UniProt functional annotation for P47735

UniProt code: P47735.

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 with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates that controls floral organ abscission. May interact with the 'INFLORESCENCE DEFICIENT IN ABSCISSION' (IDA) ligands family. {ECO:0000269|PubMed:10640280, ECO:0000269|PubMed:18660431, ECO:0000269|PubMed:18809915}.
 
Catalytic activity: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
Catalytic activity: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
Catalytic activity: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Have significantly greater activity in the presence of Mn(2+) than Mg(2+).;
Subunit: Interacts with CST (PubMed:21628627). Binds to IDA (PubMed:27058169). {ECO:0000269|PubMed:21628627, ECO:0000269|PubMed:27058169}.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10640280}; Single-pass type I membrane protein {ECO:0000269|PubMed:10640280}.
Tissue specificity: Expressed in roots and rosettes. Expressed at the base of petioles and pedicels, and in the abscission zones of the floral organs. {ECO:0000269|PubMed:10640280}.
Ptm: Autophosphorylated on Ser, Thr and Tyr residues.
Disruption phenotype: No visible phenotype; due to the redundancy with HSL2. Hae and hsl2 double mutants have a strong abscission defect. {ECO:0000269|PubMed:18660431, ECO:0000269|PubMed:18809915}.
Miscellaneous: The name HAESA derives from a Latin word meaning 'to adhere to'.
Similarity: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.

Annotations taken from UniProtKB at the EBI.