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Q91VJ1 (AIM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-inducible protein AIM2
Alternative name(s):
Interferon-inducible protein 210
Short name=Ifi-210
Interferon-inducible protein p210
Gene names
Name:Aim2
Synonyms:Gm1313, Ifi210
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in innate immune response by recognizing cytosolic double-stranded DNA and inducing caspase-1-activating inflammasome formation in macrophages. Upon binding to DNA is thought to undergo oligomerization and to associate with PYCARD initiating the recruitment of caspase-1 precusrsor and processing of interleukin-1 beta and interleukin-18. Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner. Can also trigger PYCARD-dependent, caspase-1-independent cell death that involves caspase-8. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Enzyme regulation

In absence of dsDNA DAPIN and HIN-20 domain can interact inducing a closed conformation; an autoinhibitory mechanism is proposed in which binding to dsDNA liberates the DAPIN domain for homotypic downstream signaling interactions with PYCARD By similarity.

Subunit structure

Self-associates; forms homooligomers in response to cytosolic dsDNA and the dsDNA seems to serve as oligomerization platform. Component of the AIM2 inflammasome complex. Interacts with PYCARD. Interacts with IFI16 By similarity. Interacts with EIF2AK2/PKR By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm Ref.11.

Domain

The DAPIN domain mediates homotypic interaction with PYCARD By similarity. Ref.13

The HIN-20 domain mediates dsDNA binding via electrostatic interactions. Ref.13

Sequence similarities

Belongs to the HIN-200 family.

Contains 1 DAPIN domain.

Contains 1 HIN-200 domain.

Sequence caution

The sequence AAH09664.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
Immunity
Inflammatory response
Innate immunity
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of innate immune response

Inferred from direct assay Ref.4. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to drug

Inferred from sequence orthology PubMed 19158679. Source: MGI

cellular response to interferon-beta

Inferred from direct assay PubMed 19158679. Source: MGI

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

interleukin-1 beta secretion

Inferred from sequence orthology PubMed 19158679. Source: MGI

negative regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cysteine-type endopeptidase activity

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of defense response to virus by host

Inferred from mutant phenotype Ref.5. Source: UniProtKB

positive regulation of interleukin-1 beta production

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of interleukin-1 beta secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein oligomerization

Inferred from electronic annotation. Source: Ensembl

pyroptosis

Inferred from direct assay Ref.4. Source: UniProtKB

tumor necrosis factor-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentAIM2 inflammasome complex

Inferred from direct assay PubMed 19158679. Source: MGI

cytoplasm

Inferred from direct assay PubMed 19158679. Source: MGI

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondouble-stranded DNA binding

Inferred from direct assay Ref.13. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.4. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-6253384,EBI-6253384

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Interferon-inducible protein AIM2
PRO_0000334528

Regions

Domain1 – 8787DAPIN
Domain144 – 341198HIN-200

Secondary structure

............................... 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q91VJ1 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: E860C5D902AA5D35

FASTA35440,155
        10         20         30         40         50         60 
MESEYREMLL LTGLDHITEE ELKRFKYFAL TEFQIARSTL DVADRTELAD HLIQSAGAAS 

        70         80         90        100        110        120 
AVTKAINIFQ KLNYMHIANA LEEKKKEAER KLMTNTKKRG TQKVENRSQA ENCSAASATR 

       130        140        150        160        170        180 
SDNDFKEQAA TEVCPQAKPQ KKQMVAEQEA IREDLQKDPL VVTVLKAINP FECETQEGRQ 

       190        200        210        220        230        240 
EIFHATVATE TDFFFVKVLN AQFKDKFIPK RTIKISNYLW HSNFMEVTSS SVVVDVESNH 

       250        260        270        280        290        300 
EVPNNVVKRA RETPRISKLK IQPCGTIVNG LFKVQKITEE KDRVLYGIHD KTGTMEVLVL 

