NCAP_RVFVZ
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 03-AUG-2022, entry version 82.
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).
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}.
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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; 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
