ID   NCAP_RABVH              Reviewed;         450 AA.
AC   Q8B6J9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   23-FEB-2022, entry version 68.
DE   RecName: Full=Nucleoprotein;
DE            Short=NP;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=N;
OS   Rabies virus (strain HEP-Flury) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=11296;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12505638; DOI=10.1016/s0166-0934(02)00249-5;
RA   Inoue K., Shoji Y., Kurane I., Iijima T., Sakai T., Morimoto K.;
RT   "An improved method for recovering rabies virus from cloned cDNA.";
RL   J. Virol. Methods 107:229-236(2003).
RN   [2]
RP   INTERACTION WITH PROTEIN P.
RX   PubMed=15215627; DOI=10.1111/j.1348-0421.2004.tb03529.x;
RA   Toriumi H., Kawai A.;
RT   "Association of rabies virus nominal phosphoprotein (P) with viral
RT   nucleocapsid (NC) is enhanced by phosphorylation of the viral nucleoprotein
RT   (N).";
RL   Microbiol. Immunol. 48:399-409(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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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}.
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DR   EMBL; AB085828; BAC53865.1; -; Genomic_RNA.
DR   SMR; Q8B6J9; -.
DR   Proteomes; UP000006846; 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   Ribonucleoprotein; RNA-binding; Superantigen; Viral nucleoprotein; Virion.
FT   CHAIN           1..450
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000295210"
FT   MOD_RES         389
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  50722 MW;  19EB82EC3B9A19B4 CRC64;
     MDADKIVFKV NNRVVSLKPE IIVDQYEYKY PAIKDLKKPC ITLGKAPDLN KAYKSVLSGM
     NAAKLDPDDV CSYLAAAMQF FEGTCPEDWT SYGILIARKG DKITPDSLVE IKRTDVEGNW
     ALTGGMELTR DPTVSEHASL 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