CD38

CD38 also known as ADPRC1, is a non-lineage-restricted, type II transmembrane glycoprotein. This protein synthesizes and hydrolyzes cyclic adenosine 5'-diphosphate-ribose, and it is an intracellular calcium ion mobilizing messenger. CD38 consists of an N-terminal cytoplasmic tail, a single membrane-spanning domain, as well as a C-terminal extracellular region with four N-glycosylation sites. And the crystal structure analysis of CD38 exhibited that the functional molecule of which is a dimer, with the central portion containing the catalytic site.
Initially, CD38 is found by monoclonal antibody typing of lymphocytes and therefore considered as a lymphocyte-specific antigen. Importantly, its expression in lymphocytes displays stage-related variations and ligation via agonistic antibodies against CD38 enable to trigger a great number of responses in many types of blood cells. Nevertheless, recent researches have demonstrated that CD38 is not lymphocyte-specific, but is ubiquitously expressed in virtually all tissues. CD38 is present not only on cell surfaces but also in a variety of intracellular organelles, including the nucleus. In addition, it has been reported that CD38 is a multi-functional enzyme catalyzing the metabolism of two distinct Ca2+ messengers, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP).
Gene ID: 952
UniProt ID: P28907