| UniProt functional annotation for P27038 | |||
| UniProt code: P27038. |
| Organism: | Mus musculus (Mouse). | |
| Taxonomy: | Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus. | |
| Function: | On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6 (PubMed:23527555). {ECO:0000269|PubMed:23527555}. | |
| Catalytic activity: | Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho- L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA- COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; | |
| Catalytic activity: | Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L- seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.30; | |
| Cofactor: | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | |
| Subunit: | Interacts with AIP1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3 (PubMed:10681527). Interacts with type I receptor ACVR1 (By similarity). Interacts with BMP7 (By similarity). {ECO:0000250|UniProtKB:P27037, ECO:0000269|PubMed:10681527}. | |
| Subcellular location: | Membrane; Single-pass type I membrane protein. | |
| Tissue specificity: | Brain, testis, intestine, liver and kidney. | |
| Similarity: | Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.