Q06738 · RD29A_ARATH
- ProteinLow-temperature-induced 78 kDa protein
- GeneRD29A
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids710 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in responses to abiotic stresses (PubMed:21374086).
Regulates probably root elongation in cold conditions (PubMed:19470100).
Regulates probably root elongation in cold conditions (PubMed:19470100).
Biotechnology
The cold-inducible promoter of RD29A can be used to improve chill-resistance of crops by triggering the expression of given genes in low temperature conditions (e.g. potato low temperature sweetening).
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 | cytosol | |
Cellular Component | plastid | |
Biological Process | circadian rhythm | |
Biological Process | hyperosmotic salinity response | |
Biological Process | leaf senescence | |
Biological Process | regulation of root development | |
Biological Process | response to abscisic acid | |
Biological Process | response to cold | |
Biological Process | response to mannitol | |
Biological Process | response to osmotic stress | |
Biological Process | response to reactive oxygen species | |
Biological Process | response to salt | |
Biological Process | response to salt stress | |
Biological Process | response to symbiotic bacterium | |
Biological Process | response to water deprivation | |
Biological Process | response to wounding |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameLow-temperature-induced 78 kDa protein
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ06738
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Enhanced root growth, photosynthesis and water use efficiency (WUE) under salt stress.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 76 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000084511 | 1-710 | Low-temperature-induced 78 kDa protein | |||
Sequence: MDQTEEPPLNTHQQHPEEVEHHENGATKMFRKVKARAKKFKNSLTKHGQSNEHEQDHDLVEEDDDDDELEPEVIDAPGVTGKPRETNVPASEEIIPPGTKVFPVVSSDYTKPTESVPVQEASYGHDAPAHSVRTTFTSDKEEKRDVPIHHPLSELSDREESRETHHESLNTPVSLLSGTEDVTSTFAPSGDDEYLDGQRKVNVETPITLEEESAVSDYLSGVSNYQSKVTDPTKEETGGVPEIAESFGNMEVTDESPDQKPGQFERDLSTRSKEFKEFDQDFDSVLGKDSPAKFPGESGVVFPVGFGDESGAELEKDFPTRSHDFDMKTETGMDTNSPSRSHEFDLKTESGNDKNSPMGFGSESGAELEKEFDQKNDSGRNEYSPESDGGLGAPLGGNFPVRSHELDLKNESDIDKDVPTGFDGEPDFLAKGRPGYGEASEEDKFPARSDDVEVETELGRDPKTETLDQFSPELSHPKERDEFKESRDDFEETRDEKTEEPKQSTYTEKFASMLGYSGEIPVGDQTQVAGTVDEKLTPVNEKDQETESAVTTKLPISGGGSGVEEQRGEDKSVSGRDYVAEKLTTEEEDKAFSDMVAEKLQIGGEEEKKETTTKEVEKISTEKAASEEGEAVEEEVKGGGGMVGRIKGWFGGGATDEVKPESPHSVEEAPKSSGWFGGGATEEVKPKSPHSVEESPQSLGSTVVPVQKEL | ||||||
Modified residue | 626 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Accumulates rapidly in leaves, stems, roots, flower petals, filaments, and sepals during cold-acclimation.
Induction
Levels follow a circadian cycle with higher levels during the day, in a calcium ion-dependent manner (PubMed:17227550).
Triggered by water stress, osmotic stress (e.g. salt and mannitol), diacylglycerol pyrophosphate (DGPP) and abscisic acid (ABA) (PubMed:12694590, PubMed:16463099, PubMed:16766676, PubMed:1830821, PubMed:21374086, PubMed:8148648, PubMed:8448363, PubMed:9418048).
Pretreatment with lanthanum, a calcium-channel blocker, prevents mannitol-mediated induction (PubMed:9418048).
Induced reversibly by low temperature; by both acute (2-24 hours at 4 degrees Celsius) and chronic (5-6 weeks at 10 degrees Celsius) cold treatments (PubMed:12694590, PubMed:17227550, PubMed:1830821, PubMed:19470100, PubMed:21374086, PubMed:8148648, PubMed:8290624, PubMed:8448363).
