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
N/A
Organism
Influenza A virus (A/swine/Korea/S452/2004(H9N2))
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 annotation

Names & Taxonomyi

Protein namesi
Recommended name:
NucleoproteinUniRule annotation
OrganismiInfluenza A virus (A/swine/Korea/S452/2004(H9N2))Imported
Taxonomic identifieri300749 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A

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
4HUUX-ray2.00C/F367-375[»]
4HUVX-ray2.50C/F367-375[»]
4HUWX-ray3.16I/J/K/L367-375[»]
4HUXX-ray2.20C367-375[»]
4HV8X-ray2.00E/F367-375[»]
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.

Q5Q157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQGTKRSY EQMETGGERQ NATEIRASVG RMVGGIGRFY IQMCTELKLS
60 70 80 90 100
DHEGRLIQNS ITIERMVLSA FDERRNRYLE EHPSAGKDPK KTGGPIYRRR
110 120 130 140 150
DGKWMRELIL YDKEEIRRIW RQANNGEDAT AGLTHIMIWH SNLNDATYQR
160 170 180 190 200
TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVMGVGTMV MELIRMIKRG
210 220 230 240 250
IDDRIFWRGE NGPKNKGLHM RECATFSKGS SKQQHKEQWW TRYEKAGIPG
260 270 280 290 300
NAEIEDLIFL ARSALILRGS VAHKSCLPAC VYGLAVASGY DFEREGYSLV
310 320 330 340 350
GIDPFRLLQN SQVFSLIRPN ENPAHKSQLV WMACHSAAFE DLRVSSFIRG
360 370 380 390 400
ARVVPRGQLS TRGVQIASNE NTETMDSSTL ELRSRYWAIR TRSGGNTNQQ
410 420 430 440 450
RASAGQISVQ PTFSVQRNLP FERATIMAAF TGSTEGRTSD MRTEIIKMME
460 470 480 490
SARPEDVSFQ GRGVFELSDE KATNPIVPSF DMSKEGSYFF GDNAEEYDN
Length:499
Mass (Da):56,235
Last modified:January 4, 2005 - v1
Checksum:i1228BFBA9131BCE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY790308 Genomic RNA. Translation: AAV68025.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY790308 Genomic RNA. Translation: AAV68025.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HUUX-ray2.00C/F367-375[»]
4HUVX-ray2.50C/F367-375[»]
4HUWX-ray3.16I/J/K/L367-375[»]
4HUXX-ray2.20C367-375[»]
4HV8X-ray2.00E/F367-375[»]
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. "Reassorted Swine H9N2 Influenza virus in Korea, 2004."
    Seo S.-H., Kim J.-A., Jo S.-K.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A/Swine/Korea/S452/2004Imported.
  2. "Preemptive priming readily overcomes structure-based mechanisms of virus escape."
    Valkenburg S.A., Gras S., Guillonneau C., Hatton L.A., Bird N.A., Twist K.A., Halim H., Jackson D.C., Purcell A.W., Turner S.J., Doherty P.C., Rossjohn J., Kedzierska K.
    Proc. Natl. Acad. Sci. U.S.A. 110:5570-5575(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 367-375.

Entry informationi

Entry nameiQ5Q157_9INFA
AccessioniPrimary (citable) accession number: Q5Q157
Entry historyi
Integrated into UniProtKB/TrEMBL: January 4, 2005
Last sequence update: January 4, 2005
Last modified: March 4, 2015
This is version 49 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.