Q5Q157 (Q5Q157_9INFA) Unreviewed, UniProtKB/TrEMBL
Last modified February 19, 2014. Version 44. History...
Names and origin
|Sequence length||499 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. SAAS SAAS002141
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.
|Biological process||Host-virus interaction SAAS SAAS002141|
Viral penetration into host nucleus SAAS SAAS002141
Virus entry into host cell
|Cellular component||Capsid protein|
Helical capsid protein SAAS SAAS002141
Host nucleus SAAS SAAS002141
|Ligand||RNA-binding SAAS SAAS002141|
|Technical term||3D-structure PDB 4HUU PDB 4HUV PDB 4HUW PDB 4HUX PDB 4HV8|
|Gene Ontology (GO)|
|Biological_process||viral entry into host cell|
Inferred from electronic annotation. Source: UniProtKB-KWviral penetration into host nucleus
Inferred from electronic annotation. Source: UniProtKB-KW
|Cellular_component||helical viral capsid|
Inferred from electronic annotation. Source: UniProtKB-KWhost cell nucleus
Inferred from electronic annotation. Source: UniProtKB-SubCellintracellular
Inferred from electronic annotation. Source: GOC
Inferred from electronic annotation. Source: UniProtKB-KWstructural molecule activity
Inferred from electronic annotation. Source: InterPro
|Complete GO annotation...|
|||"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.
|||"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.
|AY790308 Genomic RNA. Translation: AAV68025.1.|
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: Q5Q157|
|Entry status||Unreviewed (UniProtKB/TrEMBL)|