Q8S8E3 · PYL6_ARATH
- ProteinAbscisic acid receptor PYL6
- GenePYL6
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids215 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) in an ABA-independent manner but more efficiently when activated by ABA (PubMed:21658606, PubMed:23844015).
Can be activated by both --ABA and +-ABA (PubMed:23844015).
May link ABA and jasmonate signaling pathways by modifying MYC2 transcriptional activity, and regulation of JAZ6 and JAZ8 gene expression by MYC2 (PubMed:27357749).
Can be activated by both --ABA and +-ABA (PubMed:23844015).
May link ABA and jasmonate signaling pathways by modifying MYC2 transcriptional activity, and regulation of JAZ6 and JAZ8 gene expression by MYC2 (PubMed:27357749).
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 90 | abscisate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 119 | Involved in interactions with PP2Cs | ||||
Sequence: P | ||||||
Binding site | 120-125 | abscisate (UniProtKB | ChEBI) | ||||
Sequence: AAFSLE | ||||||
Binding site | 147-153 | abscisate (UniProtKB | ChEBI) | ||||
Sequence: RLMNYKS | ||||||
Binding site | 174 | abscisate (UniProtKB | ChEBI) | ||||
Sequence: E |
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | abscisic acid binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | protein phosphatase inhibitor activity | |
Molecular Function | signaling receptor activity | |
Biological Process | abscisic acid-activated signaling pathway | |
Biological Process | jasmonic acid mediated signaling pathway |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAbscisic acid receptor PYL6
- 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 accessionQ8S8E3
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes at the plasma membrane in the presence of a CAR protein (e.g. CAR1 and CAR4).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions, but mutant seedlings exhibit increased sensitivity to abscisic acid-induced inhibition of cotyledon expansion. The inhibition effect is more severe with the combination of abscisic acid and jasmonate.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000391741 | 1-215 | Abscisic acid receptor PYL6 | |||
Sequence: MPTSIQFQRSSTAAEAANATVRNYPHHHQKQVQKVSLTRGMADVPEHVELSHTHVVGPSQCFSVVVQDVEAPVSTVWSILSRFEHPQAYKHFVKSCHVVIGDGREVGSVREVRVVSGLPAAFSLERLEIMDDDRHVISFSVVGGDHRLMNYKSVTTVHESEEDSDGKKRTRVVESYVVDVPAGNDKEETCSFADTIVRCNLQSLAKLAENTSKFS | ||||||
Disulfide bond | 61↔190 | Reversible | ||||
Sequence: CFSVVVQDVEAPVSTVWSILSRFEHPQAYKHFVKSCHVVIGDGREVGSVREVRVVSGLPAAFSLERLEIMDDDRHVISFSVVGGDHRLMNYKSVTTVHESEEDSDGKKRTRVVESYVVDVPAGNDKEETC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Monomer (PubMed:21658606).
Homodimer. Binds ABA on one subunit only (By similarity).
Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs (PubMed:19624469, PubMed:19874541, PubMed:19898420).
Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus. Interacts directly with CAR1 and CAR4 (PubMed:25465408).
Interacts with MYC2 in the nucleus. Interaction with MYC2 is increased in the presence of abscisic acid (PubMed:27357749).
Homodimer. Binds ABA on one subunit only (By similarity).
Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs (PubMed:19624469, PubMed:19874541, PubMed:19898420).
Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus. Interacts directly with CAR1 and CAR4 (PubMed:25465408).
Interacts with MYC2 in the nucleus. Interaction with MYC2 is increased in the presence of abscisic acid (PubMed:27357749).
Binary interactions
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 54-209 | START-like | ||||
Sequence: HVVGPSQCFSVVVQDVEAPVSTVWSILSRFEHPQAYKHFVKSCHVVIGDGREVGSVREVRVVSGLPAAFSLERLEIMDDDRHVISFSVVGGDHRLMNYKSVTTVHESEEDSDGKKRTRVVESYVVDVPAGNDKEETCSFADTIVRCNLQSLAKLAE | ||||||
Motif | 116-120 | Gate loop | ||||
Sequence: SGLPA | ||||||
Motif | 146-148 | Latch loop | ||||
Sequence: HRL |
Domain
Upon interaction with ABA, the 'latch' and 'gate' loops change in conformation leading to a tight dimerization and the creation a surface that enables the receptor to dock into and inhibit the PP2C active site.
Sequence similarities
Belongs to the PYR/PYL/RCAR abscisic acid intracellular receptor family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length215
- Mass (Da)23,843
- Last updated2002-06-01 v1
- Checksum8B9D3F7BD9E2860D
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF085279 EMBL· GenBank· DDBJ | AAD25950.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AC007020 EMBL· GenBank· DDBJ | AAD25668.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC09815.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT004281 EMBL· GenBank· DDBJ | AAO42281.1 EMBL· GenBank· DDBJ | mRNA | ||
BT005608 EMBL· GenBank· DDBJ | AAO64028.1 EMBL· GenBank· DDBJ | mRNA | ||
AY088453 EMBL· GenBank· DDBJ | AAM65989.1 EMBL· GenBank· DDBJ | mRNA |