Q9R016 · BIR1E_MOUSE
- ProteinBaculoviral IAP repeat-containing protein 1e
- GeneNaip5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1403 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Sensor component of the NLRC4 inflammasome that specifically recognizes and binds flagellin from pathogenic bacteria such as Legionella or Salmonella (PubMed:12526741, PubMed:21874021, PubMed:21918512, PubMed:29146805, PubMed:29182158).
Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis (PubMed:21874021, PubMed:21918512, PubMed:29146805, PubMed:29182158).
The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri (PubMed:21874021, PubMed:21918512, PubMed:29146805, PubMed:29182158).
May contribute to prevent motor-neuron apoptosis induced by a variety of signals (By similarity).
Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis (PubMed:21874021, PubMed:21918512, PubMed:29146805, PubMed:29182158).
The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria. The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri (PubMed:21874021, PubMed:21918512, PubMed:29146805, PubMed:29182158).
May contribute to prevent motor-neuron apoptosis induced by a variety of signals (By similarity).
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | IPAF inflammasome complex | |
Cellular Component | neuronal cell body | |
Cellular Component | perikaryon | |
Molecular Function | ATP binding | |
Molecular Function | cysteine-type endopeptidase inhibitor activity involved in apoptotic process | |
Molecular Function | metal ion binding | |
Biological Process | apoptotic process | |
Biological Process | defense response to bacterium | |
Biological Process | defense response to Gram-negative bacterium | |
Biological Process | detection of bacterium | |
Biological Process | inflammatory response | |
Biological Process | innate immune response | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | positive regulation of interleukin-1 beta production | |
Biological Process | pyroptotic inflammatory response | |
Biological Process | symbiont entry into host cell |
Keywords
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBaculoviral IAP repeat-containing protein 1e
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9R016
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1-40 | Abolishes production of IL1B in response to bacterial flagellin. | ||||
Sequence: Missing | ||||||
Mutagenesis | 11 | Strongly reduces production of IL1B in response to bacterial flagellin; then associated with F-15. | ||||
Sequence: R → I | ||||||
Mutagenesis | 15 | Strongly reduces production of IL1B in response to bacterial flagellin; then associated with I-11. | ||||
Sequence: I → F | ||||||
Mutagenesis | 106-108 | Strongly reduces production of IL1B in response to bacterial flagellin. | ||||
Sequence: GNS → STR | ||||||
Mutagenesis | 626-627 | Strongly reduced interaction with flagellin. | ||||
Sequence: II → AA | ||||||
Mutagenesis | 837-838 | Mildly reduced interaction with flagellin. | ||||
Sequence: QT → AA | ||||||
Mutagenesis | 839-840 | Mildly reduced interaction with flagellin. | ||||
Sequence: FL → AA | ||||||
