NCAP_RABVE
ID NCAP_RABVE Reviewed; 450 AA.
AC P0DOF3; Q7TBN9;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 29-SEP-2021, entry version 24.
DE RecName: Full=Nucleoprotein;
DE Short=NP;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Rabies virus (strain ERA) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11295;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=CVS-2003;
RX PubMed=12970438; DOI=10.1128/jvi.77.19.10537-10547.2003;
RA Prehaud C., Lay S., Dietzschold B., Lafon M.;
RT "Glycoprotein of nonpathogenic rabies viruses is a key determinant of human
RT cell apoptosis.";
RL J. Virol. 77:10537-10547(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=CVS-2001;
RA Prehaud C.J., Lay S.J.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=ERA;
RA Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
RA Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E.,
RA Cox J., Mueller T.;
RT "Complete nucleotide sequencing of SAD derivatives of attenuated rabies
RT virus vaccine strains.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS).
RX PubMed=16778023; DOI=10.1126/science.1125280;
RA Albertini A.A., Wernimont A.K., Muziol T., Ravelli R.B., Clapier C.R.,
RA Schoehn G., Weissenhorn W., Ruigrok R.W.;
RT "Crystal structure of the rabies virus nucleoprotein-RNA complex.";
RL Science 313:360-363(2006).
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; AF406696; AAP81753.1; -; Genomic_RNA.
DR EMBL; EF206707; ABN11291.1; -; Genomic_RNA.
DR PDB; 2GTT; X-ray; 3.49 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-450.
DR PDBsum; 2GTT; -.
DR SMR; P0DOF3; -.
DR Proteomes; UP000008619; 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 3D-structure; Capsid protein; Helical capsid protein; Host cytoplasm;
KW Phosphoprotein; Ribonucleoprotein; RNA-binding; Superantigen;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..450
FT /note="Nucleoprotein"
FT /id="PRO_0000295209"
FT MOD_RES 389
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:2GTT"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2GTT"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 134..152
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:2GTT"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:2GTT"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2GTT"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:2GTT"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:2GTT"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:2GTT"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:2GTT"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:2GTT"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 335..349
FT /evidence="ECO:0007829|PDB:2GTT"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 363..370
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 402..410
FT /evidence="ECO:0007829|PDB:2GTT"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:2GTT"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:2GTT"
SQ SEQUENCE 450 AA; 50578 MW; 6B5A4419AAFCEE04 CRC64;
MDADKIVFKV NNQVVSLKPE IIVDQHEYKY PAIKDLKKPC ITLGKAPDLN KAYKSVLSGM
SAAKLDPDDV CSYLAAAMQF FEGTCPEDWT SYGIVIARKG DKITPGSLVE IKRTDVEGNW
ALTGGMELTR DPTVPEHASL 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 FLNKTYSSDS