UniProt functional annotation for Q9ZVR7

UniProt code: Q9ZVR7.

Organism: Arabidopsis thaliana (Mouse-ear cress).
Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
 
Function: Phytosulfokine receptor with both a serine/threonine-protein kinase activity and a guanylate cyclase activity (PubMed:21504901). Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis, somatic embryogenesis, cellular proliferation and plant growth. Involved in plant immunity, with antagonistic effects on bacterial and fungal resistances (PubMed:23062058). Not involved in PSY perception. CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:26071421). {ECO:0000269|PubMed:16829587, ECO:0000269|PubMed:17989228, ECO:0000269|PubMed:21504901, ECO:0000269|PubMed:23062058}.
 
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; Evidence={ECO:0000269|PubMed:21504901};
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; Evidence={ECO:0000269|PubMed:21504901};
Catalytic activity: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000269|PubMed:21504901};
Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21504901}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:21504901};
Activity regulation: cGMP suppresses kinase activity. {ECO:0000269|PubMed:21504901}.
Biophysicochemical properties: Kinetic parameters: KM=7.5 uM for Ser/Thr peptide 1 for the protein serine-threonine kinase activity {ECO:0000269|PubMed:21504901}; Vmax=1800 nmol/min/mg enzyme with Ser/Thr peptide 1 as substrate {ECO:0000269|PubMed:21504901};
Subunit: Homo- and heterodimers with PSY1R (PubMed:25267325). Heterodimers with the somatic embryogenesis receptor-like kinases (SERKs) (PubMed:26308901). PSK is not directly involved in PSKR-SERK interaction but stabilizes PSKR island domain for recruitment of a SERK (PubMed:26308901). Part of a functional complex containing PSKR1, BAK1, CNGC17, and AHA (PubMed:26071421). Interacts with AHA1, AHA2, and BAK1, but not with CNGC17 or BRI1 (PubMed:26071421). {ECO:0000269|PubMed:25267325, ECO:0000269|PubMed:26071421, ECO:0000269|PubMed:26308901}.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26071421}; Single-pass type I membrane protein {ECO:0000305}.
Tissue specificity: Weakly expressed in roots, leaves, stems and flowers (PubMed:16829587). Expressed in the primary and lateral roots, including root primordia and root tips, but not in the hypocotyl (PubMed:19076296). {ECO:0000269|PubMed:16829587, ECO:0000269|PubMed:19076296}.
Induction: Up-regulated by fungal infection and wounding. {ECO:0000269|PubMed:20403122}.
Disruption phenotype: Gradual loss of individual cells potential to form callus as the tissues mature (PubMed:16829587). Premature senescence of the leaves (PubMed:17989228). Limitted root growth (PubMed:19076296). Enhanced resistance to bacterial biotrophic pathogens, but increased susceptibility to necrotrophic fungal infection (PubMed:23062058). {ECO:0000269|PubMed:16829587, ECO:0000269|PubMed:17989228, ECO:0000269|PubMed:19076296, ECO:0000269|PubMed:23062058}.
Miscellaneous: PSKR1 and PSYR1 mediate a signaling pathway by two distinct ligands, which redundantly contribute to cellular proliferation and plant growth. {ECO:0000269|PubMed:17989228}.
Similarity: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.

Annotations taken from UniProtKB at the EBI.