Q8VZG7 · TSN1_ARATH
- ProteinRibonuclease TUDOR 1
- GeneTSN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids991 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cytoprotective ribonuclease (RNase) required for resistance to abiotic stresses, acting as a positive regulator of mRNA decapping during stress (PubMed:25736060).
Essential for the integrity and function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes called stress granules (SGs) and processing bodies (PBs), sites of post-transcriptional gene regulation during stress (e.g. salt and heat) (PubMed:25736060).
Involved in gibberellic acid (GA) biosynthesis (PubMed:25205572).
Essential for stress tolerance, probably by regulating mRNAs entering the secretory pathway (PubMed:20484005).
Component of stress granules (SGs) that regulates growth under salt stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3 mRNA (PubMed:25205572).
May inhibit the degradation of mRNAs involved in stress adaptation (PubMed:26237081).
Essential for the integrity and function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes called stress granules (SGs) and processing bodies (PBs), sites of post-transcriptional gene regulation during stress (e.g. salt and heat) (PubMed:25736060).
Involved in gibberellic acid (GA) biosynthesis (PubMed:25205572).
Essential for stress tolerance, probably by regulating mRNAs entering the secretory pathway (PubMed:20484005).
Component of stress granules (SGs) that regulates growth under salt stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3 mRNA (PubMed:25205572).
May inhibit the degradation of mRNAs involved in stress adaptation (PubMed:26237081).
Activity regulation
Repressed by the specific inhibitor 3',5'-deoxythymidine bisphosphate (pdTp); this RNase activity inhibition impairs subcellular relocation upon abiotic stress and leads to reduced stress resistance.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic stress granule | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | nuclear envelope | |
Cellular Component | P-body | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plant-type cell wall | |
Cellular Component | plasma membrane | |
Cellular Component | RNAi effector complex | |
Molecular Function | mRNA binding | |
Molecular Function | nuclease activity | |
Molecular Function | RNA binding | |
Biological Process | cellular response to heat | |
Biological Process | mRNA catabolic process | |
Biological Process | mRNA processing | |
Biological Process | positive regulation of gibberellin biosynthetic process | |
Biological Process | regulatory ncRNA-mediated gene silencing | |
Biological Process | response to salt stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease TUDOR 1
- EC number
- Short namesAtTudor1 ; TUDOR-SN protein 1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8VZG7
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Accumulates heterogeneously in the cytosol, in patches around the nucleus and in the cell periphery, and relocates transiently to a diffuse pattern in response to salt stress (PubMed:20484005).
Accumulates in cytoplasmic stress granules (SGs) and processing bodies (PBs) in response to abiotic stresses (e.g. salt and heat) (PubMed:25205572, PubMed:25736060).
Accumulates in cytoplasmic stress granules (SGs) and processing bodies (PBs) in response to abiotic stresses (e.g. salt and heat) (PubMed:25205572, PubMed:25736060).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Normal vegetative growth, flowering time and flower morphology (PubMed:20396901).
Reduced expression of enzyme involved in GA biosynthesis leading to reduced levels of GA-4 (e.g. GA20OX3). Slower growth in salt conditions (PubMed:25205572).
The double mutant tsn1 tsn2 exhibits severe alteration in germination, growth, and survival under high salinity stress. Reduced levels of stress-regulated mRNAs encoding secreted proteins (PubMed:20484005).
Abnormal stress granules (SGs) and processing bodies (PBs) assembly accompanied by reduced uncapped RNAs levels in heat-stressed double mutant tsn1 tsn2 (PubMed:25736060).
The double mutant tsn1 tsn2 is also showing enriched uncapping and subsequent degradation of mRNAs involved in stress adaptation (PubMed:26237081).
Reduced expression of enzyme involved in GA biosynthesis leading to reduced levels of GA-4 (e.g. GA20OX3). Slower growth in salt conditions (PubMed:25205572).
The double mutant tsn1 tsn2 exhibits severe alteration in germination, growth, and survival under high salinity stress. Reduced levels of stress-regulated mRNAs encoding secreted proteins (PubMed:20484005).
Abnormal stress granules (SGs) and processing bodies (PBs) assembly accompanied by reduced uncapped RNAs levels in heat-stressed double mutant tsn1 tsn2 (PubMed:25736060).
