NCAP_RABVA
ID NCAP_RABVA Reviewed; 450 AA.
AC P15197; Q4F903;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 23-FEB-2022, entry version 82.
DE RecName: Full=Nucleoprotein;
DE Short=NP;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Rabies virus (strain PM1503/AVO1) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11293;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate AVO1;
RX PubMed=3147698; DOI=10.1016/0300-9084(88)90265-9;
RA Poch O., Tordo N., Keith G.;
RT "Sequence of the 3386 3' nucleotides of the genome of the AVO1 strain
RT rabies virus: structural similarities in the protein regions involved in
RT transcription.";
RL Biochimie 70:1019-1029(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate PM1503;
RA Stallkamp I., Lopez-Yomayuza C.C., Thiel H.-J.;
RT "Characterization of rabies virus vaccine strains.";
RL Submitted (JUN-2005) 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; X13357; CAA31733.1; -; Genomic_RNA.
DR EMBL; DQ099525; AAZ07891.1; -; Genomic_RNA.
DR PIR; S07813; VHVNAV.
DR SMR; P15197; -.
DR Proteomes; UP000008617; 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_0000222816"
FT MOD_RES 389
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
FT VARIANT 377
FT /note="T -> S (in strain: Isolate AVO1)"
SQ SEQUENCE 450 AA; 50748 MW; 004FE0FC57ED8176 CRC64;
MDADKIVFKV NNQVVSLKPE IIVDQYEYKY PAIKDLKKPC ITLGKAPDLN KAYKSVLSGM
NAAKLDPDDV CSYLAAAMQF FEGTCPEDWT SYGILIARKG DRITPNSLVE 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 FLNKTYSNDS