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Q5Q157 (Q5Q157_9INFA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length499 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 By similarity. SAAS SAAS002141

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 By similarity.

Subcellular location

Virion. Host nucleus By similarity SAAS SAAS002141.

Sequences

Sequence LengthMass (Da)Tools
Q5Q157 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 1228BFBA9131BCE7

FASTA49956,235
        10         20         30         40         50         60 
MASQGTKRSY EQMETGGERQ NATEIRASVG RMVGGIGRFY IQMCTELKLS DHEGRLIQNS 

        70         80         90        100        110        120 
ITIERMVLSA FDERRNRYLE EHPSAGKDPK KTGGPIYRRR DGKWMRELIL YDKEEIRRIW 

       130        140        150        160        170        180 
RQANNGEDAT AGLTHIMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG 

       190        200        210        220        230        240 
AAVMGVGTMV MELIRMIKRG IDDRIFWRGE NGPKNKGLHM RECATFSKGS SKQQHKEQWW 

       250        260        270        280        290        300 
TRYEKAGIPG NAEIEDLIFL ARSALILRGS VAHKSCLPAC VYGLAVASGY DFEREGYSLV 

       310        320        330        340        350        360 
GIDPFRLLQN SQVFSLIRPN ENPAHKSQLV WMACHSAAFE DLRVSSFIRG ARVVPRGQLS 

       370        380        390        400        410        420 
TRGVQIASNE NTETMDSSTL ELRSRYWAIR TRSGGNTNQQ RASAGQISVQ PTFSVQRNLP 

       430        440        450        460        470        480 
FERATIMAAF TGSTEGRTSD MRTEIIKMME SARPEDVSFQ GRGVFELSDE KATNPIVPSF 

       490 
DMSKEGSYFF GDNAEEYDN 

« Hide

References

[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/S452/2004 EMBL AAV68025.1.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY790308 Genomic RNA. Translation: AAV68025.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Entry information

Entry nameQ5Q157_9INFA
AccessionPrimary (citable) accession number: Q5Q157
Entry history
Integrated into UniProtKB/TrEMBL: January 4, 2005
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)