Q60462 · IFIT2_CRIGR
- ProteinInterferon-induced protein with tetratricopeptide repeats 2
- GeneIFIT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids468 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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 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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Molecular Function | RNA binding | |
Biological Process | apoptotic process | |
Biological Process | defense response to virus | |
Biological Process | innate immune response | |
Biological Process | positive regulation of apoptotic process | |
Biological Process | response to virus |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameInterferon-induced protein with tetratricopeptide repeats 2
- Short namesIFIT-2
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Cricetidae > Cricetinae > Cricetulus
Accessions
- Primary accessionQ60462
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Modified residue | 2 | N-acetylserine | |||
Chain | PRO_0000106346 | 2-468 | Interferon-induced protein with tetratricopeptide repeats 2 | ||
Keywords
- PTM
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).
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Repeat | 51-89 | TPR 1 | |||
Repeat | 90-135 | TPR 2 | |||
Repeat | 136-171 | TPR 3 | |||
Repeat | 172-208 | TPR 4 | |||
Repeat | 242-275 | TPR 5 | |||
Repeat | 276-328 | TPR 6 | |||
Repeat | 329-359 | TPR 7 | |||
Repeat | 360-398 | TPR 8 | |||
Repeat | 399-441 | TPR 9 | |||
Region | 441-468 | Disordered | |||
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length468
- Mass (Da)55,046
- Last updated1996-11-01 v1
- Checksum9D92B878F81B1E27
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X77259 EMBL· GenBank· DDBJ | CAA54477.1 EMBL· GenBank· DDBJ | Genomic DNA |