ID   NCAP_RABVD              Reviewed;         450 AA.
AC   Q0GBX9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   23-FEB-2022, entry version 57.
DE   RecName: Full=Nucleoprotein;
DE            Short=NP;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=N;
OS   Rabies virus (strain China/DRV) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=445792;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Zhao Y.J., Guo L., Huang Y., Qian A.D.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ875051; ABI47942.1; -; Genomic_RNA.
DR   SMR; Q0GBX9; -.
DR   Proteomes; UP000008618; 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   3: Inferred from homology;
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_0000295208"
FT   MOD_RES         389
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  50838 MW;  B5203FDCADB365B0 CRC64;
     MDADKIVFKV NNQVVSLKPE IIVDQYEYKY PAIKDLKKPC ITLGKAPDLN KAYKSALSSM
     NAVKLDPDDD CSYLAAAMEF FEGTCPEDWT SYGMLIARNR DKITPYSLVE IKRTDVEGNW
     ALTGGMEMTR DPTGSEHTSL VGLLVSLYRL SKISGQNTGN YKTNIADRIE QIFETAPFVK
     LVEHHTLMTT HKMCANWNTI PNFRVLAGTY DLFFSRIEHL YSAIRVGTVV TAYEDCSGLV
     SFTGFIKQIN LTAREAILYF FHKNFEEEIR RMLEGRQETA VPHSYFIHFR SLGLSGKSPY
     SSNAVGHLFN LIHFVGCYMG QIRSLNSTVI AACAPHEMSV LGGYLGDEFF GRGTFERRFF
     RDEKELQEYE AAELTKTDVA LADDGTVNSD DEDYFSGEAR GPEAVYARIM MNGGRLKRSH
     IRRYVSVSSN HQARPNSFAE FLNKTYSSDS