We previously found a brain-specific glycoprotein in the rat brain. It postnatally increases and is rich in the mature brain. We cloned cDNA of this protein. It is composed of a signal peptide, a V-type immunoglobulin domain, two C1-type immunoglobulin domains, a transmembrane segment and a cytoplasmic region containing two tyrosine-based activation motifs (TAM) that are variants of the antigen receptor signaling motifs. The overall structure is similar to those of immune antigen receptors. This molecule, BIT (brain immunoglobulin-like molecule with TAMs), is a major endogenous substrates of brain tyrosine kinases in vitro. Cerebral cortical neurons could extend their neurites on BIT-coated substrate and anti-BIT monoclonal antibody specifically inhibited the effect. These findings and our recent study concerning BIT signal transduction mechanism suggest that BIT, an immune antigen receptor-like molecule of the brain, functions as a membrane signaling molecule that may participate in cell-cell interaction.