NCAP_RVFV
ID NCAP_RVFV Reviewed; 245 AA.
AC D3K5I7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Rift valley fever virus (RVFV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus.
OX NCBI_TaxID=11588;
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 DNA].
RX PubMed=17192303; DOI=10.1128/JVI.02095-06;
RA Bird B.H., Khristova M.L., Rollin P.E., Ksiazek T.G., Nichol S.T.;
RT "Complete genome analysis of 33 ecologically and biologically diverse Rift
RT Valley fever virus strains reveals widespread virus movement and low
RT genetic diversity due to recent common ancestry.";
RL J. Virol. 81:2805-2816(2007).
RN [2] {ECO:0007744|PDB:3LYF}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS),
RP SUBUNIT, FUNCTION, AND MUTAGENESIS OF TRP-125 AND ARG-178.
RC STRAIN=ZH-501 {ECO:0000312|EMBL:ADC42124.1};
RX PubMed=20547879; DOI=10.1073/pnas.1001760107;
RA Raymond D.D., Piper M.E., Gerrard S.R., Smith J.L.;
RT "Structure of the Rift Valley fever virus nucleocapsid protein reveals
RT another architecture for RNA encapsidation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11769-11774(2010).
RN [3]
RP RNA-BINDING, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=34960686; DOI=10.3390/v13122417;
RA Hayashi M., Schultz E.P., Lanchy J.M., Lodmell J.S.;
RT "Time-Resolved Analysis of N-RNA Interactions during RVFV Infection Shows
RT Qualitative and Quantitative Shifts in RNA Encapsidation and Packaging.";
RL Viruses 13:0-0(2021).
RN [4] {ECO:0007744|PDB:4H5M, ECO:0007744|PDB:4H5O, ECO:0007744|PDB:4H5P, ECO:0007744|PDB:4H5Q, ECO:0007744|PDB:4V9E}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH SINGLE-STRANDED RNA,
RP RNA-BINDING, SUBUNIT, AND FUNCTION.
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).
CC -!- FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases
CC (Probable) (PubMed:20547879). Displays high affinity for single-
CC stranded nucleic acid (PubMed:23129612). The encapsidated genomic RNA
CC is termed the nucleocapsid (NC) or ribonucleoprotein (PubMed:20547879).
CC The ribonucleoprotein has a non-helical structure (PubMed:20547879).
CC Serves as template for viral transcription and replication (By
CC similarity). 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:P21700,
CC ECO:0000269|PubMed:20547879, ECO:0000269|PubMed:23129612,
CC ECO:0000305|PubMed:34960686}.
CC -!- SUBUNIT: Homodimer (PubMed:20547879). Homohexamer; ring-shaped,
CC necessary to form the nucleocapsid (PubMed:20547879, PubMed:23129612).
CC Homopentamers; opened pentamers in solution (By similarity). Binds to
CC viral genomic RNA (PubMed:34960686). Interacts with glycoprotein Gn;
CC this interaction allows packaging of nucleocapsids into virions (By
CC similarity). {ECO:0000250|UniProtKB:P21700,
CC ECO:0000250|UniProtKB:P21701, ECO:0000269|PubMed:20547879,
CC ECO:0000269|PubMed:23129612, ECO:0000269|PubMed:34960686}.
CC -!- INTERACTION:
CC D3K5I7; D3K5I7: N; NbExp=6; IntAct=EBI-15861524, EBI-15861524;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:34960686}. Host
CC cytoplasm {ECO:0000269|PubMed:34960686}. Host nucleus
CC {ECO:0000269|PubMed:34960686}. 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; GU372973; ADC42124.1; -; mRNA.
DR PDB; 3LYF; X-ray; 1.93 A; A/B/C/D=1-245.
DR PDB; 4H5M; X-ray; 3.10 A; A/B/C/D/E/F=1-245.
DR PDB; 4H5O; X-ray; 3.90 A; A/B/C/D/E/F/G/H/I/J=1-245.
DR PDB; 4H5P; X-ray; 2.15 A; A/B/C/D=1-245.
DR PDB; 4H5Q; X-ray; 2.70 A; A/B/C=1-245.
DR PDB; 4V9E; X-ray; 3.40 A; AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL=1-245.
DR PDBsum; 3LYF; -.
DR PDBsum; 4H5M; -.
DR PDBsum; 4H5O; -.
DR PDBsum; 4H5P; -.
DR PDBsum; 4H5Q; -.
DR PDBsum; 4V9E; -.
DR SMR; D3K5I7; -.
DR DIP; DIP-59349N; -.
DR Proteomes; UP000150713; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; Host cytoplasm; Host Golgi apparatus;
KW Host nucleus; Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..245
FT /note="Nucleoprotein"
FT /id="PRO_0000456175"
FT REGION 1..71
FT /note="Essential for oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P21700"
FT SITE 30
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23129612"
FT SITE 33
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23129612"
FT SITE 66
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23129612"
FT SITE 67
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23129612"
FT SITE 70
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23129612"
FT SITE 99
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23129612"
FT SITE 106
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23129612"
FT SITE 125
FT /note="Important for dimerization"
FT /evidence="ECO:0000269|PubMed:20547879"
FT MUTAGEN 125
FT /note="W->A: Almost complete loss of transcription."
FT /evidence="ECO:0000269|PubMed:20547879"
FT MUTAGEN 178
FT /note="R->E: 90% loss of transcription."
FT /evidence="ECO:0000269|PubMed:20547879"
FT MUTAGEN 178
FT /note="R->Q: 75% loss of 30transcription."
FT /evidence="ECO:0000269|PubMed:20547879"
SQ SEQUENCE 245 AA; 27330 MW; E13DACE16314CB58 CRC64;
MDNYQELAIQ FAAQAVDRNE IEQWVREFAY QGFDARRVIE LLKQYGGADW EKDAKKMIVL
ALTRGNKPRR MMMKMSKEGK ATVEALINKY KLKEGNPSRD ELTLSRVAAA LAGRTCQALV
VLSEWLPVTG TTMDGLSPAY PRHMMHPSFA GMVDPSLPGD YLRAILDAHS LYLLQFSRVI
NPNLRGRTKE EVAATFTQPM NAAVNSNFIS HEKRREFLKA FGLVDSNGKP SAAVMAAAQA
YKTAA
