Q0GUM3 · IRB10_MOUSE
- ProteinInterferon-gamma-inducible GTPase 10
- GeneGm12250
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids417 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens by mediating cytosolic release of pathogenic ligands that activate the inflammasomes (PubMed:16959883, PubMed:20109161, PubMed:27693356, PubMed:30062052, PubMed:30510167, PubMed:34694641).
Following infection, recruited to the membrane of pathogens in a GBP-dependent manner and mediates disruption of the pathogen membrane, liberating ligands that are detected by inflammasomes, such as lipopolysaccharide (LPS) that activates the non-canonical CASP4/CASP11 inflammasome or double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (PubMed:27693356, PubMed:30062052, PubMed:30510167).
Promotes AIM2 and NLRP3 inflammasome activation following A.fumigatus infection by liberating beta-glucan, which directly triggers inflammasome assembly (PubMed:30510167).
Promotes NLRP3 inflammasome activation following influenza A virus infection (PubMed:34694641).
Following infection, recruited to the membrane of pathogens in a GBP-dependent manner and mediates disruption of the pathogen membrane, liberating ligands that are detected by inflammasomes, such as lipopolysaccharide (LPS) that activates the non-canonical CASP4/CASP11 inflammasome or double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (PubMed:27693356, PubMed:30062052, PubMed:30510167).
Promotes AIM2 and NLRP3 inflammasome activation following A.fumigatus infection by liberating beta-glucan, which directly triggers inflammasome assembly (PubMed:30510167).
Promotes NLRP3 inflammasome activation following influenza A virus infection (PubMed:34694641).
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 78 | GDP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 79 | GDP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 82 | GDP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 83 | GDP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 101 | GDP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 183 | GDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 185 | GDP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 231 | GDP (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | symbiont cell surface | |
Molecular Function | G protein activity | |
Molecular Function | GTP binding | |
Molecular Function | membrane destabilizing activity | |
Biological Process | defense response to bacterium | |
Biological Process | defense response to fungus | |
Biological Process | defense response to protozoan | |
Biological Process | defense response to virus | |
Biological Process | disruption of plasma membrane integrity in another organism | |
Biological Process | innate immune response | |
Biological Process | killing of cells of another organism | |
Biological Process | positive regulation of AIM2 inflammasome complex assembly | |
Biological Process | positive regulation of NLRP3 inflammasome complex assembly | |
Biological Process | positive regulation of pyroptotic inflammatory response | |
Biological Process | protein homooligomerization | |
Biological Process | response to bacterium |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterferon-gamma-inducible GTPase 10
- EC number
- Short namesIrgb10
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 accessionQ0GUM3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Cytoplasmic vesicle membrane ; Multi-pass membrane protein
Note: Recruited to the membrane of pathogens in the cytosol in a GBP (Gbp1, Gbp2, Gbp3, Gbp5 ad/or Gbp7)-dependent manner (PubMed:27693356).
Recruited to the membrane of pathogen-containing vacuoles: vacuoles may serve as a cellular transport mechanism to deliver Gm12250/Irgb10 to the pathogen membrane (Probable) (PubMed:23785284, PubMed:27693356).
Recruited to the membrane of pathogen-containing vacuoles: vacuoles may serve as a cellular transport mechanism to deliver Gm12250/Irgb10 to the pathogen membrane (Probable) (PubMed:23785284, PubMed:27693356).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 284-302 | Helical | ||||
Sequence: EALKAGASATIPMMSFFND | ||||||
Transmembrane | 370-387 | Helical | ||||
Sequence: AVTGGFVATGLYFRKSYY |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 81 | Abolished GTPase activity, promoting localization to lipid droplets. | ||||
Sequence: K → A | ||||||
Mutagenesis | 82 | Abolished localization to pathogen-containing vacuoles. | ||||
Sequence: S → N | ||||||
Mutagenesis | 132 | Does not affect formation of a head-to-head homodimer in presence of GDP. | ||||
Sequence: T → W | ||||||
Mutagenesis | 185 | Impaired formation of a head-to-head homodimer in presence of GDP. | ||||
Sequence: D → R | ||||||
Mutagenesis | 193 | Impaired formation of a head-to-head homodimer in presence of GDP. | ||||
Sequence: K → E | ||||||
Mutagenesis | 206 | Does not affect formation of a head-to-head homodimer in presence of GDP. | ||||
Sequence: E → K |
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000457891 | 2-417 | Interferon-gamma-inducible GTPase 10 | |||
Sequence: GQSSSKPDAKAHNMASSLTEFFKNFKMESKIISKETIDSIQSCIQEGDIQKVISIINAALTDIEKAPLNIAVTGETGAGKSTFINALRGIGHEESESAESGAVETTKDRKKYTHPKFPNVTIWDLPGVGTTNFKPEEYLKKMKFQEYDFFLIISSARFRDNEAQLAEAIKKMKKKFYFVRTKIDSDLWNEKKAKPSSYNREKILEVIRSDCVKNLQNANAASTRVFLVSSFEVAQFDFPSLESTLLEELPAHKRHIFVQCLPTITEPAIDRRRDVLKQTIWLEALKAGASATIPMMSFFNDDIEEFEKILSHYRACFGLDDESLENMAKEWSMSVEELESTIKSPHLLSSEPNESVADKLVKTMEKIFAVTGGFVATGLYFRKSYYMQNYFLDTVTEDAKVLLKKKVFLQDSVDSE |
Post-translational modification
Myristoylation is required for localization to pathogen-containing vacuoles (PubMed:23785284).
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 67-249 | IRG-type G | ||||
Sequence: APLNIAVTGETGAGKSTFINALRGIGHEESESAESGAVETTKDRKKYTHPKFPNVTIWDLPGVGTTNFKPEEYLKKMKFQEYDFFLIISSARFRDNEAQLAEAIKKMKKKFYFVRTKIDSDLWNEKKAKPSSYNREKILEVIRSDCVKNLQNANAASTRVFLVSSFEVAQFDFPSLESTLLEE |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length417
- Mass (Da)47,264
- Last updated2006-10-03 v1
- ChecksumC43A27660835EB6F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 15 | in Ref. 1; ABF85831 | ||||
Sequence: M → T | ||||||
Sequence conflict | 108 | in Ref. 1; ABF85831 | ||||
Sequence: K → M | ||||||
Sequence conflict | 161 | in Ref. 1; ABF85831 | ||||
Sequence: D → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ508486 EMBL· GenBank· DDBJ | ABF85830.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ508487 EMBL· GenBank· DDBJ | ABF85831.1 EMBL· GenBank· DDBJ | mRNA | ||
AL928857 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |