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UniProt functional annotation for P43298 | ||
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| UniProt code: P43298. |
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| Organism: | |
Arabidopsis thaliana (Mouse-ear cress). |
| Taxonomy: | |
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. |
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| Function: | |
Transmembrane kinase receptor (PubMed:1332795). Phosphorylates only serine and threonine residues (PubMed:8224199). Involved in auxin signal transduction and cell expansion and proliferation regulation (PubMed:23613767). Forms with ABP1 a cell surface auxin perception complex that activates ROP signaling pathways (PubMed:24578577). Required for auxin promotion of pavement cell interdigitation (PubMed:24578577). Auxin promotes the formation of the ABP1-TMK1 protein complex (PubMed:24578577). {ECO:0000269|PubMed:23613767, ECO:0000269|PubMed:24578577, ECO:0000269|PubMed:8224199, ECO:0000303|PubMed:1332795}. |
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| 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:1332795, ECO:0000269|PubMed:8224199}; |
| 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:1332795, ECO:0000269|PubMed:8224199}; |
| Cofactor: | |
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:8224199}; |
| Subunit: | |
Interacts (via extracellular domain) with ABP1. {ECO:0000269|PubMed:24578577}. |
| Subcellular location: | |
Cell membrane {ECO:0000269|PubMed:23613767, ECO:0000269|PubMed:24578577}; Single-pass type I membrane protein {ECO:0000255}. |
| Tissue specificity: | |
Expressed in roots, leaves, stems, siliques and flowers. {ECO:0000269|PubMed:1332795, ECO:0000269|PubMed:23613767}. |
| Domain: | |
The leucine-rich repeat (LRR) domain is disrupted by a non-LRR region, resulting in the formation of two LRR solenoid structures shaped like the Arabic number '7'. This is strikingly different from the horseshoe structures of the canonical LRR proteins. {ECO:0000269|PubMed:23147790}. |
| Ptm: | |
Autophosphorylated on serine and threonine residues. {ECO:0000269|PubMed:1332795}. |
| Ptm: | |
Glycosylated. {ECO:0000269|PubMed:8224199}. |
| Disruption phenotype: | |
No visible phenotype (PubMed:23613767). Tmk1 and tmk2 double mutants, tmk1 and tmk3 double mutants and tmk1, tmk2 and tmk3 triple mutants have no visible phenotypes (PubMed:23613767). Tmk1 and tmk4 double mutants, tmk1, tmk2 and tmk4 triple mutants and tmk1, tmk3 and tmk4 triple mutants have a severe reduction in organ size, a substantial delay in growth and development, and a decrease in fertility (PubMed:23613767). Tmk1, tmk2, tmk3 and tmk4 quadruple mutants are embryo lethal (PubMed:23613767, PubMed:24578577). {ECO:0000269|PubMed:23613767, ECO:0000269|PubMed:24578577}. |
| Similarity: | |
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.