Q1ECF1 · PYL7_ARATH
- ProteinAbscisic acid receptor PYL7
- GenePYL7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids211 (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) when activated by ABA.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 65 | abscisate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 66 | Involved in ABA binding | ||||
Sequence: P | ||||||
Site | 92 | Involved in interactions with PP2Cs | ||||
Sequence: P | ||||||
Binding site | 93-98 | abscisate (UniProtKB | ChEBI) | ||||
Sequence: ATTSTE | ||||||
Site | 112 | Involved in ABA binding | ||||
Sequence: I | ||||||
Binding site | 120-126 | abscisate (UniProtKB | ChEBI) | ||||
Sequence: RLKNYSS | ||||||
Binding site | 145 | abscisate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 156 | Involved in interactions with PP2Cs | ||||
Sequence: T | ||||||
Site | 164 | Involved in ABA binding | ||||
Sequence: V | ||||||
Site | 167 | Involved in ABA binding | ||||
Sequence: L |
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 | 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 |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameAbscisic acid receptor PYL7
- 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 accessionQ1ECF1
- 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.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000391742 | 1-211 | Abscisic acid receptor PYL7 | |||
Sequence: MEMIGGDDTDTEMYGALVTAQSLRLRHLHHCRENQCTSVLVKYIQAPVHLVWSLVRRFDQPQKYKPFISRCTVNGDPEIGCLREVNVKSGLPATTSTERLEQLDDEEHILGINIIGGDHRLKNYSSILTVHPEMIDGRSGTMVMESFVVDVPQGNTKDDTCYFVESLIKCNLKSLACVSERLAAQDITNSIATFCNASNGYREKNHTETNL | ||||||
Disulfide bond | 31↔161 | Reversible | ||||
Sequence: CRENQCTSVLVKYIQAPVHLVWSLVRRFDQPQKYKPFISRCTVNGDPEIGCLREVNVKSGLPATTSTERLEQLDDEEHILGINIIGGDHRLKNYSSILTVHPEMIDGRSGTMVMESFVVDVPQGNTKDDTC | ||||||
Disulfide bond | 36↔161 | Reversible | ||||
Sequence: CTSVLVKYIQAPVHLVWSLVRRFDQPQKYKPFISRCTVNGDPEIGCLREVNVKSGLPATTSTERLEQLDDEEHILGINIIGGDHRLKNYSSILTVHPEMIDGRSGTMVMESFVVDVPQGNTKDDTC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer. Binds ABA on one subunit only. Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus (By similarity).
Interacts with ABI1, and possibly with other PP2Cs (PubMed:19874541).
Interacts with ABI1, and possibly with other PP2Cs (PubMed:19874541).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q1ECF1 | ABI1 P49597 | 5 | EBI-2363203, EBI-782526 | |
BINARY | Q1ECF1 | AIP1 Q9LNW3 | 7 | EBI-2363203, EBI-1573499 | |
BINARY | Q1ECF1 | At1g72340 A0A1P8AVS2 | 3 | EBI-2363203, EBI-25528474 | |
BINARY | Q1ECF1 | At2g29380 Q9ZW21 | 5 | EBI-2363203, EBI-4441103 | |
BINARY | Q1ECF1 | HAB1 Q9CAJ0 | 4 | EBI-2363203, EBI-2309302 | |
BINARY | Q1ECF1 | HAB2 Q9LNP9 | 3 | EBI-2363203, EBI-15803614 | |
BINARY | Q1ECF1 | NAC089 Q94F58 | 3 | EBI-2363203, EBI-2319707 | |
BINARY | Q1ECF1 | TCP19 Q9LT89 | 3 | EBI-2363203, EBI-4426178 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 29-180 | START-like | ||||
Sequence: HHCRENQCTSVLVKYIQAPVHLVWSLVRRFDQPQKYKPFISRCTVNGDPEIGCLREVNVKSGLPATTSTERLEQLDDEEHILGINIIGGDHRLKNYSSILTVHPEMIDGRSGTMVMESFVVDVPQGNTKDDTCYFVESLIKCNLKSLACVSE | ||||||
Motif | 89-93 | Gate loop | ||||
Sequence: SGLPA | ||||||
Motif | 119-121 | 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
- Length211
- Mass (Da)23,676
- Last updated2006-07-11 v1
- Checksum6381793C94A43C32
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL080237 EMBL· GenBank· DDBJ | CAB45785.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161491 EMBL· GenBank· DDBJ | CAB80911.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE81969.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT025783 EMBL· GenBank· DDBJ | ABF83673.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087511 EMBL· GenBank· DDBJ | AAM65054.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |