|PDB:3OV9" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 211..220 FT /evidence="ECO:0007829|PDB:3OV9" FT HELIX 232..243 FT /evidence="ECO:0007829|PDB:3OV9" SQ SEQUENCE 245 AA; 27431 MW; 8B6190549F4A6FF5 CRC64; MDNYQELRVQ FAAQAVDRNE IEQWVREFAY QGFDARRVIE LLKQYGGADW EKDAKKMIVL ALTRGNKPRR MMMKMSKEGK ATVEALINKY KLKEGNPSRD ELTLSRVAAA LAGWTCQALV VLSEWLPVTG TTMDGLSPAY PRHMMHPSFA GMVDPSLPGD YLRAILDAHS LYLLQFSRVI NPNLRGRTKE EVAATFTQPM NAAVNSNFIS HEKRREFLKA FGLVDSNGKP SAAVMAAAQA YKTAA //