A0A484CL50 · A0A484CL50_PERFV
- ProteinProtein argonaute-2
- GeneAGO2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids872 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include ago2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by ago2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur.
Catalytic activity
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | P-body | |
Cellular Component | RISC complex | |
Molecular Function | endoribonuclease activity, cleaving siRNA-paired mRNA | |
Molecular Function | metal ion binding | |
Molecular Function | miRNA binding | |
Molecular Function | mRNA cap binding | |
Molecular Function | RNA 7-methylguanosine cap binding | |
Molecular Function | single-stranded RNA binding | |
Molecular Function | siRNA binding | |
Biological Process | miRNA-mediated gene silencing by inhibition of translation | |
Biological Process | miRNA-mediated gene silencing by mRNA destabilization | |
Biological Process | negative regulation of translational initiation | |
Biological Process | pre-miRNA processing | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein argonaute-2
- EC number
- Short namesArgonaute2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Percoidei > Percidae > Percinae > Perca
Accessions
- Primary accessionA0A484CL50
Proteomes
Subcellular Location
Interaction
Subunit
Component of the RISC loading complex (RLC), or micro-RNA (miRNA) loading complex (miRLC), which is composed of dicer1, ago2 and tarbp2. Note that the trimeric RLC/miRLC is also referred to as RISC.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-26 | Polar residues | ||||
Sequence: MYSSAGVTEMQEGPRSSGSTGSDPPS | ||||||
Region | 1-39 | Disordered | ||||
Sequence: MYSSAGVTEMQEGPRSSGSTGSDPPSSPVPEYVFKPPSR | ||||||
Domain | 240-359 | PAZ | ||||
Sequence: PVIEFMCEVLDFKSIEEQQKPLTDSQRVKFTKEIKGLKVEITHCGQMKRKYRVCNVTRRPASHQTFPLQQENGQTIECTVAQYFKDKYKLILRYPHLPCLQVGQEQKHTYLPLEVCNIVA | ||||||
Domain | 528-831 | Piwi | ||||
Sequence: LVVVILPGKTPVYAEVKRVGDTVLGMATQCVQVKNVQKTTPQTLSNLCLKINVKLGGVNNILLPQGRPLVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPSRYCATVRVQQHRQDIIQDLATMVRELLIQFYKSTRFKPTRIIYYRDGISEGQFNQMQVLQHELLAIREACIKLEKDYQPGITFVVVQKRHHTRLFCMDRNERVGKSGNIPAGTTVDTKITHPSEFDFYLCSHAGIQGTSRPSHYHVLWDDNHFSSDELQVLTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLV | ||||||
Region | 835-856 | Disordered | ||||
Sequence: HDSAEGSHTSGQSNGRDQQALA |
Domain
The Piwi domain may perform RNA cleavage by a mechanism similar to that of RNase H. However, while RNase H utilizes a triad of Asp-Asp-Glu (DDE) for metal ion coordination, this protein appears to utilize a triad of Asp-Asp-His (DDH).
Sequence similarities
Belongs to the argonaute family. Ago subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length872
- Mass (Da)98,948
- Last updated2019-06-05 v1
- Checksum7635E3015518BEC7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-26 | Polar residues | ||||
Sequence: MYSSAGVTEMQEGPRSSGSTGSDPPS |
Keywords
- Technical term