NCAP_SFTSV
ID NCAP_SFTSV Reviewed; 245 AA.
AC P0DW82;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 1.
DT 03-AUG-2022, entry version 1.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=NP;
OS SFTS phlebovirus (isolate SFTSV/Human/China/HB29/2010) (Severe fever with
OS thrombocytopenia virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Phenuiviridae; Bandavirus; Dabie bandavirus.
OX NCBI_TaxID=992212;
OH NCBI_TaxID=44386; Haemaphysalis longicornis (Bush tick).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=21410387; DOI=10.1056/nejmoa1010095;
RA Yu X.J., Liang M.F., Zhang S.Y., Liu Y., Li J.D., Sun Y.L., Zhang L.,
RA Zhang Q.F., Popov V.L., Li C., Qu J., Li Q., Zhang Y.P., Hai R., Wu W.,
RA Wang Q., Zhan F.X., Wang X.J., Kan B., Wang S.W., Wan K.L., Jing H.Q.,
RA Lu J.X., Yin W.W., Zhou H., Guan X.H., Liu J.F., Bi Z.Q., Liu G.H., Ren J.,
RA Wang H., Zhao Z., Song J.D., He J.R., Wan T., Zhang J.S., Fu X.P.,
RA Sun L.N., Dong X.P., Feng Z.J., Yang W.Z., Hong T., Zhang Y., Walker D.H.,
RA Wang Y., Li D.X.;
RT "Fever with thrombocytopenia associated with a novel bunyavirus in China.";
RL N. Engl. J. Med. 364:1523-1532(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25552716; DOI=10.1128/jvi.03432-14;
RA Brennan B., Li P., Zhang S., Li A., Liang M., Li D., Elliott R.M.;
RT "A reverse genetic system for severe fever with thrombocytopenia syndrome
RT virus.";
RL J. Virol. 89:3026-3037(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT, FUNCTION, AND MUTAGENESIS
RP OF ALA-8; PHE-11; ALA-25; LEU-28; ARG-64; LYS-67; LYS-70; ARG-95; ARG-99;
RP ARG-106; LYS-164; LYS-184; ARG-186 AND GLU-192.
RX PubMed=23702688; DOI=10.1007/s13238-013-3901-4;
RA Zhou H., Sun Y., Wang Y., Liu M., Liu C., Wang W., Liu X., Li L., Deng F.,
RA Wang H., Guo Y., Lou Z.;
RT "The nucleoprotein of severe fever with thrombocytopenia syndrome virus
RT processes a stable hexameric ring to facilitate RNA encapsidation.";
RL Protein Cell 4:445-455(2013).
CC -!- FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases
CC (PubMed:23702688). Displays high affinity for single-stranded nucleic
CC acid (PubMed:23702688). The encapsidated genomic RNA is termed the
CC nucleocapsid (NC) or ribonucleoprotein (PubMed:23702688). The
CC ribonucleoprotein has a non-helical structure (By similarity). Serves
CC as 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 (By similarity).
CC {ECO:0000250|UniProtKB:D3K5I7, ECO:0000250|UniProtKB:P21700,
CC ECO:0000269|PubMed:23702688}.
CC -!- SUBUNIT: Homodimer (By similarity). Homohexamer; ring-shaped, necessary
CC to form the nucleocapsid (PubMed:23702688). Homopentamers; opened
CC pentamers in solution (By similarity). Binds to viral genomic RNA (By
CC similarity). Interacts with glycoprotein Gn; this interaction allows
CC packaging of nucleocapsids into virions (By similarity).
CC {ECO:0000250|UniProtKB:D3K5I7, ECO:0000250|UniProtKB:P21700,
CC ECO:0000250|UniProtKB:P21701, ECO:0000269|PubMed:23702688}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:D3K5I7}. Host
CC cytoplasm {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 -!- MISCELLANEOUS: Binds suramin, which inhibits the replication of SFTSV
CC in vivo. {ECO:0000250|UniProtKB:I6WJ72}.
CC -!- SIMILARITY: Belongs to the phlebovirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; HM745932; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; KP202165; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR RefSeq; YP_006504092.1; NC_018137.1.
DR GeneID; 13231122; -.
DR KEGG; vg:13231122; -.
DR Proteomes; UP000117954; Genome.
DR Proteomes; UP000201130; 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: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 Capsid protein; Host cytoplasm; Host Golgi apparatus; Host nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Viral nucleoprotein;
KW Virion.
FT CHAIN 1..245
FT /note="Nucleoprotein"
FT /id="PRO_0000456176"
FT SITE 64
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23702688"
FT SITE 67
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23702688"
FT SITE 70
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23702688"
FT SITE 95
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23702688"
FT SITE 106
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23702688"
FT SITE 184
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 8
FT /note="A->K: Complete loss of ringshaped oligomers."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 11
FT /note="F->D: Complete loss of ringshaped oligomers and RNA-
FT binding."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 25
FT /note="A->D: Complete loss of ringshaped oligomers."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 28
FT /note="L->E: 200-fold decrease in RNA binding."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 28
FT /note="L->K: Complete loss of ringshaped oligomers."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 64
FT /note="R->A: Partial loss of RNA-binding. Complete loss of
FT RNA-binding; when associated with A-67 and A-184."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 67
FT /note="K->A: Partial loss of RNA-binding. Complete loss of
FT RNA-binding; when associated with A-64 and A-184."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 70
FT /note="K->A: Partial loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 95
FT /note="R->A: Partial loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 99
FT /note="R->A: No effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 106
FT /note="R->A: Partial loss of RNA-binding. No effect on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 164
FT /note="K->A: No effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 184
FT /note="K->A: Partial loss of RNA-binding. Complete loss of
FT RNA-binding; when associated with A-64 and A-67."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 186
FT /note="R->A: Partial loss of RNA-binding. No effect on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:23702688"
FT MUTAGEN 192
FT /note="E->A: No effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:23702688"
SQ SEQUENCE 245 AA; 26985 MW; 8CB3FD67684F2F42 CRC64;
MSEWSRIAVE FGEQQLNLTE LEDFARELAY EGLDPALIIK KLKETGGDDW VKDTKFIIVF
ALTRGNKIVK ASGKMSNSGS KRLMALQEKY GLVERAETRL SITPVRVAQS LPTWTCAAAA
ALKEYLPVGP AVMNLKVENY PPEMMCMAFG SLIPTAGVSE ATTKTLMEAY SLWQDAFTKT
INVKMRGASK TEVYNSFRDP LHAAVNSVFF PNDVRVKWLK AKGILGPDGV PSRAAEVAAA
AYRNL
