UniProt ID: A0A8M9PX37 |
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:0000256|ARBA:ARBA00001171}; SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. CAUTION: Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. |
UniProt ID: A0A8M3ARU2 |
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:0000256|ARBA:ARBA00001171}; SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. CAUTION: Lacks conserved residue(s) required for the propagation of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. |
UniProt ID: O73791 |
FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for angiopoietins and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Can activate or inhibit angiogenesis, depending on the context. Angiopoietin signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors (By similarity). {ECO:0000250}. 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:PRU10028}; ACTIVITY REGULATION: Angiopoietin binding leads to receptor dimerization and activation by autophosphorylation at Tyr-984 on the kinase activation loop. {ECO:0000250}. SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Recruited to cell-cell contacts in quiescent endothelial cells. Colocalizes with the actin cytoskeleton and at actin stress fibers during cell spreading. Recruited to the lower surface of migrating cells, especially the rear end of the cell (By similarity). {ECO:0000250}. TISSUE SPECIFICITY: Expressed in most populations of endothelial cells in 24 hours embryos. Not present in intersegmental vessels. {ECO:0000269|PubMed:9603430}. PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner, where Tyr-984 in the kinase activation loop is phosphorylated first, followed by autophosphorylation at additional tyrosine residues. Phosphorylation is important for interaction with scaffold proteins and effectors. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. |
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