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Q1K9H2

- Q1K9H2_I33A0

UniProt

Q1K9H2 - Q1K9H2_I33A0

Protein
Submitted name:

Nucleocapsid protein

Gene

NP

Organism
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (30 May 2006)
      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.SAAS annotation
    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.

    GO - Molecular functioni

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

    GO - Biological processi

    1. viral entry into host cell Source: UniProtKB-KW
    2. viral penetration into host nucleus Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interactionSAAS annotation, Viral penetration into host nucleusSAAS annotation, Virus entry into host cell

    Keywords - Ligandi

    RNA-bindingSAAS annotation, Viral nucleoproteinImported

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Nucleocapsid proteinImported
    Gene namesi
    Name:NPImported
    OrganismiInfluenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))Imported
    Taxonomic identifieri381518 [NCBI]
    Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
    Virus hostiAves [TaxID: 8782]
    Homo sapiens (Human) [TaxID: 9606]
    Sus scrofa (Pig) [TaxID: 9823]

    Subcellular locationi

    Virion SAAS annotation. Host nucleus SAAS annotation

    GO - Cellular componenti

    1. helical viral capsid Source: UniProtKB-KW
    2. host cell nucleus Source: UniProtKB-SubCell
    3. intracellular Source: GOC
    4. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Helical capsid proteinSAAS annotation, Host nucleusSAAS annotation, Virion

    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.SAAS annotation

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IQHX-ray3.20A/B/C8-498[»]
    3RO5X-ray2.66A/B8-498[»]
    3TG6X-ray3.00A/B8-498[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q1K9H2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATKGTKRSY EQMETDGERQ NATEIRASVG KMIDGIGRFY IQMCTELKLS    50
    DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV 100
    DGKWRRELIL YDKEEIRRIW RQANNGDDAT AGLTHMMIWH SNLNDATYQR 150
    TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELIRMIKRG 200
    INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRTMVD QVRESRNPGN 250
    AEFEDLIFLA RSALILRGSV AHKSCLPACV YGSAVASGYD FEREGYSLVG 300
    IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT 350
    KVVPRGKLST RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR 400
    ASSGQISIQP TFSVQRNLPF DRPTIMAAFT GNTEGRTSDM RTEIIRLMES 450
    ARPEDVSFQG RGVFELSDEK ATSPIVPSFD MSNEGSYFFG DNAEEYDN 498
    Length:498
    Mass (Da):56,377
    Last modified:May 30, 2006 - v1
    Checksum:i91390B2963EAB5A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ508906 Genomic RNA. Translation: ABF21292.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ508906 Genomic RNA. Translation: ABF21292.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IQH X-ray 3.20 A/B/C 8-498 [» ]
    3RO5 X-ray 2.66 A/B 8-498 [» ]
    3TG6 X-ray 3.00 A/B 8-498 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

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

    Publicationsi

    1. "The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA."
      Ye Q., Krug R.M., Tao Y.J.
      Nature 444:1078-1082(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 8-498.
    2. "Complete Genome Sequencing And Analysis Of Selected Influenza Virus Vaccine Strains Spanning Six Decades (1933-1999)."
      Mbawuike I.N., Zhang Y., Yamada R.E., Nino D., Bui H.-H., Sette A., Couch R.B.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: A/Wilson-Smith/1933Imported.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 8-498.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 8-498.

    Entry informationi

    Entry nameiQ1K9H2_I33A0
    AccessioniPrimary (citable) accession number: Q1K9H2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 30, 2006
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 47 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3