Unreviewed,
UniProtKB/TrEMBL A0A4M4 (A0A4M4_9INFA)
Last modified
September 23, 2008.
Version 17.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Submitted name: Nucleoprotein EMBL ABJ90249.1 | ||
| Gene names |
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| Organism | Influenza A virus (A/chicken/Italy/5093/99(H7N1)) EMBL ABJ90249.1 | ||
| Taxonomic identifier | 414453 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Orthomyxoviridae › Influenzavirus A |
Protein attributes
| Sequence length | 497 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Predicted. |
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. Spearmint SPM002141 |
| 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. Spearmint SPM002141 |
| Subcellular location | VirionPotential. Nucleus. Spearmint SPM002141 |
Ontologies
Keywords | |
|---|---|
| Biological process | Host-virus interaction Spearmint SPM002141 |
| Cellular component | Nucleus Spearmint SPM002141 Virion |
| Ligand | RNA-binding Spearmint SPM002141 Viral nucleoprotein |
Gene Ontology (GO) | |
| Biological process | interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoprotein complexInferred from electronic annotation. Source: UniProtKB-KW virionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequences
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References
| [1] | "Pneumo- and neurotropism of avian origin Italian highly pathogenic avian influenza H7N1 isolates in experimentally infected mice." Rigoni M., Shinya K., Toffan A., Milani A., Bettini F., Kawaoka Y., Cattoli G., Capua I. Virology 364:28-35(2007) [PubMed: 17408714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: A/chicken/Italy/5093/99 EMBL ABJ90249.1. |
Cross-references
Sequence databases | |
|---|---|
| DQ991321 Viral cRNA. Translation: ABJ90249.1. DQ991329 Viral cRNA. Translation: ABJ90260.2. | |
3D structure databases | |
| SMR | A0A4M4. Positions 20-488. |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR002141. Flu_NP. [Graphical view] |
| Pfam | PF00506. Flu_NP. 1 hit. [Graphical view] |
| ProDom | A0A4M4. [Graphical view] [Entries sharing at least one domain] |
Entry information
| Entry name | A0A4M4_9INFA | ||||||||
| Accession | Primary (citable) accession number: A0A4M4 Secondary accession number(s): A0A4N5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||
Relevant documents
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |

Clusters with