Levels are correlated with the rate of root elongation in the cold (PubMed:19470100).
Induced by the plant growth promoting rhizobacteria (PGPRs) Enterobacter sp. EJ01 (PubMed:24598995).
Triggered by WRKY8 during salt stress via direct promoter regulation in a pathway that involves PP2CG1 (PubMed:21374086, PubMed:22627139, PubMed:23451802).
Induction by salt is also ethylene-dependent, with the intervention of EIN3 that activates ESE1, the transcription regulator of the pathway (PubMed:21832142).
The salt-mediated accumulation involves reactive oxygen species (ROS), ROS-dependent induction being repressed by the NADPH oxidase inhibitor diphenylene iodonium (DPI) (PubMed:21677096).
Stimulated reversibly via histone modifications (e.g. enrichment of H3K9ac and H3K4me3) by wounding and water deprivation (PubMed:18779215, PubMed:22505693, PubMed:22983672).
Inactivated via histone modifications after rehydration (e.g. removal of H3K9ac and reduction of H3K4me3) (PubMed:22505693).
At 22 degrees Celsius, induced synergistically by osmotic stress and ABA. In cold conditions, however, impaired induction by osmotic stress but induced synergistically by cold and ABA (PubMed:9880362).
Triggered by water stress, osmotic stress (e.g. salt and mannitol), diacylglycerol pyrophosphate (DGPP) and abscisic acid (ABA) (PubMed:12694590, PubMed:16463099, PubMed:16766676, PubMed:1830821, PubMed:21374086, PubMed:8148648, PubMed:8448363, PubMed:9418048).
Pretreatment with lanthanum, a calcium-channel blocker, prevents mannitol-mediated induction (PubMed:9418048).
Induced reversibly by low temperature; by both acute (2-24 hours at 4 degrees Celsius) and chronic (5-6 weeks at 10 degrees Celsius) cold treatments (PubMed:12694590, PubMed:17227550, PubMed:1830821, PubMed:19470100, PubMed:21374086, PubMed:8148648, PubMed:8290624, PubMed:8448363).
Levels are correlated with the rate of root elongation in the cold (PubMed:19470100).
Induced by the plant growth promoting rhizobacteria (PGPRs) Enterobacter sp. EJ01 (PubMed:24598995).
Triggered by WRKY8 during salt stress via direct promoter regulation in a pathway that involves PP2CG1 (PubMed:21374086, PubMed:22627139, PubMed:23451802).
Induction by salt is also ethylene-dependent, with the intervention of EIN3 that activates ESE1, the transcription regulator of the pathway (PubMed:21832142).
The salt-mediated accumulation involves reactive oxygen species (ROS), ROS-dependent induction being repressed by the NADPH oxidase inhibitor diphenylene iodonium (DPI) (PubMed:21677096).
Stimulated reversibly via histone modifications (e.g. enrichment of H3K9ac and H3K4me3) by wounding and water deprivation (PubMed:18779215, PubMed:22505693, PubMed:22983672).
Inactivated via histone modifications after rehydration (e.g. removal of H3K9ac and reduction of H3K4me3) (PubMed:22505693).