       310        320        330        340        350 
GNPSKTKCEE GDKIRLTFFE VSKNGVKIQL KSGPCSFFKV IKAAKPKTDM KSVE 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-354.
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"The HIN-200 family: more than interferon-inducible genes?"
Ludlow L.E.A., Johnstone R.W., Clarke C.J.P.
Exp. Cell Res. 308:1-17(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[4]"AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA."
Fernandes-Alnemri T., Yu J.W., Datta P., Wu J., Alnemri E.S.
Nature 458:509-513(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC."
Hornung V., Ablasser A., Charrel-Dennis M., Bauernfeind F., Horvath G., Caffrey D.R., Latz E., Fitzgerald K.A.
Nature 458:514-518(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA."
Roberts T.L., Idris A., Dunn J.A., Kelly G.M., Burnton C.M., Hodgson S., Hardy L.L., Garceau V., Sweet M.J., Ross I.L., Hume D.A., Stacey K.J.
Science 323:1057-1060(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol."
Sauer J.D., Witte C.E., Zemansky J., Hanson B., Lauer P., Portnoy D.A.
Cell Host Microbe 7:412-419(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The AIM2 inflammasome is critical for innate immunity to Francisella tularensis."
Fernandes-Alnemri T., Yu J.W., Juliana C., Solorzano L., Kang S., Wu J., Datta P., McCormick M., Huang L., McDermott E., Eisenlohr L., Landel C.P., Alnemri E.S.
Nat. Immunol. 11:385-393(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses."
Rathinam V.A., Jiang Z., Waggoner S.N., Sharma S., Cole L.E., Waggoner L., Vanaja S.K., Monks B.G., Ganesan S., Latz E., Hornung V., Vogel S.N., Szomolanyi-Tsuda E., Fitzgerald K.A.
Nat. Immunol. 11:395-402(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Absent in melanoma 2 is required for innate immune recognition of Francisella tularensis."
Jones J.W., Kayagaki N., Broz P., Henry T., Newton K., O'Rourke K., Chan S., Dong J., Qu Y., Roose-Girma M., Dixit V.M., Monack D.M.
Proc. Natl. Acad. Sci. U.S.A. 107:9771-9776(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages."
Pierini R., Juruj C., Perret M., Jones C.L., Mangeot P., Weiss D.S., Henry T.
Cell Death Differ. 19:1709-1721(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"Francisella infection triggers activation of the AIM2 inflammasome in murine dendritic cells."
Belhocine K., Monack D.M.
Cell. Microbiol. 14:71-80(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Structural basis for termination of AIM2-mediated signaling by p202."
Ru H., Ni X., Zhao L., Crowley C., Ding W., Hung L.W., Shaw N., Cheng G., Liu Z.J.
Cell Res. 23:855-858(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 158-349 IN COMPLEX WITH DNA, FUNCTION, DOMAIN, DNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC084073 Genomic DNA. No translation available.
BC009664 mRNA. Translation: AAH09664.1. Different initiation.
RefSeqNP_001013801.2. NM_001013779.2.
XP_006496978.1. XM_006496915.1.
XP_006496979.1. XM_006496916.1.
XP_006496980.1. XM_006496917.1.
XP_006496981.1. XM_006496918.1.
XP_006496982.1. XM_006496919.1.
XP_006496983.1. XM_006496920.1.
XP_006496984.1. XM_006496921.1.
XP_006496985.1. XM_006496922.1.
XP_006496986.1. XM_006496923.1.
XP_006496987.1. XM_006496924.1.
XP_006496988.1. XM_006496925.1.
XP_006496989.1. XM_006496926.1.
UniGeneMm.131453.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4JBMX-ray2.22A/B158-349[»]
ProteinModelPortalQ91VJ1.
SMRQ91VJ1. Positions 1-97, 158-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91VJ1. 2 interactions.
STRING10090.ENSMUSP00000119465.

PTM databases

PhosphoSiteQ91VJ1.

Proteomic databases

PRIDEQ91VJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000147604; ENSMUSP00000119465; ENSMUSG00000037860.
ENSMUST00000166137; ENSMUSP00000132253; ENSMUSG00000037860.
GeneID383619.
KEGGmmu:383619.
UCSCuc011wws.1. mouse.

Organism-specific databases

CTD9447.
MGIMGI:2686159. Aim2.

Phylogenomic databases

eggNOGNOG132015.
GeneTreeENSGT00390000013296.
HOVERGENHBG006122.
KOK12966.
OMAFQKLNYM.
OrthoDBEOG78H3TT.
PhylomeDBQ91VJ1.
TreeFamTF337385.

Enzyme and pathway databases

ReactomeREACT_98458. Immune System.

Gene expression databases

BgeeQ91VJ1.
GenevestigatorQ91VJ1.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
2.40.50.140. 2 hits.
InterProIPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF02760. HIN. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50824. DAPIN. 1 hit.
PS50834. HIN_200. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio404044.
PROQ91VJ1.
SOURCESearch...

Entry information

Entry nameAIM2_MOUSE
AccessionPrimary (citable) accession number: Q91VJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: April 16, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot