NCAP_RABVS
ID NCAP_RABVS Reviewed; 450 AA.
AC P16285; Q6HA98; Q7TBN9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 23-FEB-2022, entry version 93.
DE RecName: Full=Nucleoprotein;
DE Short=NP;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Rabies virus (strain SAD B19) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11300;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2139267; DOI=10.1016/0042-6822(90)90433-r;
RA Conzelmann K.-K., Cox J.H., Schneider L.G., Thiel H.-J.;
RT "Molecular cloning and complete nucleotide sequence of the attenuated
RT rabies virus SAD B19.";
RL Virology 175:485-499(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=SRV9;
RA Wang T., Zhang S., Hu R.;
RT "Analysis of the whole sequence of rabies virus vaccine strain SRV9.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate SAD B19, Isolate SAD VA1, Isolate SAD1-3670 var 1,
RC Isolate SAD1-3670 var 2, and Isolate SAG 2;
RA Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
RA Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E.,
RA Cox J.H., Mueller T.;
RT "Complete nucleotide sequencing of SAD derivatives of attenuated rabies
RT virus vaccine strains.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION AT SER-389, AND MUTAGENESIS OF SER-389.
RX PubMed=9882376; DOI=10.1128/jvi.73.2.1661-1664.1999;
RA Yang J., Koprowski H., Dietzschold B., Fu Z.F.;
RT "Phosphorylation of rabies virus nucleoprotein regulates viral RNA
RT transcription and replication by modulating leader RNA encapsidation.";
RL J. Virol. 73:1661-1664(1999).
RN [5]
RP PHOSPHORYLATION AT SER-389, AND MUTAGENESIS OF SER-389.
RX PubMed=11932380; DOI=10.1128/jvi.76.9.4153-4161.2002;
RA Wu X., Gong X., Foley H.D., Schnell M.J., Fu Z.F.;
RT "Both viral transcription and replication are reduced when the rabies virus
RT nucleoprotein is not phosphorylated.";
RL J. Virol. 76:4153-4161(2002).
RN [6]
RP PHOSPHORYLATION AT SER-389 BY HOST CK2.
RX PubMed=12711319; DOI=10.1016/s0006-291x(03)00594-1;
RA Wu X., Lei X., Fu Z.F.;
RT "Rabies virus nucleoprotein is phosphorylated by cellular casein kinase
RT II.";
RL Biochem. Biophys. Res. Commun. 304:333-338(2003).
RN [7]
RP INTERACTION WITH PHOSPHOPROTEIN.
RX PubMed=15557246; DOI=10.1099/vir.0.80325-0;
RA Liu P., Yang J., Wu X., Fu Z.F.;
RT "Interactions amongst rabies virus nucleoprotein, phosphoprotein and
RT genomic RNA in virus-infected and transfected cells.";
RL J. Gen. Virol. 85:3725-3734(2004).
CC -!- FUNCTION: Encapsidates the genome in a ratio of one protein N per nine
CC ribonucleotides, protecting it from nucleases. If expressed without
CC protein P it binds non-specifically RNA and therefore can bind it's own
CC mRNA. Interaction with protein P abolishes any non-specific RNA
CC binding, and prevents phosphorylation. The soluble N-P complex
CC encapsidates specifically the genomic RNA, with protein N protecting
CC the genome like a pearl necklace. The encapsidated genomic RNA is
CC termed the nucleocapsid (NC) and serves as template for viral
CC transcription and replication. Protein N binds protein P in the NC
CC through a different interaction, and can be phosphorylated. Subsequent
CC viral replication is dependent on intracellular concentration of newly
CC synthesized protein N. During replication, encapsidation by protein N
CC is coupled to RNA synthesis and all replicative products are resistant
CC to nucleases.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. In nucleocapsid, binds protein P and thereby positions the
CC polymerase on the template. Protein P acts as a chaperone on free
CC protein N to prevent it from aggregation before encapsidating genomic
CC RNA.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm.
CC -!- PTM: Phosphorylated by host CK2. Unphosphorylated protein N seems to
CC have a better affinity for leader viral promoter encapsidation.