The double mutant tsn1 tsn2 is also showing enriched uncapping and subsequent degradation of mRNAs involved in stress adaptation (PubMed:26237081).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 43 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000437883 | 2-991 | Ribonuclease TUDOR 1 | |||
Sequence: ATGAENQWLKGRVKAVTSGDCLVITALSHNRAGPPPEKTITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVAFKVDYKVEAIAGREFGSVFLGNENLAKLVVKTGWAKVREPGQQNQDKVSPYIKELLQLEELAKQEGYGRWSKVPGAAEASIRNLPPSAIGDSAGFDAMGLLAANKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVFVAGVQAPSMGRRTTNGSVVETVPDEPNGDVSAESRGPLTTAQRLAASAASSVEVSSDPFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGETVKDLGLELVENGLAKFVEWSANMMEEEAKKKLKAAELQCKKDKVKMWANYVPPATNSKAIHDQNFTGKVVEVVSGDCLIVADDAVPFGSPAAERRVCLSSIRSPKMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQMEYSRKVTQGDGPTTSGAADRFMDFGSVFLPSAAKADSDEVTAPPAAAIAGSQPVGVNIAELVLVRGFGNVVRHRDFEERSNHYDALLAAEARALAGKKGIHSAKESPAMHITDLTVSAAKKAKDFLPSLQRIRRIPAVVEYVLSGHRFKLYIPKITCSIAFSFSGVRCPGRGEPYSEEAISVMRRRIMQRDVEIEVETVDRTGTFLGSMWESRTNVATVLLEAGLAKMQTSFGADRIAEAHLLEQAERSAKNQKLKIWENYVEGEEVSNGNTNTVETRQKETLKVVVTEVLGGGRFYVQSAGDQKIASIQNQLASLSIKDAPIIGSFNPKRGDIVLAQFSLDNSWNRAMIVTAPRAAVQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYIKVPSLEDDFGPEAGEYLHTVTLGSGKEFKAVIEERDTSGGKVKGQGTGTEFVVTLIAVDDEISVNAAMLQEGIARMEKRQKWGHKGKQAALDALEKFQEEARKSRIGIWQYGDIESDDEDTGPARKPAGGRR | ||||||
Modified residue | 970 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 975 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 980 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-151 | TNase-like 1 | ||||
Sequence: QWLKGRVKAVTSGDCLVITALSHNRAGPPPEKTITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVAFKVDYKVEAIAGREFGSVFLGNENLAKLVVKTGWAKVREPGQQNQDKVSPYIKELLQLEELAKQEGYGRWSK | ||||||
Domain | 186-364 | TNase-like 2 | ||||
Sequence: KPMEGIVEQVRDGSTIRVYLLPEFQFVQVFVAGVQAPSMGRRTTNGSVVETVPDEPNGDVSAESRGPLTTAQRLAASAASSVEVSSDPFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGETVKDLGLELVENGLAKFVEWSANMMEEEAKKKLKAAELQCKKDKVKMWAN | ||||||
Region | 227-250 | Disordered | ||||
Sequence: RTTNGSVVETVPDEPNGDVSAESR | ||||||
Domain | 378-557 | TNase-like 3 | ||||
Sequence: QNFTGKVVEVVSGDCLIVADDAVPFGSPAAERRVCLSSIRSPKMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQMEYSRKVTQGDGPTTSGAADRFMDFGSVFLPSAAKADSDEVTAPPAAAIAGSQPVGVNIAELVLVRGFGNVVRHRDFEERSNHYDALLAAEARALAGKKGIHSA | ||||||
Domain | 587-714 | TNase-like 4 | ||||
Sequence: RRIPAVVEYVLSGHRFKLYIPKITCSIAFSFSGVRCPGRGEPYSEEAISVMRRRIMQRDVEIEVETVDRTGTFLGSMWESRTNVATVLLEAGLAKMQTSFGADRIAEAHLLEQAERSAKNQKLKIWEN | ||||||
Domain | 782-847 | Tudor | ||||
Sequence: NPKRGDIVLAQFSLDNSWNRAMIVTAPRAAVQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAA | ||||||
Region | 971-991 | Disordered | ||||
Sequence: GDIESDDEDTGPARKPAGGRR | ||||||
Compositional bias | 977-991 | Basic and acidic residues | ||||
Sequence: DEDTGPARKPAGGRR |
Domain
TNase-like domains are required for relocation to cytoplasmic foci upon abiotic stresses.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8VZG7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length991
- Mass (Da)108,235
- Last updated2002-03-01 v1
- Checksum4192E2F57B896010
Q8VZG7-2
- Name2
- Differences from canonical
- 990-991: RR → LEIRGSLNHAYKQKKSRD
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 977-991 | Basic and acidic residues | ||||
Sequence: DEDTGPARKPAGGRR | ||||||
Alternative sequence | VSP_058574 | 990-991 | in isoform 2 | |||
Sequence: RR → LEIRGSLNHAYKQKKSRD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL163912 EMBL· GenBank· DDBJ | CAB87924.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002688 EMBL· GenBank· DDBJ | AED91140.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED91141.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY064975 EMBL· GenBank· DDBJ | AAL57629.1 EMBL· GenBank· DDBJ | mRNA |