Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nucleoprotein

Gene

NP

Organism
Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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.UniRule 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.SAAS annotation

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
Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

RNA-bindingSAAS annotation, Viral nucleoproteinUniRule annotationImported

Names & Taxonomyi

Protein namesi
Recommended name:
NucleoproteinUniRule annotation
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 UniRule annotationSAAS annotation. Host nucleus UniRule annotationSAAS 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
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Helical capsid proteinSAAS annotation, Host nucleusUniRule annotationSAAS annotation, Virion

Interactioni

Subunit structurei

Homomultimerizes to form the nucleocapsid.UniRule annotation
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:
PDBei
RCSB PDBi
PDBji
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

Sequence similaritiesi

Belongs to the influenza viruses nucleoprotein family.UniRule annotation

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

        10         20         30         40         50
MATKGTKRSY EQMETDGERQ NATEIRASVG KMIDGIGRFY IQMCTELKLS
60 70 80 90 100
DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV
110 120 130 140 150
DGKWRRELIL YDKEEIRRIW RQANNGDDAT AGLTHMMIWH SNLNDATYQR
160 170 180 190 200
TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELIRMIKRG
210 220 230 240 250
INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRTMVD QVRESRNPGN
260 270 280 290 300
AEFEDLIFLA RSALILRGSV AHKSCLPACV YGSAVASGYD FEREGYSLVG
310 320 330 340 350
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT
360 370 380 390 400
KVVPRGKLST RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR
410 420 430 440 450
ASSGQISIQP TFSVQRNLPF DRPTIMAAFT GNTEGRTSDM RTEIIRLMES
460 470 480 490
ARPEDVSFQG RGVFELSDEK ATSPIVPSFD MSNEGSYFFG DNAEEYDN
Length:498
Mass (Da):56,377
Last modified:May 29, 2006 - v1
Checksum:i91390B2963EAB5A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ508906 Genomic RNA. Translation: ABF21292.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ508906 Genomic RNA. Translation: ABF21292.1.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

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(2005) [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 (MAR-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 29, 2006
Last sequence update: May 29, 2006
Last modified: February 3, 2015
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.