CC Phosphorylation of protein N in ribonucleocapsid may stabilize the
CC interaction with protein P, thereby playing an important role in viral
CC transcription/replication. {ECO:0000269|PubMed:11932380,
CC ECO:0000269|PubMed:12711319, ECO:0000269|PubMed:9882376}.
CC -!- MISCELLANEOUS: Displays a superantigen activity in human and mouse,
CC activating mostly V-beta-8 subtypes of T-cell receptor. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lyssavirus 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; M31046; AAA47199.1; -; Genomic_RNA.
DR EMBL; AF499686; AAT48623.1; -; Genomic_RNA.
DR EMBL; EF206709; ABN11301.1; -; Genomic_RNA.
DR EMBL; EF206716; ABN11336.1; -; Genomic_RNA.
DR EMBL; EF206717; ABN11341.1; -; Genomic_RNA.
DR EMBL; EF206718; ABN11346.1; -; Genomic_RNA.
DR EMBL; EF206719; ABN11351.1; -; Genomic_RNA.
DR PIR; A34746; VHVNSB.
DR SMR; P16285; -.
DR iPTMnet; P16285; -.
DR Proteomes; UP000006363; Genome.
DR Proteomes; UP000007308; Genome.
DR Proteomes; UP000100286; Genome.
DR Proteomes; UP000107382; Genome.
DR Proteomes; UP000118099; Genome.
DR Proteomes; UP000167748; Genome.
DR Proteomes; UP000174835; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3570.10; -; 1.
DR Gene3D; 1.10.3610.10; -; 1.
DR InterPro; IPR000448; Rhabdo_ncapsid.
DR InterPro; IPR023331; Rhabdovirus_ncapsid_C.
DR InterPro; IPR023330; Rhabdovirus_ncapsid_N.
DR InterPro; IPR035961; Rhabdovirus_nucleoprotein-like.
DR Pfam; PF00945; Rhabdo_ncap; 1.
DR SUPFAM; SSF140809; SSF140809; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Helical capsid protein; Host cytoplasm; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Superantigen;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..450
FT /note="Nucleoprotein"
FT /id="PRO_0000222819"
FT MOD_RES 389
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000269|PubMed:11932380,
FT ECO:0000269|PubMed:12711319, ECO:0000269|PubMed:9882376"
FT MUTAGEN 389
FT /note="S->A: Increases leader RNA encapsidation, but
FT decreases viral transcription and replication."
FT /evidence="ECO:0000269|PubMed:11932380,
FT ECO:0000269|PubMed:9882376"
FT MUTAGEN 389
FT /note="S->D: Decreases viral transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:11932380,
FT ECO:0000269|PubMed:9882376"
FT MUTAGEN 389
FT /note="S->E: No effect on viral transcription and
FT replication."
FT /evidence="ECO:0000269|PubMed:11932380,
FT ECO:0000269|PubMed:9882376"
SQ SEQUENCE 450 AA; 50603 MW; 783BF3E01E7BE325 CRC64;
MDADKIVFKV NNQVVSLKPE IIVDQYEYKY PAIKDLKKPC ITLGKAPDLN KAYKSVLSGM
SAAKLNPDDV CSYLAAAMQF FEGTCPEDWT SYGIVIARKG DKITPGSLVE IKRTDVEGNW
ALTGGMELTR DPTVPEHASL VGLLLSLYRL SKISGQNTGN YKTNIADRIE QIFETAPFVK
IVEHHTLMTT HKMCANWSTI PNFRFLAGTY DMFFSRIEHL YSAIRVGTVV TAYEDCSGLV
SFTGFIKQIN LTAREAILYF FHKNFEEEIR RMFEPGQETA VPHSYFIHFR SLGLSGKSPY
SSNAVGHVFN LIHFVGCYMG QVRSLNATVI AACAPHEMSV LGGYLGEEFF GKGTFERRFF
RDEKELQEYE AAELTKTDVA LADDGTVNSD DEDYFSGETR SPEAVYTRIM MNGGRLKRSH
IRRYVSVSSN HQARPNSFAE FLNKTYSSDS
