a receptor tyrosine kinase. Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A3, -A4 AND -A5. The Eph receptor tyrosine kinase family, the largest in the tyrosine kinase group, has fourteen members. They bind membrane-anchored ligands, ephrins, at sites of cell-cell contact, regulating the repulsion and adhesion of cells that underlie the establishment, maintenance, and remodeling of patterns of cellular organization. Eph signals are particularly important in regulating cell adhesion and cell migration during development, axon guidance, homeostasis and disease. EphA receptors bind to GPI-anchored ephrin-A ligands, while EphB receptors bind to ephrin-B proteins that have a transmembrane and cytoplasmic domain. Interactions between EphB receptor kinases and ephrin-B proteins transduce signals bidirectionally, signaling to both interacting cell types. Eph receptors and ephrins also regulate the adhesion of endothelial cells and are required for the remodeling of blood vessels. Overexpressed in many cancers including aggressive ovarian, cervical and breast carcinomas, and lung cancer. Expression correlates with degree of angiogenesis, metastasis and xenograft tumor growth. Soluble receptor inhibits tumor growth and angiogenesis in mice. Note: This description may include information from UniProtKB.
Protein type: EC 18.104.22.168; Eph family; Kinase, protein; Membrane protein, integral; Protein kinase, TK; Protein kinase, tyrosine (receptor); TK group
Cellular Component: cell surface; cell-cell adherens junction; focal adhesion; integral to plasma membrane; lamellipodium; plasma membrane
Molecular Function: protein binding; transmembrane receptor protein tyrosine kinase activity
Biological Process: bone remodeling; cAMP metabolic process; cell migration; cell motility involved in cell locomotion; DNA damage response, signal transduction resulting in induction of apoptosis; ephrin receptor signaling pathway; keratinocyte differentiation; mammary gland epithelial cell proliferation; multicellular organismal development; negative regulation of protein kinase B signaling cascade; osteoblast differentiation; osteoclast differentiation; protein kinase B signaling cascade; regulation of angiogenesis; regulation of blood vessel endothelial cell migration; regulation of cell adhesion mediated by integrin