The C-type lectin family is a group of animal proteins which can be distinguished from other lectins by the presence of a Ca2+-dependent carbohydrate recognition domain (CRD) in their protein sequence. They are classified into 17 groups according to their domain architecture and have a wide variety of functions. The human chondrolectin gene encodes transmembrane (CHODL, CHODLf) and soluble proteins (CHODLΔE, CHODLfΔE) belonging to the family of C-type lectins because of the presence of one CRD domain in their N-terminal region. The CHODL splice variants (CHODLf, CHODLΔE and CHODLfΔE) are differentially expressed in T lymphocytes. The transmembrane-containing isoform CHODLf is localized in the ER—Golgi apparatus. CHODLΔE and CHODLfΔE are devoid of the transmembrane domain and terminate in QDEL, an ER retention signal. In this paper we have investigated the expression of the CHODLΔE/CHODLfΔE protein. This variant localizes in the late endoplasmic reticulum. We detected the protein in spleen and tonsils in a small population of lymphocytes. Moreover, the isoform seems to be differentially expressed in thymocytes and lymphocytes suggesting an important biological function during T cell development.