Echinoderm Microtubule Associated Protein Like Protein 4 (EML4)

Heidebrecht et al. (2000) purified a 120-kD protein that was highly expressed in mitotic Hodgkin lymphoma cells. Using degenerate primers designed from the amino acid sequence for PCR amplification, followed by an EST database search, they cloned the full-length EML4 cDNA, which they called ROPP120 (restrictedly overexpressed proliferation-associated protein of 120 kD). The deduced 981-amino acid protein has a calculated molecular mass of 109 kD. It contains 4 WD repeats in the C terminus, a trypsin-like serine protease active site, a histidine acid phosphate site, an EF-hand calcium-binding domain, 6 N-glycosylation sites, and more than 20 putative phosphorylation sites. EML4 shares 56% sequence identity with EML1 and 57% with the echinoderm microtubule-associated protein.