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P26087 (NCAP_I81A4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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/Swine/Ontario/2/1981 H1N1)
Taxonomic identifier384501 [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 existenceInferred from homology

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.

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 By similarity.

Sequence similarities

Belongs to the influenza viruses nucleoprotein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Nucleoprotein
PRO_0000079135

Regions

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

Sequences

Sequence LengthMass (Da)Tools
P26087 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 94237149AC015D83

FASTA49856,043
        10         20         30         40         50         60 
MASQGTKRSY EQMETGGERQ DATEIRASVG RMIGGIGRFY IQMCTELKLS DYEGRLIQNS 

        70         80         90        100        110        120 
ITIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV DGKWMRELIL YDKEEIRRVW 

       130        140        150        160        170        180 
RQANNGEDAT AGLTHIMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG 

       190        200        210        220        230        240 
AAVKGVGTIA MELIRMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRAMMD 

       250        260        270        280        290        300 
QVRESRNPGN AEIEDLIFLA RSALILRGSV AHKSCLPACV YGLAVASGHD FEREGYSLVG 

       310        320        330        340        350        360 
IDPFKLLQNS QVFSLIRPNE NPAHKSQLVW MACHSAAFED LRVSGFIRGK KVVPRGKLST 

       370        380        390        400        410        420 
RGVQIASNEN VEAMDSSTLE LRSRYWAIRT RSGGNTNQQK ASAGQISVQP TFSVQRNLPF 

       430        440        450        460        470        480 
ERATVMAAFI GNNEGRTSDM RIEIIRMMES AKPEDLSFQG RGVFELSDEK ATNPIVPSFD 

       490 
MNNEGSYFFG DNAEEYDN 

« Hide

References

[1]"Evolution of influenza A virus nucleoprotein genes: implications for the origins of H1N1 human and classical swine viruses."
Gorman O.T., Bean W.J., Kawaoka Y., Donatelli I., Guo Y., Webster R.G.
J. Virol. 65:3704-3714(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63767 Genomic RNA. Translation: AAA52266.1.

3D structure databases

ProteinModelPortalP26087.
SMRP26087. 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_I81A4
AccessionPrimary (citable) accession number: P26087
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: February 19, 2014
This is version 51 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