P0C0U1 (PB1F2_I34A1) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 46.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein PB1-F2 | ||
| Gene names |
| ||
| Organism | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) [Reference proteome] | ||
| Taxonomic identifier | 211044 [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] |
Protein attributes
| Sequence length | 87 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Plays an important role in promoting lung pathology in both primary viral infection and secondary bacterial infection. Promotes alteration of mitochondrial morphology, dissipation of mitochondrial membrane potential, and cell death. Alternatively, inhibits the production of interferon in the infected cell at the level of host mitochondrial antiviral signaling MAVS. Its level of expression differs greatly depending on which cell type is infected, in a manner that is independent of the levels of expression of other viral proteins. Monocytic cells are more affected than epithelial cells. Seems to disable virus-infected monocytes or other host innate immune cells. May also act in trans: extracellular PB1-F2 released by infected cells could potentially inactivate hosts cell recruitment to the site of infection. During early stage of infection, may predispose the mitochondria to permeability transition through interaction with human SLC25A6/ANT3 and VDAC1. These proteins participate in the formation of the permeability transition pore complex (PTPC) responsible of the release of mitochondrial products that triggers apoptosis. Ref.8 |
| Subunit structure | Oligomer. Interacts with human SLC25A6/ANT3 and VDAC1. Ref.6 |
| Subcellular location | Host mitochondrion inner membrane. Host nucleus. Host cytoplasm › host cytosol. Note: Inner mitochondrial membrane in most cells types. Otherwise is detected in the nucleus and cytosol. Ref.5 |
| Miscellaneous | Is not encoded in all strains, and seems to be dispensable for replication. |
| Sequence similarities | Belongs to the influenza viruses PB1-F2 family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||
Molecule processing | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 87 | 87 | Protein PB1-F2 | PRO_0000078743 | |||||||||
Regions | |||||||||||||
| Region | 65 – 87 | 23 | Mitochondrial targeting sequence | ||||||||||
Sites | |||||||||||||
| Site | 66 | 1 | Important for pathogenicity, S is highly pathogenic whereas N is low pathogenic By similarity | ||||||||||
Natural variations | |||||||||||||
| Natural variant | 22 | 1 | Q → E. | ||||||||||
| Natural variant | 59 – 60 | 2 | KQ → RR. | ||||||||||
Secondary structure | |||||||||||||
Helix Strand Turn | |||||||||||||
| Helix | 52 – 62 | 11 | |||||||||||
| Helix | 65 – 86 | 22 | |||||||||||
Sequences
References
| [1] | "Nucleotide sequence of human influenza A/PR/8/34 segment 2." Winter G., Fields S. Nucleic Acids Res. 10:2135-2143(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [2] | "Efficient generation and growth of influenza virus A/PR/8/34 from eight cDNA fragments." de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., Osterhaus A.D.M.E., Fouchier R.A.M. Virus Res. 103:155-161(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], REVERSE GENETICS. |
| [3] | "The NIAID influenza genome sequencing project." Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y. Tatusova T.Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [4] | "A novel influenza A virus mitochondrial protein that induces cell death." Chen W., Calvo P.A., Malide D., Gibbs J., Schubert U., Bacik I., Basta S., O'Neill R., Schickli J., Palese P., Henklein P., Bennink J.R., Yewdell J.W. Nat. Med. 7:1306-1312(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. |
| [5] | "The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function." Gibbs J.S., Malide D., Hornung F., Bennink J.R., Yewdell J.W. J. Virol. 77:7214-7224(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [6] | "Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1." Zamarin D., Garcia-Sastre A., Xiao X., Wang R., Palese P. PLoS Pathog. 1:40-54(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HUMAN SLC25A6/ANT3 AND VDAC1. |
| [7] | "Structural characterization and oligomerization of PB1-F2, a proapoptotic Influenza A Virus protein." Bruns K., Studtrucker N., Sharma A., Fossen T., Mitzner D., Eissmann A., Tessmer U., Roder R., Henklein P., Wray V., Schubert U. J. Biol. Chem. 282:353-363(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 50-87. |
| [8] | "The influenza virus protein PB1-F2 inhibits the induction of type I interferon at the level of the MAVS adaptor protein." Varga Z.T., Ramos I., Hai R., Schmolke M., Garcia-Sastre A., Fernandez-Sesma A., Palese P. PLoS Pathog. 7:E1002067-E1002067(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | J02151 Genomic RNA. No translation available. EF467819 Genomic RNA. Translation: ABO21707.1. CY009450 Genomic RNA. Translation: ABD77684.1. | ||||||||||||||||||
| RefSeq | YP_418248.1. NC_002021.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P0C0U1. | ||||||||||||||||||
| SMR | P0C0U1. Positions 50-87. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 3802042. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| Reactome | REACT_116125. Disease. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR021045. Flu_proapoptotic_PB1-F2. [Graphical view] | ||||||||||||||||||
| Pfam | PF11986. PB1-F2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other | |||||||||||||||||||
| EvolutionaryTrace | P0C0U1. | ||||||||||||||||||
Entry information
| Entry name | PB1F2_I34A1 | ||||||||
| Accession | Primary (citable) accession number: P0C0U1 Secondary accession number(s): A4GXH2, Q20N29 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
