Lysosomal Associated Membrane Protein 3 (LAMP3)

By screening a DC subtraction library, de Saint-Vis et al. (1998) isolated a cDNA encoding DCLAMP. Sequence analysis predicted that the 416-amino acid type I integral membrane protein has an N-terminal signal peptide, followed by a 381-amino acid extracellular domain, a hydrophobic transmembrane domain, and a 10-amino acid cytoplasmic domain containing a conserved GY lysosomal targeting motif, characteristic of LAMP family members.The DCLAMP protein contains multiple N- and O-glycosylation sites. Northern blot and RT-PCR analysis revealed expression of a 3.2-kb transcript in appendix, thymus, lymph node, lung, and weakly in spleen, as well as in dendritic cell lines; expression was weak or undetectable in other cell lines.