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CD100 was originally described as a 150 kDa surface T-cell antigen induced after T-cell activation. Human CD100 exhibits widespread gene expression but is most prominent in peripheral lymphocytes, thymus, skeletal muscle, and brain. The full CD100 protein is 862 amino acids with homolgy to the semaphorin family of proteins at its extracellular domain followed by a short Ig-like domain. The short cytoplasmic domain contains a putative tyrosine phosphorylation site which may be the site for association with intracellular kinases. Cells that overexpress CD100 induce a rapid aggregation of B cells and increase the CD90L-B cell aggregation. Because semaphorins are axon-guiding molecules for the nervous system, it has been proposed that CD100 may have a guidance role in the immune system.
