Q5XET5 · HESO1_ARATH
- ProteinProtein HESO1
- GeneHESO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids511 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Uridylates small RNAs to trigger their degradation (PubMed:22464191, PubMed:22464194, PubMed:25928341).
Catalyzes the uridylation of 5' fragments produced by AGO1-mediated cleavage of miRNA target RNAs (PubMed:24733911).
Acts synergistically with URT1 in unmethylated miRNA uridylation, leading to their degradation (PubMed:25928341).
URT1 and HESO1 prefer substrates with different 3' end nucleotides and act cooperatively to tail different forms of the same miRNAs (PubMed:25928405).
URT1 and HESO1 act sequentially, with URT1 mono-uridylating the miRNAs followed by their further uridylation by HESO1 (PubMed:25928405).
URT1 and HESO1 are involved in the uridylation and clearance of RISC-generated 5' mRNA fragments (PubMed:30364210).
Able to act on AGO1-bound miRNAs and the uridylated species stay associated with AGO1 (PubMed:24733911, PubMed:25928405).
Catalyzes the uridylation of 5' fragments produced by AGO1-mediated cleavage of miRNA target RNAs (PubMed:24733911).
Acts synergistically with URT1 in unmethylated miRNA uridylation, leading to their degradation (PubMed:25928341).
URT1 and HESO1 prefer substrates with different 3' end nucleotides and act cooperatively to tail different forms of the same miRNAs (PubMed:25928405).
URT1 and HESO1 act sequentially, with URT1 mono-uridylating the miRNAs followed by their further uridylation by HESO1 (PubMed:25928405).
URT1 and HESO1 are involved in the uridylation and clearance of RISC-generated 5' mRNA fragments (PubMed:30364210).
Able to act on AGO1-bound miRNAs and the uridylated species stay associated with AGO1 (PubMed:24733911, PubMed:25928405).
Catalytic activity
- RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide
RNA(n) RHEA-COMP:14527 + CHEBI:46398 = CHEBI:33019 + RNA(n)-3'-uridine ribonucleotide RHEA-COMP:17348
Activity regulation
Completely inhibited by 2'-O-methylation on the substrate RNA.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | P-body | |
Molecular Function | nucleotidyltransferase activity | |
Molecular Function | RNA uridylyltransferase activity | |
Biological Process | miRNA catabolic process | |
Biological Process | RNA 3' uridylation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein HESO1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ5XET5
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No effect on miRNA accumulation in the wild-type background, but increased abundance of the heterogeneous miRNA species in a hen1 background. Reduced 3' uridylation of miRNAs without affecting the 3' truncation.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 40 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000434143 | 1-511 | Protein HESO1 | |||
Sequence: MSRNPFLDPTLQEILQVIKPTRADRDTRITVIDQLRDVLQSVECLRGATVQPFGSFVSNLFTRWGDLDISVDLFSGSSILFTGKKQKQTLLGHLLRALRASGLWYKLQFVIHARVPILKVVSGHQRISCDISIDNLDGLLKSRFLFWISEIDGRFRDLVLLVKEWAKAHNINDSKTGTFNSYSLSLLVIFHFQTCVPAILPPLRVIYPKSAVDDLTGVRKTAEESIAQVTAANIARFKSERAKSVNRSSLSELLVSFFAKFSDINVKAQEFGVCPFTGRWETISSNTTWLPKTYSLFVEDPFEQPVNAARSVSRRNLDRIAQVFQITSRRLVSECNRNSIIGILTGQHIQESLYRTISLPSQHHANGMHNVRNLHGQARPQNQQMQQNWSQSYNTPNPPHWPPLTQSRPQQNWTQNNPRNLQGQPPVQGQTWPVITQTQTQQKSPYKSGNRPLKNTSAGSSQNQGHIGKPSGHMNGVNSARPAYTNGVNSARPPSKIPSQGGQIWRPRHEQ |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 378-395 | Polar residues | ||||
Sequence: ARPQNQQMQQNWSQSYNT | ||||||
Region | 378-511 | Disordered | ||||
Sequence: ARPQNQQMQQNWSQSYNTPNPPHWPPLTQSRPQQNWTQNNPRNLQGQPPVQGQTWPVITQTQTQQKSPYKSGNRPLKNTSAGSSQNQGHIGKPSGHMNGVNSARPAYTNGVNSARPPSKIPSQGGQIWRPRHEQ | ||||||
Compositional bias | 406-469 | Polar residues | ||||
Sequence: QSRPQQNWTQNNPRNLQGQPPVQGQTWPVITQTQTQQKSPYKSGNRPLKNTSAGSSQNQGHIGK | ||||||
Compositional bias | 478-497 | Polar residues | ||||
Sequence: NSARPAYTNGVNSARPPSKI |
Sequence similarities
Belongs to the DNA polymerase type-B-like family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length511
- Mass (Da)57,592
- Last updated2004-11-23 v1
- Checksum9071261E200B77B1
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 89 | in Ref. 4; BAE99845 | ||||
Sequence: T → I | ||||||
Compositional bias | 378-395 | Polar residues | ||||
Sequence: ARPQNQQMQQNWSQSYNT | ||||||
Compositional bias | 406-469 | Polar residues | ||||
Sequence: QSRPQQNWTQNNPRNLQGQPPVQGQTWPVITQTQTQQKSPYKSGNRPLKNTSAGSSQNQGHIGK | ||||||
Compositional bias | 478-497 | Polar residues | ||||
Sequence: NSARPAYTNGVNSARPPSKI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC003000 EMBL· GenBank· DDBJ | AAB87123.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002685 EMBL· GenBank· DDBJ | AEC09717.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | ANM62240.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | ANM62241.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT015881 EMBL· GenBank· DDBJ | AAU95417.1 EMBL· GenBank· DDBJ | mRNA | ||
BT020198 EMBL· GenBank· DDBJ | AAV59264.1 EMBL· GenBank· DDBJ | mRNA | ||
AK227869 EMBL· GenBank· DDBJ | BAE99845.1 EMBL· GenBank· DDBJ | mRNA |