Mutagenesis | 840 | Strongly reduces production of IL1B in response to bacterial flagellin. | ||||
Sequence: L → R | ||||||
Mutagenesis | 841-842 | Mildly reduced interaction with flagellin. | ||||
Sequence: WF → AA | ||||||
Mutagenesis | 843-844 | Strongly reduced interaction with flagellin. | ||||
Sequence: QF → AA | ||||||
Mutagenesis | 844 | Strongly reduces production of IL1B in response to bacterial flagellin. | ||||
Sequence: F → C | ||||||
Mutagenesis | 847 | Strongly reduces production of IL1B in response to bacterial flagellin. | ||||
Sequence: G → E | ||||||
Mutagenesis | 847 | Nearly abolishes interaction with flagellin. | ||||
Sequence: G → K | ||||||
Mutagenesis | 848-849 | Strongly reduced interaction with flagellin. | ||||
Sequence: LW → AA | ||||||
Mutagenesis | 857 | No effect on production of IL1B in response to bacterial flagellin. | ||||
Sequence: S → Y | ||||||
Mutagenesis | 974-975 | Strongly reduced interaction with flagellin. | ||||
Sequence: YE → AA | ||||||
Mutagenesis | 1329-1330 | Reduced interaction with flagellin. | ||||
Sequence: CR → AA | ||||||
Mutagenesis | 1390-1403 | Abolishes production of IL1B in response to bacterial flagellin. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 153 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000122344 | 1-1403 | Baculoviral IAP repeat-containing protein 1e | |||
Sequence: MAEHGESSEDRISEIDYEFLPELSALLGVDAFQVAKSQEEEEHKERMKMKKGFNSQMRSEAKRLKTFETYDTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFLQGKDVGNIGKYDIRVKRPEKMLRGGKARYHEEEARLESFEDWPFYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQSKKSSEEIAQYIQSYEGFVHVTGEHFVKSWVRRELPMVSAYCNDSVFANEELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQTLKSSAEVIPTLQSQYALPEATETTRESNHGDAAAVHSTVVDLGRSEAQWFQEARSLSEQLRDNYTKATFRHMNLPEVCSSLGTDHLLSCDVSIISKHISQPVQEALTIPEVFSNLNSVMCVEGETGSGKTTFLKRIAFLWASGCCPLLYRFQLVFYLSLSSITPDQGLANIICAQLLGAGGCISEVCLSSSIQQLQHQVLFLLDDYSGLASLPQALHTLITKNYLSRTCLLIAVHTNRVRDIRLYLGTSLEIQEFPFYNTVSVLRKFFSHDIICVEKLIIYFIDNKDLQGVYKTPLFVAAVCTDWIQNASAQDKFQDVTLFQSYMQYLSLKYKATAEPLQATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDEKLTTLLMSKFTAQRLRPVYRFLGPLFQEFLAAVRLTELLSSDRQEDQDLGLYYLRQIDSPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFLWFQFVRGLWLVSPESSSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGKTLALRVLNLQYFRDHPESLLLLRSLKVSINGNKMSSYVDYSFKTYFENLQPPAIDEEYTSAFEHISEWRRNFAQDEEIIKNYENIRPRALPDISEGYWKLSPKPCKIPKLEVQVNNTDAADQALLQVLMEVFSASQSIEFRLFNSSGFLESICPALELSKASVTKCSMSRLELSRAEQELLLTLPALQSLEVSETNQLPEQLFHNLHKFLGLKELCVRLDGKPNVLSVLPREFPNLLHMEKLSIQTSTESDLSKLVKFIQNFPNLHVFHLKCDFLSNCESLMAVLASCKKLREIEFSGRCFEAMTFVNILPNFVSLKILNLKDQQFPDKETSEKFAQALGSLRNLEELLVPTGDGIHQVAKLIVRQCLQLPCLRVLTFHDILDDDSVIEIARAATSGGFQKLENLDISMNHKITEEGYRNFFQALDNLPNLQELNICRNIPGRIQVQATTVKALGQCVSRLPSLIRLHMLSWLLDEEDMKVINDVKERHPQSKRLIIFWKLIVPFSPVILE |
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the NLRC4 inflammasome, at least composed of NLRC4, caspase-1 (CASP1) and some NAIP protein. Flagellin binding by NAIP5 triggers assembly of the inflammasome, a huge complex that contains a single NAIP5 chain and multiple copies of NLRC4 (PubMed:29182158).
(Microbial infection) Interacts with S.typhimurium (Salmonella) flagellin.
