NCAP_ABLVH
ID NCAP_ABLVH Reviewed; 450 AA.
AC Q8JTH3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Nucleoprotein;
DE Short=NP;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Australian bat lyssavirus (isolate Human/AUS/1998) (ABLV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=446562;
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=12083841; DOI=10.1006/viro.2002.1417;
RA Warrilow D., Smith I.L., Harrower B., Smith G.A.;
RT "Sequence analysis of an isolate from a fatal human infection of Australian
RT bat lyssavirus.";
RL Virology 297:109-119(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; AF418014; AAN05306.1; -; Genomic_RNA.
DR SMR; Q8JTH3; -.
DR Proteomes; UP000006884; 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_0000295201"
FT MOD_RES 389
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 50645 MW; 1005D4E71E17E942 CRC64;
MDSDKIVFKV NNQLVSVKPE VIVDQYEYKY PAIKDQKKPS ITLGKAPDLN KAYKSILSGM
NAAKLDPDDV CSYLAAAMEL FEGVCPEDWT SYGILIARKG DKITPATLVD IKRTDIEGNW
ALTGGQDLTR DPTVAEHASL VGLLLSLYRL SKISGQNTGN YKTNIADRIE QIFETAPFAK
IVEHHTLMTT HKMCANWSTI PNFRFLAGTY DMFFSRVEHL YSAIRVGTVV TAYEDCSGLV
SFTGFIKQIN LTAREAILYF FHKNFEEEIR RMFEPGQETA VPHSYFIHFR SLGLSGKSPY
SSNAVGHVFN LIHFVGCYMG QIRSLNATVI STCAPHEMSV LGGYLGEEFF GKGTFERRFF
RNEKELQDYE AAESMKTDIA LADDATVNSD DEDYFSGETR GPEAVYTRIM MNGGRLKRSH
IRRYISVSSN HQSRPNSFAE FLNKTYSSDS