Q60462 · IFIT2_CRIGR

Function

function

IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Molecular FunctionRNA binding
Biological Processapoptotic process
Biological Processdefense response to virus
Biological Processinnate immune response
Biological Processpositive regulation of apoptotic process
Biological Processresponse to virus

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Interferon-induced protein with tetratricopeptide repeats 2
  • Short names
    IFIT-2
  • Alternative names
    • CL-54 K
    • Interferon-induced 54 kDa protein (IFI-54K)

Gene names

    • Name
      IFIT2
    • Synonyms
      IFI54

Organism names

Accessions

  • Primary accession
    Q60462

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylserine
ChainPRO_00001063462-468Interferon-induced protein with tetratricopeptide repeats 2

Keywords

Proteomic databases

Expression

Induction

By interferons.

Interaction

Subunit

Domain-swapped homodimer. Component of an interferon-dependent multiprotein complex, at least composed of IFIT1, IFIT2 and IFIT3. Interacts with IFIT1 and IFIT3 (By similarity).
Interacts with STING1/MITA and disrupts its interaction with MAVS or TBK1 (By similarity).
Interacts with EIF3E and EIF3C (By similarity).

Structure

Family & Domains

Features

Showing features for repeat, region.

Type
IDPosition(s)Description
Repeat51-89TPR 1
Repeat90-135TPR 2
Repeat136-171TPR 3
Repeat172-208TPR 4
Repeat242-275TPR 5
Repeat276-328TPR 6
Repeat329-359TPR 7
Repeat360-398TPR 8
Repeat399-441TPR 9
Region441-468Disordered

Domain

The C-terminal part folds into a super-helical structure and has an extensively positively-charged nucleotide-binding channel on its inner surface.

Sequence similarities

Belongs to the IFIT family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    468
  • Mass (Da)
    55,046
  • Last updated
    1996-11-01 v1
  • Checksum
    9D92B878F81B1E27
MSTTTKKSLESKLQQLKCHFTWNLMAGDESLDEFEDKVFNKDEFQKRECKATMCNILAFVKHRRGQNASALKELEKAEQFIQQQHPDHVEIRNIVTWGNYAWVYYHMGQLEKAQAYLDKVRQVCEKFSSPYRIESPELDCEEGWARLKCTRNQNERVKVCFEKALEKDPKNPEFTSGWAISNYRLDFWPAQQNAVDSLKQAIRMSPNSPYVKVLLALKLEMNQENQGKELVEEALREAPGETDVLRSAARFYYKTHDKDRAIQLLSQALELLPNNAYVYYYIGCFYRSKVLQIDSRRETSQNENREQLLKQAIYYLKKAEETKEMIKDSCSYLAHLYVLAEQYKEADYYFQKGFKKELTPGLKQLLHLRYGNFQFFQMKCEDKAIHQYLEGVKIRQKTKPKEKMTNKLRFIAERRRSQNGFDSKALHILAFLQELNKESQQAAKVSERGQDSERPVFSPSLHEGGNEQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X77259
EMBL· GenBank· DDBJ
CAA54477.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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