Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development (PubMed:7936648). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (By similarity). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (PubMed:7936648). Can also bind EPHB2 and EPHB3 (By similarity). Binds to, and induces the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity). Interacts (via PDZ-binding motif) with GRIP1 and GRIP2 (via PDZ domain 6) (PubMed:10197531). Interacts with TLE1 (By similarity). The intracellular domain peptide interacts with ZHX2; the interaction enhances ZHX2 transcriptional repression activity (By similarity). May recruit GRIP1 and GRIP2 to membrane raft domains. Colocalizes with ZHX2 in the nucleus. Detected in lung, kidney, heart and testis. Detected at embryonic stage E18 in kidney, heart, brain, lung, skeletal muscle and thymus. Expression is particularly strong in kidney. Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. Proteolytically processed. The ectodomain is cleaved, probably by a metalloprotease, to produce a membrane-tethered C-terminal fragment. This fragment is then further processed by the gamma-secretase complex to yield a soluble intracellular domain peptide which can translocate to the nucleus. The intracellular domain peptide is highly labile suggesting that it is targeted for degradation by the proteasome. Belongs to the ephrin family.