| Primary information |
|---|
| ID | 33315 |
| Uniprot ID | P35916 |
| Description | Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4) |
| Organism | Homo sapiens |
| Txonomy | Homo ; Homininae ; Hominidae ; Hominoidea ; Catarrhini ; Simiiformes ; Haplorrhini ; Primates ; Euarchontoglires ; Boreoeutheria ; Eutheria ; Theria ; Mammalia ; Amniota ; Tetrapoda ; Dipnotetrapodomorpha ; Sarcopterygii ; Euteleostomi ; Teleostomi ; Gnathostomata ; Vertebrata ; Craniata ; Chordata ; Deuterostomia ; Bilateria ; Eumetazoa ; Metazoa ; Opisthokonta ; Eukaryota ; cellular organisms |
| Subcellular Location | Cell membrane |
| Developmental Stage | NA |
| Similarity | NA |
| Post Translational Modification | Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans; i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation in response to H(2)O(2) is mediated by a process that requires SRC and PRKCD activity. Phosphorylation at Tyr-1068 is required for autophosphorylation at additional tyrosine residues. Phosphorylation at Tyr-1063 and Tyr-1337 is important for interaction with CRK and subsequent activation o |
| Function | Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD; and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation; survival and migration of endothelial cells; and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC; and to a lesser degree VEGFA; thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction; because it has a truncated C-terminus and therefore lacks several phosph |
| Length | 1363 |
| Molecular Weight | 152757 |
| Reference | 1327515; 1319394; 83 |
| Hormone | NA |
| PDB ID | NA
|