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P15682 (NCAP_I33A0) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleoprotein
Alternative name(s):
Nucleocapsid protein
Short name=Protein N
Gene names
Name:NP
OrganismInfluenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) [Complete proteome]
Taxonomic identifier381518 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus By similarity. Ref.3

Subunit structure

Homomultimerizes to form the nucleocapsid. May bind human exportin-1. Binds to viral genomic RNA. Protein-RNA contacts are mediated by a combination of electrostatic interactions between positively charged residues and the phosphate backbone and planar interactions between aromatic side chains and bases By similarity.

Subcellular location

Virion Potential. Host nucleus.

Post-translational modification

Late in virus-infected cells, may be cleaved from a 56-kDa protein to a 53-kDa protein by a cellular caspase. This cleavage might be a marker for the onset of apoptosis in infected cells or have a specific function in virus host interaction. Ref.2

Sequence similarities

Belongs to the influenza viruses nucleoprotein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Nucleoprotein
PRO_0000079113

Regions

Motif1 – 1818Unconventional nuclear localization signal By similarity
Motif198 – 21619Bipartite nuclear localization signal By similarity

Secondary structure

...................................................................... 498
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15682 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 27AA1703050AA877

FASTA49856,244
        10         20         30         40         50         60 
MATKGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS DYEGRLIQNS 

        70         80         90        100        110        120 
LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV DGKWMRELIL YDKEEIRRIW 

       130        140        150        160        170        180 
RQANNGDDAT AGLTHMMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG 

       190        200        210        220        230        240 
AAVKGVGTMV MELIRMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRAMVD 

       250        260        270        280        290        300 
QVRESRNPGN AEFEDLIFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG 

       310        320        330        340        350        360 
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT KVVPRGKLST 

       370        380        390        400        410        420 
RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR ASSGQISIQP TFSVQRNLPF 

       430        440        450        460        470        480 
DRPTIMAAFT GNTEGRTSDM RTEIIRLMES ARPEDVSFQG RGVFELSDEK AASPIVPSFD 

       490 
MSNEGSYFFG DNAEEYDN 

« Hide

References

[1]"Evolution of the nucleoprotein gene of influenza A virus."
Gorman O.T., Bean W.J., Kawaoka Y., Webster R.G.
J. Virol. 64:1487-1497(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Caspase-dependent N-terminal cleavage of influenza virus nucleocapsid protein in infected cells."
Zhirnov O.P., Konakova T.E., Garten W., Klenk H.
J. Virol. 73:10158-10163(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE.
[3]"An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein."
Cros J.F., Garcia-Sastre A., Palese P.
Traffic 6:205-213(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30746 Genomic RNA. Translation: AAA43452.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZDPX-ray2.69A/B/C1-498[»]
4BBLelectron microscopy18.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X8-498[»]
4IRYX-ray2.80A/B1-401[»]
A/B430-498[»]
ProteinModelPortalP15682.
SMRP15682. Positions 22-496.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002141. Flu_NP.
[Graphical view]
PfamPF00506. Flu_NP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNCAP_I33A0
AccessionPrimary (citable) accession number: P15682
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 60 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references