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P03466

- NCAP_I34A1

UniProt

P03466 - NCAP_I34A1

Protein

Nucleoprotein

Gene

NP

Organism
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA binding Source: UniProtKB-KW
    3. structural molecule activity Source: InterPro

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: Reactome
    2. intracellular transport of virus Source: Reactome
    3. receptor-mediated endocytosis of virus by host cell Source: Reactome
    4. uncoating of virus Source: Reactome
    5. viral entry into host cell Source: Reactome
    6. viral genome maturation Source: Reactome
    7. viral genome packaging Source: Reactome
    8. viral life cycle Source: Reactome
    9. viral penetration into host nucleus Source: UniProtKB-KW
    10. viral process Source: Reactome
    11. viral release from host cell Source: Reactome
    12. viral transcription Source: Reactome
    13. virion assembly Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    Host-virus interaction, Viral penetration into host nucleus, Virus entry into host cell

    Keywords - Ligandi

    RNA-binding, Viral nucleoprotein

    Enzyme and pathway databases

    ReactomeiREACT_6145. Influenza Life Cycle.
    REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
    REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
    REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.
    REACT_6212. Budding.
    REACT_6235. Packaging of Eight RNA Segments.
    REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
    REACT_6277. Assembly of Viral Components at the Budding Site.
    REACT_6321. Uncoating of the Influenza Virion.
    REACT_6326. Release.
    REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
    REACT_6354. Viral Messenger RNA Synthesis.
    REACT_9434. vRNP Assembly.
    REACT_9491. Viral mRNA Translation.
    REACT_9497. vRNA Synthesis.
    REACT_9527. cRNA Synthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoprotein
    Alternative name(s):
    Nucleocapsid protein
    Short name:
    Protein N
    Gene namesi
    Name:NP
    OrganismiInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1)
    Taxonomic identifieri211044 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]
    Sus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000009255: Genome

    Subcellular locationi

    Virion Curated. Host nucleus 2 Publications

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endosome lumen Source: Reactome
    3. extracellular region Source: Reactome
    4. Golgi membrane Source: Reactome
    5. helical viral capsid Source: UniProtKB-KW
    6. host cell nucleus Source: UniProtKB-SubCell
    7. nucleoplasm Source: Reactome
    8. plasma membrane Source: Reactome
    9. ribonucleoprotein complex Source: UniProtKB-KW
    10. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Helical capsid protein, Host nucleus, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81R → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi104 – 1041W → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi120 – 1201W → A: Partial loss of RNA-binding activity. 1 Publication
    Mutagenesisi139 – 1391W → A: Partial loss of RNA-binding activity. 1 Publication
    Mutagenesisi148 – 1481Y → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi150 – 1501R → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi156 – 1561R → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi175 – 1751R → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi199 – 1991R → A: 60% loss of Homomultimerization affinity. No effect on RNA-binding activity. 2 Publications
    Mutagenesisi204 – 2041R → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi207 – 2071W → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi208 – 2081R → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi213 – 2131R → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi267 – 2671R → A: Complete loss of RNA-binding activity. 1 Publication
    Mutagenesisi330 – 3301W → A: Complete loss of RNA-binding activity. 1 Publication
    Mutagenesisi386 – 3861W → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi391 – 3911R → A: No effect on RNA-binding activity. 1 Publication
    Mutagenesisi412 – 4121F → A: Complete loss of RNA-binding activity. 1 Publication
    Mutagenesisi416 – 4161R → A: Complete loss of Homomultimerization. Complete loss of RNA-binding activity. 2 Publications
    Mutagenesisi479 – 4791F → A: 2-fold increase of self association. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498NucleoproteinPRO_0000079092Add
    BLAST

    Post-translational modificationi

    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.By similarity

    Interactioni

    Subunit structurei

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTN4O437072EBI-2547640,EBI-351526From a different organism.
    MP034852EBI-2547640,EBI-2547543

    Protein-protein interaction databases

    IntActiP03466. 21 interactions.
    MINTiMINT-3375097.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP03466.
    SMRiP03466. Positions 22-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03466.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1 – 1818Unconventional nuclear localization signalAdd
    BLAST
    Motifi198 – 21619Bipartite nuclear localization signalAdd
    BLAST

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR002141. Flu_NP.
    [Graphical view]
    PfamiPF00506. Flu_NP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P03466-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASQGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS    50
    DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV 100
    NGKWMRELIL YDKEEIRRIW RQANNGDDAT AGLTHMMIWH SNLNDATYQR 150
    TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELVRMIKRG 200
    INDRNFWRGE NGRKTRIAYE RMCNILKGKF QTAAQKAMMD QVRESRNPGN 250
    AEFEDLTFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG 300
    IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVLSFIKGT 350
    KVLPRGKLST RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR 400
    ASAGQISIQP TFSVQRNLPF DRTTIMAAFN GNTEGRTSDM RTEIIRMMES 450
    ARPEDVSFQG RGVFELSDEK AASPIVPSFD MSNEGSYFFG DNAEEYDN 498
    Length:498
    Mass (Da):56,210
    Last modified:September 11, 2007 - v2
    Checksum:i4F750FEF05D6E668
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti135 – 1351H → N in CAA24268. (PubMed:7292985)Curated
    Sequence conflicti247 – 2471N → D in CAA24268. (PubMed:7292985)Curated
    Sequence conflicti353 – 3531L → V in CAA24268. (PubMed:7292985)Curated
    Sequence conflicti425 – 4251I → V in CAA24268. (PubMed:7292985)Curated
    Sequence conflicti430 – 4301N → T in CAA24268. (PubMed:7292985)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_040982.1. NC_002019.1.

    Genome annotation databases

    GeneIDi956531.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_040982.1. NC_002019.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BST X-ray 2.10 C 383-391 [» ]
    2WFS electron microscopy 12.00 A/B/C/D/E/F/G/H/I 8-498 [» ]
    4NQV X-ray 2.39 M/N/O/P/Q/R 44-52 [» ]
    ProteinModelPortali P03466.
    SMRi P03466. Positions 22-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P03466. 21 interactions.
    MINTi MINT-3375097.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 956531.

    Enzyme and pathway databases

    Reactomei REACT_6145. Influenza Life Cycle.
    REACT_6147. Entry of Influenza Virion into Host Cell via Endocytosis.
    REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
    REACT_6198. Viral RNP Complexes in the Host Cell Nucleus.
    REACT_6212. Budding.
    REACT_6235. Packaging of Eight RNA Segments.
    REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
    REACT_6277. Assembly of Viral Components at the Budding Site.
    REACT_6321. Uncoating of the Influenza Virion.
    REACT_6326. Release.
    REACT_6351. Fusion of the Influenza Virion to the Host Cell Endosome.
    REACT_6354. Viral Messenger RNA Synthesis.
    REACT_9434. vRNP Assembly.
    REACT_9491. Viral mRNA Translation.
    REACT_9497. vRNA Synthesis.
    REACT_9527. cRNA Synthesis.

    Miscellaneous databases

    EvolutionaryTracei P03466.

    Family and domain databases

    InterProi IPR002141. Flu_NP.
    [Graphical view ]
    Pfami PF00506. Flu_NP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiNCAP_I34A1
    AccessioniPrimary (citable) accession number: P03466
    Secondary accession number(s): Q20N34
    , Q58NB3, Q67228, Q80AB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3