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 16-JAN-2019, entry version 73. 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; ssRNA viruses; ssRNA negative-strand viruses; Bunyavirales; OC Phenuiviridae; Phlebovirus. 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., RA Hilditch C., Morikawa S., Bishop D.H.L.; RT "Sequences and coding strategies of the S RNAs of Toscana and Rift RT Valley fever viruses compared to those of Punta Toro, Sicilian Sandfly RT fever, and Uukuniemi viruses."; RL Virology 180:738-753(1991). RN [2] RP FUNCTION. RC STRAIN=MP12; RX PubMed=7769655; 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 RT 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 RT for 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 RT genomic RNA."; RL PLoS ONE 6:E18070-E18070(2011). CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. CC The encapsidated genomic RNA is termed the nucleocapsid (NC). CC Serves as template for viral transcription and replication. After CC replication, the nucleocapsid is recruited to the host Golgi CC apparatus by glycoprotein Gn for packaging into virus particles. CC {ECO:0000269|PubMed:21445316, ECO:0000269|PubMed:7769655}. CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid CC (PubMed:16140773). Binds to viral genomic RNA. Interacts with CC glycoprotein Gn; this interaction allows packaging of CC nucleocapsids into virions (PubMed:21445316). CC {ECO:0000269|PubMed:16140773, ECO:0000269|PubMed:21445316}. CC -!- SUBCELLULAR LOCATION: Virion. Note=Internal protein of virus CC particle. CC -!- SIMILARITY: Belongs to the phlebovirus nucleocapsid protein CC family. {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: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; Complete proteome; KW Helical capsid protein; Reference proteome; Ribonucleoprotein; KW RNA-binding; Viral nucleoprotein; Virion. FT CHAIN 1 245 Nucleoprotein. FT /FTId=PRO_0000221995. FT REGION 1 71 Essential for oligomerization. FT {ECO:0000269|PubMed:16140773}. FT HELIX 4 13 {ECO:0000244|PDB:3OV9}. FT HELIX 18 28 {ECO:0000244|PDB:3OV9}. FT HELIX 35 46 {ECO:0000244|PDB:3OV9}. FT HELIX 47 49 {ECO:0000244|PDB:3OV9}. FT HELIX 50 63 {ECO:0000244|PDB:3OV9}. FT HELIX 68 71 {ECO:0000244|PDB:3OV9}. FT HELIX 72 74 {ECO:0000244|PDB:3OV9}. FT HELIX 77 90 {ECO:0000244|PDB:3OV9}. FT STRAND 94 96 {ECO:0000244|PDB:3OV9}. FT HELIX 104 110 {ECO:0000244|PDB:3OV9}. FT HELIX 112 122 {ECO:0000244|PDB:3OV9}. FT HELIX 123 125 {ECO:0000244|PDB:3OV9}. FT STRAND 126 128 {ECO:0000244|PDB:3OV9}. FT HELIX 130 136 {ECO:0000244|PDB:3OV9}. FT HELIX 142 144 {ECO:0000244|PDB:3OV9}. FT HELIX 147 152 {ECO:0000244|PDB:3OV9}. FT HELIX 159 180 {ECO:0000244|PDB:3OV9}. FT HELIX 182 184 {ECO:0000244|PDB:3OUO}. FT HELIX 189 204 {ECO:0000244|PDB:3OV9}. FT STRAND 207 209 {ECO:0000244|PDB:3OV9}. FT HELIX 211 220 {ECO:0000244|PDB:3OV9}. FT HELIX 232 243 {ECO:0000244|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 //