ID   NCAP_VSNJO              Reviewed;         422 AA.
AC   P04881;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Nucleoprotein;
DE            Short=NP;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=N;
OS   Vesicular stomatitis New Jersey virus (strain Ogden subtype Concan)
OS   (VSNJV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=11283;
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=58271; Culicoides.
OH   NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=252607; Lutzomyia.
OH   NCBI_TaxID=7370; Musca domestica (House fly).
OH   NCBI_TaxID=7190; Simuliidae (black flies).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6091339; DOI=10.1016/0042-6822(84)90237-x;
RA   Banerjee A.K., Rhodes D.P., Gill D.S.;
RT   "Complete nucleotide sequence of the mRNA coding for the N protein of
RT   vesicular stomatitis virus (New Jersey serotype).";
RL   Virology 137:432-438(1984).
RN   [2]
RP   MUTAGENESIS OF 418-VAL--PHE-420 AND 421-ASP-LYS-422.
RX   PubMed=10364506; DOI=10.1006/viro.1999.9768;
RA   Das T., Chakrabarti B.K., Chattopadhyay D., Banerjee A.K.;
RT   "Carboxy-terminal five amino acids of the nucleocapsid protein of vesicular
RT   stomatitis virus are required for encapsidation and replication of genome
RT   RNA.";
RL   Virology 259:219-227(1999).
RN   [3]
RP   FUNCTION.
RX   PubMed=16775325; DOI=10.1128/jvi.00211-06;
RA   Das S.C., Nayak D., Zhou Y., Pattnaik A.K.;
RT   "Visualization of intracellular transport of vesicular stomatitis virus
RT   nucleocapsids in living cells.";
RL   J. Virol. 80:6368-6377(2006).
CC   -!- FUNCTION: Encapsidates the genome in a ratio of one N per nine
CC       ribonucleotides, protecting it from nucleases. The encapsidated genomic
CC       RNA is termed the NC and serves as template for transcription and
CC       replication. Replication is dependent on intracellular concentration of
CC       newly synthesized N, termed N(0), which corresponds to the protein not
CC       associated with RNA. In contrast, when associated with RNA, it is
CC       termed N. During replication, encapsidation by N(0) is coupled to RNA
CC       synthesis and all replicative products are resistant to nucleases (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:16775325}.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC       genomic RNA. N in nucleocapsid binds the P protein and thereby
CC       positions the polymerase on the template. Interaction of N(0) with the
CC       P protein prevents the uncontrolled aggregation of N(0) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm. Note=The nucleocapsid is
CC       synthesized in the cytoplasm, and is subsequently transported via
CC       microtubules to the cell periphery.
CC   -!- SIMILARITY: Belongs to the vesiculovirus nucleocapsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; K02379; AAA48449.1; -; mRNA.
DR   SMR; P04881; -.
DR   PRIDE; P04881; -.
DR   Proteomes; UP000007626; 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; Ribonucleoprotein;
KW   RNA-binding; Viral nucleoprotein; Virion.
FT   CHAIN           1..422
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000222822"
FT   MUTAGEN         418..420
FT                   /note="VEF->AAA: Complete loss of leader encapsidation."
FT                   /evidence="ECO:0000269|PubMed:10364506"
FT   MUTAGEN         421..422
FT                   /note="DK->AA: Complete loss of leader encapsidation."
FT                   /evidence="ECO:0000269|PubMed:10364506"
FT   MUTAGEN         422
FT                   /note="K->A,R: No effect on leader encapsidation."
FT   MUTAGEN         422
FT                   /note="K->D,I: Complete loss of leader encapsidation."
SQ   SEQUENCE   422 AA;  47884 MW;  DE62095B11CD3AF0 CRC64;
     MAPTVKRIIN DSIIQPKLPA NEDPVEYPAD YFKNNTNIVL YVSTKVALND LRAYVYQGIK
     SGNPSILHIN AYLYAALKGV EGTLDRDWVS FGRTIGKREE NVKIFDLVKV EELKTALPDG
     KSDPDRSAED DKWLPIYILG LYRVGRSKVT DYRKKLLDGL ENQCRVASTR FESLVEDGLD
     FFDIWENDPN FTKIVAAVDM FFHMFKKHER APIRYGTIVS RFKDCAALAT FGHLSKVSGL
     SIEDLTTWVL NREVADELCQ MMYPGQEIDK ADSYMPYMID FGLSQKSPYS SVKNPAFHFW
     GQLAALLLRS TRAKNARQPD DIEYTSLTCA SLLLSFAVGS SADIEQQFYI GEDKYTTEKD
     DSLKKSDVPP KGRNVVDWLG WYDDNGGKPT PDMLNFARRA VSSLQSLREK TIGKYAKVEF
     DK