(Microbial infection) Interacts with L.pneumophila flagellin.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q9R016 | flaA Q48824 | 2 | EBI-15944130, EBI-15944232 | |
XENO | Q9R016 | fliC P06179 | 9 | EBI-15944130, EBI-2011501 | |
BINARY | Q9R016 | Nlrc4 Q3UP24 | 18 | EBI-15944130, EBI-16006652 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 60-127 | BIR 1 | ||||
Sequence: EAKRLKTFETYDTFRSWTPQEMAAAGFYHTGVRLGVQCFCCSLILFGNSLRKLPIERHKKLRPECEFL | ||||||
Repeat | 159-227 | BIR 2 | ||||
Sequence: EEARLESFEDWPFYAHGTSPRVLSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFL | ||||||
Repeat | 278-345 | BIR 3 | ||||
Sequence: EELRMDMFKDWPQESPVGVEALVRAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFL | ||||||
Domain | 464-759 | NACHT | ||||
Sequence: SVMCVEGETGSGKTTFLKRIAFLWASGCCPLLYRFQLVFYLSLSSITPDQGLANIICAQLLGAGGCISEVCLSSSIQQLQHQVLFLLDDYSGLASLPQALHTLITKNYLSRTCLLIAVHTNRVRDIRLYLGTSLEIQEFPFYNTVSVLRKFFSHDIICVEKLIIYFIDNKDLQGVYKTPLFVAAVCTDWIQNASAQDKFQDVTLFQSYMQYLSLKYKATAEPLQATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDEDEKLTTLLMSKFTAQRLRPVYRFLGPLFQEFLAAVRLTE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,403
- Mass (Da)159,839
- Last updated2018-04-25 v3
- Checksum04C04877908103EE
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 92 | in Ref. 2; AAD56760 and 6; AAC52974 | ||||
Sequence: R → K | ||||||
Sequence conflict | 144 | in Ref. 2; AAD56760 and 6; AAC52974 | ||||
Sequence: R → S | ||||||
Sequence conflict | 242 | in Ref. 2; AAD56760 | ||||
Sequence: S → G | ||||||
Sequence conflict | 472 | in Ref. 2; AAD56760 | ||||
Sequence: T → A | ||||||
Sequence conflict | 516 | in Ref. 2; AAD56760 | ||||
Sequence: A → D | ||||||
Sequence conflict | 521 | in Ref. 2; AAD56760 | ||||
Sequence: A → T | ||||||
Sequence conflict | 533 | in Ref. 2; AAD56760 | ||||
Sequence: V → A | ||||||
Sequence conflict | 538 | in Ref. 2; AAD56760 | ||||
Sequence: S → I | ||||||
Sequence conflict | 1092 | in Ref. 2; AAD56760 | ||||
Sequence: E → D | ||||||
Sequence conflict | 1116 | in Ref. 1; AAD56764 and 2; AAD56760 | ||||
Sequence: N → D | ||||||
Sequence conflict | 1123 | in Ref. 1; AAD56764 and 2; AAD56760 | ||||
Sequence: R → G | ||||||
Sequence conflict | 1129 | in Ref. 1; AAD56764 | ||||
Sequence: L → H | ||||||
Sequence conflict | 1137 | in Ref. 1; AAD56764 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 1242 | in Ref. 2; AAD56760 | ||||
Sequence: V → I | ||||||
Sequence conflict | 1276 | in Ref. 2; AAD56760 | ||||
Sequence: D → N |
Polymorphism
Part of the Lgn1 locus that determines susceptibility to the intracellular pathogen L.pneumophila. Susceptibility differs between inbred mouse strains. Strain C57BL/6J is not permissive, i.e. L.pneumophila cannot multiply in C57BL/6J macrophages, contrary to the situation in mouse strain A/J. Strain FVB/NJ macrophages display intermediate permissiveness for intracellular proliferation of L.pneumophila.
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF135492 EMBL· GenBank· DDBJ | AAD56764.1 EMBL· GenBank· DDBJ | mRNA | ||
AF131205 EMBL· GenBank· DDBJ | AAD56760.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY146999 EMBL· GenBank· DDBJ | AAN60211.1 EMBL· GenBank· DDBJ | mRNA | ||
CT009518 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CT030167 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC070433 EMBL· GenBank· DDBJ | AAH70433.1 EMBL· GenBank· DDBJ | mRNA | ||
U66326 EMBL· GenBank· DDBJ | AAC52974.1 EMBL· GenBank· DDBJ | Genomic DNA |