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 07-APR-2021, entry version 80. 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. 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). CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The CC encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as CC template for viral transcription and replication. After replication, CC the nucleocapsid is recruited to the host Golgi apparatus by CC glycoprotein Gn for packaging into virus particles. CC {ECO:0000269|PubMed:21445316, ECO:0000269|PubMed:7769655}. CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid (PubMed:16140773). CC Binds to viral genomic RNA. Interacts with glycoprotein Gn; this CC interaction allows packaging of nucleocapsids into virions CC (PubMed:21445316). {ECO:0000269|PubMed:16140773, CC ECO:0000269|PubMed:21445316}. CC -!- SUBCELLULAR LOCATION: Virion. Note=Internal protein of virus particle. 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 PRIDE; 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; Helical capsid protein; Reference proteome; KW Ribonucleoprotein; 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 HELIX 4..13 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 18..28 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 35..46 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 47..49 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 50..63 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 68..71 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 72..74 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 77..90 FT /evidence="ECO:0007744|PDB:3OV9" FT STRAND 94..96 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 104..110 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 112..122 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 123..125 FT /evidence="ECO:0007744|PDB:3OV9" FT STRAND 126..128 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 130..136 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 142..144 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 147..152 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 159..180 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 182..184 FT /evidence="ECO:0007744|PDB:3OUO" FT HELIX 189..204 FT /evidence="ECO:0007744|PDB:3OV9" FT STRAND 207..209 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 211..220 FT /evidence="ECO:0007744|PDB:3OV9" FT HELIX 232..243 FT /evidence="ECO:0007744|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 //