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Q1K9H2 (Q1K9H2_I33A0) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 46. Feed History...

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

Sequence length498 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.

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. SAAS SAAS002141

Subcellular location

Virion. Host nucleus By similarity SAAS SAAS002141.

Sequences

Sequence LengthMass (Da)Tools
Q1K9H2 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 91390B2963EAB5A3

FASTA49856,377
        10         20         30         40         50         60 
MATKGTKRSY EQMETDGERQ NATEIRASVG KMIDGIGRFY IQMCTELKLS DYEGRLIQNS 

        70         80         90        100        110        120 
LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV DGKWRRELIL YDKEEIRRIW 

       130        140        150        160        170        180 
RQANNGDDAT AGLTHMMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG 

       190        200        210        220        230        240 
AAVKGVGTMV MELIRMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRTMVD 

       250        260        270        280        290        300 
QVRESRNPGN AEFEDLIFLA RSALILRGSV AHKSCLPACV YGSAVASGYD FEREGYSLVG 

       310        320        330        340        350        360 
IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT KVVPRGKLST 

       370        380        390        400        410        420 
RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR ASSGQISIQP TFSVQRNLPF 

       430        440        450        460        470        480 
DRPTIMAAFT GNTEGRTSDM RTEIIRLMES ARPEDVSFQG RGVFELSDEK ATSPIVPSFD 

       490 
MSNEGSYFFG DNAEEYDN 

« Hide

References

[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/1933 EMBL ABF21292.1.
[3]"Inhibition of influenza virus replication via small molecules that induce the formation of higher-order nucleoprotein oligomers."
Gerritz S.W., Cianci C., Kim S., Pearce B.C., Deminie C., Discotto L., McAuliffe B., Minassian B.F., Shi S., Zhu S., Zhai W., Pendri A., Li G., Poss M.A., Edavettal S., McDonnell P.A., Lewis H.A., Maskos K. expand/collapse author list , Mortl M., Kiefersauer R., Steinbacher S., Baldwin E.T., Metzler W., Bryson J., Healy M.D., Philip T., Zoeckler M., Schartman R., Sinz M., Leyva-Grado V.H., Hoffmann H.H., Langley D.R., Meanwell N.A., Krystal M.
Proc. Natl. Acad. Sci. U.S.A. 108:15366-15371(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 8-498.
[4]"Biophysical and Structural Characterization of a Novel Class of Influenza Virus Inhibitors."
Edavettal S.C., Pearce B.C., Lewis H.A., Schneeweis L., Deminie C., Discotto L., Carpenter B., Yanchunas J., Langley D.R., Metzler W., Gao M., Poss M.A., Maskos K., Mortl M., Keifersauer R., Steinbacher S., Healy M., Phillip T. expand/collapse author list , Zoeckler M., Schartman R., McAuliffe B., Minassian B.F., Shi S., Zhu S., Pendri A., Li G., Sinz M., Meanwell N.A., Krystal M., Gerritz S.W., Cianci C., Baldwin B.T., Bryson J.W., McDonnell P.A.
Submitted (AUG-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 8-498.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ508906 Genomic RNA. Translation: ABF21292.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IQHX-ray3.20A/B/C8-498[»]
3RO5X-ray2.66A/B8-498[»]
3TG6X-ray3.00A/B8-498[»]
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 nameQ1K9H2_I33A0
AccessionPrimary (citable) accession number: Q1K9H2
Entry history
Integrated into UniProtKB/TrEMBL: May 30, 2006
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)