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P0C0U1 (PB1F2_I34A1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein PB1-F2
Gene names
Name:PB1
OrganismInfluenza A virus (strain A/Puerto Rico/8/1934 H1N1) [Reference proteome]
Taxonomic identifier211044 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesOrthomyxoviridaeInfluenzavirus A
Virus hostAves [TaxID: 8782]
Homo sapiens (Human) [TaxID: 9606]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length87 AA.
Sequence statusComplete.
Protein existenceEvidence 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 cytoplasmhost 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

Keywords
   Biological processApoptosis
Host-virus interaction
Inhibition of host innate immune response by virus
Inhibition of host MAVS by virus
Inhibition of host RLR pathway by virus
Modulation of host cell apoptosis by virus
Viral immunoevasion
   Cellular componentHost cytoplasm
Host membrane
Host mitochondrion
Host mitochondrion inner membrane
Host nucleus
Membrane
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactive induction of host immune response by virus

Traceable author statement. Source: Reactome

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

modulation by virus of host apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

modulation by virus of host morphology or physiology

Traceable author statement. Source: Reactome

negative regulation of interferon-beta secretion

Inferred from mutant phenotype PubMed 2195805. Source: CACAO

suppression by virus of host MAVS activity

Inferred from direct assay Ref.8. Source: UniProtKB

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

host cell cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial intermembrane space

Traceable author statement. Source: Reactome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8787Protein PB1-F2
PRO_0000078743

Regions

Region65 – 8723Mitochondrial targeting sequence

Sites

Site661Important for pathogenicity, S is highly pathogenic whereas N is low pathogenic By similarity

Natural variations

Natural variant221Q → E.
Natural variant59 – 602KQ → RR.

Secondary structure

..... 87
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C0U1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 832A7E34E350B454

FASTA8710,483
        10         20         30         40         50         60 
MGQEQDTPWI LSTGHISTQK RQDGQQTPKL EHRNSTRLMG HCQKTMNQVV MPKQIVYWKQ 

        70         80 
WLSLRNPILV FLKTRVLKRW RLFSKHE 

« Hide

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. expand/collapse author list , Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., 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.
RefSeqYP_418248.1. NC_002021.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HN8NMR-A50-87[»]
3BUYX-ray2.60C62-70[»]
ProteinModelPortalP0C0U1.
SMRP0C0U1. Positions 50-87.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3802042.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.

Family and domain databases

InterProIPR021045. Flu_proapoptotic_PB1-F2.
[Graphical view]
PfamPF11986. PB1-F2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C0U1.

Entry information

Entry namePB1F2_I34A1
AccessionPrimary (citable) accession number: P0C0U1
Secondary accession number(s): A4GXH2, Q20N29
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references