Q1K9H2 (Q1K9H2_I33A0) Unreviewed, UniProtKB/TrEMBL
Last modified February 19, 2014. Version 46. History...
Names and origin
|Protein names||Submitted name:|
Nucleocapsid protein EMBL ABF21292.1
|Organism||Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) EMBL ABF21292.1|
|Taxonomic identifier||381518 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus A ›|
|Virus host||Aves [TaxID: 8782]|
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]
|Sequence length||498 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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.
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
|||"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.
|||"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.
|||"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. 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.
|||"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. McDonnell P.A.
Submitted (AUG-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 8-498.
|DQ508906 Genomic RNA. Translation: ABF21292.1.|
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR002141. Flu_NP. |
|Pfam||PF00506. Flu_NP. 1 hit. |
|Accession||Primary (citable) accession number: Q1K9H2|
|Entry status||Unreviewed (UniProtKB/TrEMBL)|