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P15197 (NCAP_RABVA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Nucleoprotein

Short name=NP
Alternative name(s):
Nucleocapsid protein
Short name=Protein N
Gene names
Name:N
OrganismRabies virus (strain PM1503/AVO1) (RABV) [Complete proteome]
Taxonomic identifier11293 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesMononegaviralesRhabdoviridaeLyssavirus
Virus hostHomo sapiens (Human) [TaxID: 9606]
Mammalia [TaxID: 40674]

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases By similarity.

Subunit structure

Homomultimerizes to form the nucleocapsid. Binds to viral genomic RNA. In nucleocapsid, binds protein P and thereby positions the polymerase on the template. Protein P acts as a chaperone on free protein N to prevent it from aggregation before encapsidating genomic RNA By similarity.

Subcellular location

Virion. Host cytoplasm By similarity.

Post-translational modification

Phosphorylated by host CK2. Unphosphorylated protein N seems to have a better affinity for leader viral promoter encapsidation. Phosphorylation of protein N in ribonucleocapsid may stabilize the interaction with protein P, thereby playing an important role in viral transcription/replication By similarity.

Miscellaneous

Displays a superantigen activity in human and mouse, activating mostly V-beta-8 subtypes of T-cell receptor By similarity.

Sequence similarities

Belongs to the lyssavirus nucleocapsid protein family.

Ontologies

Keywords
   Cellular componentHost cytoplasm
Virion
   LigandRNA-binding
Viral nucleoprotein
   Molecular functionRibonucleoprotein
Superantigen
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

viral nucleocapsid

Inferred from electronic annotation. Source: InterPro

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Nucleoprotein
PRO_0000222816

Amino acid modifications

Modified residue3891Phosphoserine; by host CK2 By similarity

Natural variations

Natural variant3771T → S in strain: Isolate AVO1.

Sequences

Sequence LengthMass (Da)Tools
P15197 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 004FE0FC57ED8176

FASTA45050,748
        10         20         30         40         50         60 
MDADKIVFKV NNQVVSLKPE IIVDQYEYKY PAIKDLKKPC ITLGKAPDLN KAYKSVLSGM 

        70         80         90        100        110        120 
NAAKLDPDDV CSYLAAAMQF FEGTCPEDWT SYGILIARKG DRITPNSLVE IKRTDVEGNW 

       130        140        150        160        170        180 
ALTGGMELTR DPTVSEHASL VGLLLSLYRL SKISGQNTGN YKTNIADRIE QIFETAPFVK 

       190        200        210        220        230        240 
IVEHHTLMTT HKMCANWSTI PNFRFLAGTY DMFFSRIEHL YSAIRVGTVV TAYEDCSGLV 

       250        260        270        280        290        300 
SFTGFIKQIN LTAREAILYF FHKNFEEEIR RMFEPGQETA VPHSYFIHFR SLGLSGKSPY 

       310        320        330        340        350        360 
SSNAVGHVFN LIHFVGCYMG QVRSLNATVI AACAPHEMSV LGGYLGEEFF GKGTFERRFF 

       370        380        390        400        410        420 
RDEKELQEYE AAELTKTDVA LADDGTVNSD DEDYFSGETR SPEAVYTRIM MNGGRLKRSH 

       430        440        450 
IRRYVSVSSN HQARPNSFAE FLNKTYSNDS 

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References

[1]"Sequence of the 3386 3' nucleotides of the genome of the AVO1 strain rabies virus: structural similarities in the protein regions involved in transcription."
Poch O., Tordo N., Keith G.
Biochimie 70:1019-1029(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate AVO1.
[2]"Characterization of rabies virus vaccine strains."
Stallkamp I., Lopez-Yomayuza C.C., Thiel H.-J.
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate PM1503.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13357 Genomic RNA. Translation: CAA31733.1.
DQ099525 Genomic RNA. Translation: AAZ07891.1.
PIRVHVNAV. S07813.

3D structure databases

ProteinModelPortalP15197.
SMRP15197. Positions 5-448.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.3570.10. 1 hit.
1.10.3610.10. 1 hit.
InterProIPR000448. Rhabdo_ncapsid.
IPR023331. Rhabdovirus_ncapsid_C.
IPR023330. Rhabdovirus_ncapsid_N.
[Graphical view]
PfamPF00945. Rhabdo_ncap. 1 hit.
[Graphical view]
ProDomPD002087. Rhabd_nucleocap. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF140809. SSF140809. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNCAP_RABVA
AccessionPrimary (citable) accession number: P15197
Secondary accession number(s): Q4F903
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 10, 2007
Last modified: April 3, 2013
This is version 52 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families