At 22 degrees Celsius, induced synergistically by osmotic stress and ABA. In cold conditions, however, impaired induction by osmotic stress but induced synergistically by cold and ABA (PubMed:9880362).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-198 | Disordered | ||||
Sequence: MDQTEEPPLNTHQQHPEEVEHHENGATKMFRKVKARAKKFKNSLTKHGQSNEHEQDHDLVEEDDDDDELEPEVIDAPGVTGKPRETNVPASEEIIPPGTKVFPVVSSDYTKPTESVPVQEASYGHDAPAHSVRTTFTSDKEEKRDVPIHHPLSELSDREESRETHHESLNTPVSLLSGTEDVTSTFAPSGDDEYLDGQ | ||||||
Compositional bias | 11-30 | Basic and acidic residues | ||||
Sequence: THQQHPEEVEHHENGATKMF | ||||||
Compositional bias | 57-73 | Acidic residues | ||||
Sequence: HDLVEEDDDDDELEPEV | ||||||
Compositional bias | 135-167 | Basic and acidic residues | ||||
Sequence: TFTSDKEEKRDVPIHHPLSELSDREESRETHHE | ||||||
Compositional bias | 168-186 | Polar residues | ||||
Sequence: SLNTPVSLLSGTEDVTSTF | ||||||
Region | 225-269 | Disordered | ||||
Sequence: YQSKVTDPTKEETGGVPEIAESFGNMEVTDESPDQKPGQFERDLS | ||||||
Repeat | 303-316 | 1-1 | ||||
Sequence: PVGFGDESGAELEK | ||||||
Region | 303-370 | 2 X 14 AA repeats of P-[MV]-G-F-G-[DS]-E-S-G-A-E-L-E-K | ||||
Sequence: PVGFGDESGAELEKDFPTRSHDFDMKTETGMDTNSPSRSHEFDLKTESGNDKNSPMGFGSESGAELEK | ||||||
Region | 305-507 | Disordered | ||||
Sequence: GFGDESGAELEKDFPTRSHDFDMKTETGMDTNSPSRSHEFDLKTESGNDKNSPMGFGSESGAELEKEFDQKNDSGRNEYSPESDGGLGAPLGGNFPVRSHELDLKNESDIDKDVPTGFDGEPDFLAKGRPGYGEASEEDKFPARSDDVEVETELGRDPKTETLDQFSPELSHPKERDEFKESRDDFEETRDEKTEEPKQSTYT | ||||||
Compositional bias | 310-330 | Basic and acidic residues | ||||
Sequence: SGAELEKDFPTRSHDFDMKTE | ||||||
Repeat | 317-331 | 2-1 | ||||
Sequence: DFPTRSHDFDMKTET | ||||||
Region | 317-412 | 3 X 15 AA repeats of [DN]-[FS]-P-[STV]-R-S-H-[DE]-[FL]-D-[LM]-K-[NT]-E-[ST] | ||||
Sequence: DFPTRSHDFDMKTETGMDTNSPSRSHEFDLKTESGNDKNSPMGFGSESGAELEKEFDQKNDSGRNEYSPESDGGLGAPLGGNFPVRSHELDLKNES | ||||||
Repeat | 336-350 | 2-2 | ||||
Sequence: NSPSRSHEFDLKTES | ||||||
Repeat | 357-370 | 1-2 | ||||
Sequence: PMGFGSESGAELEK | ||||||
Compositional bias | 366-382 | Basic and acidic residues | ||||
Sequence: AELEKEFDQKNDSGRNE | ||||||
Repeat | 398-412 | 2-3 | ||||
Sequence: NFPVRSHELDLKNES | ||||||
Compositional bias | 404-422 | Basic and acidic residues | ||||
Sequence: HELDLKNESDIDKDVPTGF | ||||||
Compositional bias | 436-504 | Basic and acidic residues | ||||
Sequence: YGEASEEDKFPARSDDVEVETELGRDPKTETLDQFSPELSHPKERDEFKESRDDFEETRDEKTEEPKQS | ||||||
Repeat | 510-514 | 3-1 | ||||
Sequence: FASML | ||||||
Region | 510-600 | 5 X 5 AA repeats of [FV]-[ADT]-[EST]-[KM]-L | ||||
Sequence: FASMLGYSGEIPVGDQTQVAGTVDEKLTPVNEKDQETESAVTTKLPISGGGSGVEEQRGEDKSVSGRDYVAEKLTTEEEDKAFSDMVAEKL | ||||||
Repeat | 532-536 | 3-2 | ||||
Sequence: VDEKL | ||||||
Region | 537-577 | Disordered | ||||
Sequence: TPVNEKDQETESAVTTKLPISGGGSGVEEQRGEDKSVSGRD | ||||||
Repeat | 550-554 | 3-3 | ||||
Sequence: VTTKL | ||||||
Repeat | 579-583 | 3-4 | ||||
