UniProt functional annotation for Q9SSM7



	UniProt functional annotation for Q9SSM7

UniProt code: Q9SSM7.

Organism: Arabidopsis thaliana (Mouse-ear cress).

Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.

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 (PubMed:22579247, PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015). {ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:22579247, ECO:0000269|PubMed:23844015}.

Subunit: Homodimer and monomer (PubMed:21658606). Binds ABA on one subunit only. ABA-binding favors monomer and trans-homodimer intermediate, and increases PP2C inhibitor activity (PubMed:22579247, PubMed:23844015). Binds both (-)-ABA and (+)-ABA (PubMed:23844015). Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus (By similarity). Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs (PubMed:19407142, PubMed:19898420, PubMed:22579247, PubMed:23844015). {ECO:0000250|UniProtKB:O49686, ECO:0000269|PubMed:19407142, ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:21658606, ECO:0000269|PubMed:22579247, ECO:0000269|PubMed:23844015}.

Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus {ECO:0000250|UniProtKB:O49686}. Cell membrane {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.

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. {ECO:0000250|UniProtKB:O80992}.

Miscellaneous: The synthetic growth inhibitor pyrabactin inhibits ABA- binding and subsequent PP2Cs inhibitor properties. {ECO:0000269|PubMed:22579247}.

Similarity: Belongs to the PYR/PYL/RCAR abscisic acid intracellular receptor family. {ECO:0000305}.

Sequence caution: Sequence=AAU44430.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Arabidopsis thaliana (Mouse-ear cress).
Taxonomy:		Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.



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 (PubMed:22579247, PubMed:23844015, PubMed:21658606). Can be activated by both (-)-ABA and (+)-ABA (PubMed:23844015). {ECO:0000269\|PubMed:21658606, ECO:0000269\|PubMed:22579247, ECO:0000269\|PubMed:23844015}.


Subunit:		Homodimer and monomer (PubMed:21658606). Binds ABA on one subunit only. ABA-binding favors monomer and trans-homodimer intermediate, and increases PP2C inhibitor activity (PubMed:22579247, PubMed:23844015). Binds both (-)-ABA and (+)-ABA (PubMed:23844015). Binds to CARs protein in an ABA-independent manner, both at the plasma membrane and in the nucleus (By similarity). Interacts with HAB1, ABI1 and ABI2, and possibly with other PP2Cs (PubMed:19407142, PubMed:19898420, PubMed:22579247, PubMed:23844015). {ECO:0000250\|UniProtKB:O49686, ECO:0000269\|PubMed:19407142, ECO:0000269\|PubMed:19898420, ECO:0000269\|PubMed:21658606, ECO:0000269\|PubMed:22579247, ECO:0000269\|PubMed:23844015}.
Subcellular location:		Cytoplasm {ECO:0000250\|UniProtKB:Q9FLB1}. Nucleus {ECO:0000250\|UniProtKB:O49686}. Cell membrane {ECO:0000250\|UniProtKB:O49686}. Note=Localizes at the plasma membrane in the presence of a CAR protein. {ECO:0000250\|UniProtKB:O80920}.
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. {ECO:0000250\|UniProtKB:O80992}.
Miscellaneous:		The synthetic growth inhibitor pyrabactin inhibits ABA- binding and subsequent PP2Cs inhibitor properties. {ECO:0000269\|PubMed:22579247}.
Similarity:		Belongs to the PYR/PYL/RCAR abscisic acid intracellular receptor family. {ECO:0000305}.
Sequence caution:		Sequence=AAU44430.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};