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P03466 (NCAP_I34A1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. 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·Interactions·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/Puerto Rico/8/1934 H1N1) [Reference proteome]
Taxonomic identifier211044 [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.

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. Ref.10 Ref.12

Subcellular location

Virion Potential. Host nucleus Ref.8 Ref.9.

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.

Ontologies

Keywords
   Biological processHost-virus interaction
Viral penetration into host nucleus
Virus entry into host cell
   Cellular componentCapsid protein
Helical capsid protein
Host nucleus
Virion
   LigandRNA-binding
Viral nucleoprotein
   Molecular functionRibonucleoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfusion of virus membrane with host plasma membrane

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

receptor-mediated endocytosis of virus by host cell

Traceable author statement. Source: Reactome

uncoating of virus

Traceable author statement. Source: Reactome

viral entry into host cell

Traceable author statement. Source: Reactome

viral genome maturation

Traceable author statement. Source: Reactome

viral genome packaging

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral penetration into host nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Traceable author statement. Source: Reactome

viral release from host cell

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

cytosol

Traceable author statement. Source: Reactome

endosome lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

helical viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

ribonucleoprotein complex

Inferred from electronic annotation. Source: UniProtKB-KW

viral nucleocapsid

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 17022977PubMed 20064372. Source: IntAct

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MP034852EBI-2547640,EBI-2547543

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Nucleoprotein
PRO_0000079092

Regions

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

Experimental info

Mutagenesis81R → A: No effect on RNA-binding activity. Ref.11
Mutagenesis1041W → A: No effect on RNA-binding activity. Ref.11
Mutagenesis1201W → A: Partial loss of RNA-binding activity. Ref.11
Mutagenesis1391W → A: Partial loss of RNA-binding activity. Ref.11
Mutagenesis1481Y → A: No effect on RNA-binding activity. Ref.11
Mutagenesis1501R → A: No effect on RNA-binding activity. Ref.11
Mutagenesis1561R → A: No effect on RNA-binding activity. Ref.11
Mutagenesis1751R → A: No effect on RNA-binding activity. Ref.11
Mutagenesis1991R → A: 60% loss of Homomultimerization affinity. No effect on RNA-binding activity. Ref.10 Ref.11
Mutagenesis2041R → A: No effect on RNA-binding activity. Ref.11
Mutagenesis2071W → A: No effect on RNA-binding activity. Ref.11
Mutagenesis2081R → A: No effect on RNA-binding activity. Ref.11
Mutagenesis2131R → A: No effect on RNA-binding activity. Ref.11
Mutagenesis2671R → A: Complete loss of RNA-binding activity. Ref.11
Mutagenesis3301W → A: Complete loss of RNA-binding activity. Ref.11
Mutagenesis3861W → A: No effect on RNA-binding activity. Ref.11
Mutagenesis3911R → A: No effect on RNA-binding activity. Ref.11
Mutagenesis4121F → A: Complete loss of RNA-binding activity. Ref.11
Mutagenesis4161R → A: Complete loss of Homomultimerization. Complete loss of RNA-binding activity. Ref.10 Ref.11
Mutagenesis4791F → A: 2-fold increase of self association. Ref.10
Sequence conflict1351H → N in CAA24268. Ref.1
Sequence conflict2471N → D in CAA24268. Ref.1
Sequence conflict3531L → V in CAA24268. Ref.1
Sequence conflict4251I → V in CAA24268. Ref.1
Sequence conflict4301N → T in CAA24268. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P03466 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: 4F750FEF05D6E668

FASTA49856,210
        10         20         30         40         50         60 
MASQGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS DYEGRLIQNS 

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

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

       190        200        210        220        230        240 
AAVKGVGTMV MELVRMIKRG INDRNFWRGE NGRKTRIAYE RMCNILKGKF QTAAQKAMMD 

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

       310        320        330        340        350        360 
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVLSFIKGT KVLPRGKLST 

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

       430        440        450        460        470        480 
DRTTIMAAFN GNTEGRTSDM RTEIIRMMES ARPEDVSFQG RGVFELSDEK AASPIVPSFD 

       490 
MSNEGSYFFG DNAEEYDN 

« Hide

References

[1]"The structure of the gene encoding the nucleoprotein of human influenza virus A/PR/8/34."
Winter G., Fields S.
Virology 114:423-428(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Complete nucleotide sequence of the nucleoprotein gene from the human influenza strain A/PR/8/34 (HON1)."
van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.
Eur. J. Biochem. 116:347-353(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]Erratum
van Rompuy L., Min Jou W., Huylebroeck D., Devos R., Fiers W.
Eur. J. Biochem. 116:645-645(1981)
Cited for: SEQUENCE REVISION.
[4]"Plasmid-only rescue of influenza A virus vaccine candidates."
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L., Garcia-Sastre A., Palese P.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[5]"Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments."
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., Osterhaus A.D.M.E., Fouchier R.A.M.
Virus Res. 103:155-161(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], REVERSE GENETICS.
[6]"Fluorescent antigen-transfected target cell cytotoxic T lymphocyte assay for ex vivo detection of antigen-specific cell-mediated cytotoxicity."
van Baalen C.A., Kwa D., Verschuren E.J., Reedijk M.L., Boon A.C., de Mutsert G., Rimmelzwaan G.F., Osterhaus A.D., Gruters R.A.
J. Infect. Dis. 192:1183-1190(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[7]"The NIAID influenza genome sequencing project."
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y. expand/collapse author list , Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[8]"A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins."
Weber F., Kochs G., Gruber S., Haller O.
Virology 250:9-18(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments."
Digard P., Elton D., Bishop K., Medcalf E., Weeds A., Pope B.
J. Virol. 73:2222-2231(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elements."
Elton D., Medcalf E., Bishop K., Digard P.
Virology 260:190-200(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, MUTAGENESIS OF ARG-199; ARG-416 AND PHE-479.
[11]"Identification of amino acid residues of influenza virus nucleoprotein essential for RNA binding."
Elton D., Medcalf L., Bishop K., Harrison D., Digard P.
J. Virol. 73:7357-7367(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, MUTAGENESIS OF ARG-8; TRP-104; TRP-120; TRP-139; TYR-148; ARG-150; ARG-156; ARG-175; ARG-199; ARG-204; TRP-207; ARG-208; ARG-213; ARG-267; TRP-330; TRP-386; ARG-391; PHE-412 AND ARG-416.
[12]"Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway."
Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R., McCauley J., Digard P.
J. Virol. 75:408-419(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN XPO1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01084 Genomic RNA. Translation: CAA24268.1.
J02147 Genomic RNA. Translation: AAA43467.1.
AF389119 Genomic RNA. Translation: AAM75159.1.
EF467822 Genomic RNA. Translation: ABO21710.1.
AY936882 Genomic RNA. Translation: AAX39501.1.
CY009447 Genomic RNA. Translation: ABD77679.1.
RefSeqNP_040982.1. NC_002019.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BSTX-ray2.10C383-391[»]
2WFSelectron microscopy12.00A/B/C/D/E/F/G/H/I8-498[»]
4NQVX-ray2.39M/N/O/P/Q/R44-52[»]
ProteinModelPortalP03466.
SMRP03466. Positions 22-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP03466. 20 interactions.
MINTMINT-3375097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID956531.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Family and domain databases

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

Other

EvolutionaryTraceP03466.

Entry information

Entry nameNCAP_I34A1
AccessionPrimary (citable) accession number: P03466
Secondary accession number(s): Q20N34 expand/collapse secondary AC list , Q58NB3, Q67228, Q80AB4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 11, 2007
Last modified: June 11, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references