Sequence: VAEKL | ||||||
Repeat | 596-600 | 3-5 | ||||
Sequence: VAEKL | ||||||
Compositional bias | 601-635 | Basic and acidic residues | ||||
Sequence: QIGGEEEKKETTTKEVEKISTEKAASEEGEAVEEE | ||||||
Region | 601-710 | Disordered | ||||
Sequence: QIGGEEEKKETTTKEVEKISTEKAASEEGEAVEEEVKGGGGMVGRIKGWFGGGATDEVKPESPHSVEEAPKSSGWFGGGATEEVKPKSPHSVEESPQSLGSTVVPVQKEL | ||||||
Repeat | 648-670 | 4-1 | ||||
Sequence: GWFGGGATDEVKPESPHSVEEAP | ||||||
Region | 648-696 | 2 X 23 AA repeats | ||||
Sequence: GWFGGGATDEVKPESPHSVEEAPKSSGWFGGGATEEVKPKSPHSVEESP | ||||||
Repeat | 674-696 | 4-2 | ||||
Sequence: GWFGGGATEEVKPKSPHSVEESP |
Sequence similarities
Belongs to the LTI78/LTI65 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length710
- Mass (Da)77,856
- Last updated1995-11-01 v2
- Checksum9C6C8ACAE6BDF334
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-30 | Basic and acidic residues | ||||
Sequence: THQQHPEEVEHHENGATKMF | ||||||
Compositional bias | 57-73 | Acidic residues | ||||
Sequence: HDLVEEDDDDDELEPEV | ||||||
Compositional bias | 135-167 | Basic and acidic residues | ||||
Sequence: TFTSDKEEKRDVPIHHPLSELSDREESRETHHE | ||||||
Compositional bias | 168-186 | Polar residues | ||||
Sequence: SLNTPVSLLSGTEDVTSTF | ||||||
Sequence conflict | 216 | in Ref. 2; BAA02376 | ||||
Sequence: S → P | ||||||
Compositional bias | 310-330 | Basic and acidic residues | ||||
Sequence: SGAELEKDFPTRSHDFDMKTE | ||||||
Compositional bias | 366-382 | Basic and acidic residues | ||||
Sequence: AELEKEFDQKNDSGRNE | ||||||
Compositional bias | 404-422 | Basic and acidic residues | ||||
Sequence: HELDLKNESDIDKDVPTGF | ||||||
Compositional bias | 436-504 | Basic and acidic residues | ||||
Sequence: YGEASEEDKFPARSDDVEVETELGRDPKTETLDQFSPELSHPKERDEFKESRDDFEETRDEKTEEPKQS | ||||||
Sequence conflict | 491 | in Ref. 2; BAA02376 | ||||
Sequence: E → V | ||||||
Sequence conflict | 514 | in Ref. 8; CAA40826 | ||||
Sequence: L → H | ||||||
Sequence conflict | 535 | in Ref. 3; AAA32776 | ||||
Sequence: K → R | ||||||
Compositional bias | 601-635 | Basic and acidic residues | ||||
Sequence: QIGGEEEKKETTTKEVEKISTEKAASEEGEAVEEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X67671 EMBL· GenBank· DDBJ | CAA47903.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D13044 EMBL· GenBank· DDBJ | BAA02376.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22567 EMBL· GenBank· DDBJ | AAA32775.1 EMBL· GenBank· DDBJ | mRNA | ||
L22568 EMBL· GenBank· DDBJ | AAA32776.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB019226 EMBL· GenBank· DDBJ | BAB10528.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED96199.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY054465 EMBL· GenBank· DDBJ | AAK96657.1 EMBL· GenBank· DDBJ | mRNA | ||
AK221520 EMBL· GenBank· DDBJ | BAD94805.1 EMBL· GenBank· DDBJ | mRNA | ||
X57600 EMBL· GenBank· DDBJ | CAA40826.1 EMBL· GenBank· DDBJ | mRNA |