ID   NCAP_ABLVB              Reviewed;         450 AA.
AC   Q9QSP4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   23-FEB-2022, entry version 72.
DE   RecName: Full=Nucleoprotein;
DE            Short=NP;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=N;
OS   Australian bat lyssavirus (isolate Bat/AUS/1996) (ABLV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=446561;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH   NCBI_TaxID=328804; Pteropus conspicillatus (Spectacled flying fox).
OH   NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH   NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
OH   NCBI_TaxID=446909; Saccolaimus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12367747; DOI=10.1016/s0168-1702(02)00056-4;
RA   Gould A.R., Kattenbelt J.A., Gumley S.G., Lunt R.A.;
RT   "Characterisation of an Australian bat lyssavirus variant isolated from an
RT   insectivorous bat.";
RL   Virus Res. 89:1-28(2002).
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; AF081020; AAD47896.1; -; Genomic_RNA.
DR   RefSeq; NP_478339.1; NC_003243.1.
DR   SMR; Q9QSP4; -.
DR   GeneID; 926728; -.
DR   KEGG; vg:926728; -.
DR   Proteomes; UP000006934; 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   Reference proteome; Ribonucleoprotein; RNA-binding; Superantigen;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..450
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000295200"
FT   MOD_RES         389
FT                   /note="Phosphoserine; by host CK2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   450 AA;  50705 MW;  76B7E64FFA10CEC8 CRC64;
     MESDKIAFKI NNQLVSVKPE VIVDQYEYKY PAIKDQRKPS ITLGKAPDLN KAYKSILSGM
     NAAKLDPDDV CSYLAAAMEL FEGICPEDWT SYGILIARKG DKITPATLVD IRRTDIQGSW
     ALAGGQDFTR DPTIAEHASL VGLLLSLYRL SKISGQNTGN YKTNIADRIE QIFETAPFAK
     IVEHHTLMTT HKMCANWSTI PNFRFLAGTY DMFFSRVEHL YSAIRVGTVV TAYEDCSGLV
     SFTGFIKQIN LTAREAILYF FHKNFEEEIR RMFEPGQETA VPHSYFIHFR SLGLSGKSPY
     SSNAVGHVFN LIHFVGCYMG QIRSLNATVI STCAPHEMSV LGGYLGEEFF GKGTFERRFF
     RDEKELQDYE AAEAMKIDLA LADDGTVNSY DEDYLSGETR SPEAVYTRIM MNGGRLKKSH
     IRRYISVSSN HQSRPNSFAE FLNKTYSSDS