|CD296||ART1 (ADP-ribosyltransferase 1), ART2|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
|37 / 37|
|CD296 is expressed on neutrophils, epithelial and skeletal muscle cells and NK and T cell subsets. Expression is also in the heart and skeletal muscle.|
|MOLECULAR FAMILY NAME: Belongs to the Arg-specific ADP-ribosyltransferase family.|
CD296 is 273 aa GPI-anchor protein. It contain an extracellular domain which contains a C-terminal which contains a β-sheet rich domain and thought to be formed by the intersection of three domains and has 2 potential N-terminal glycosylation sites but there is no transmembrane domain or cytoplasmic domain. Domain 1 and 2 are defined by a conserved arginine and consensus Ser-X-Ser motifs and is involved in stabilizing NAD binding. Domain 3 contains a catalytic glutamate which is required for NAD hydrolysis. The N-terminal contains α helices and influences the transfer of ADP-ribose to an acceptor amino acid or to water. CD296 is an ADP-ribosyltransferase which catalyzes the ADP-ribosylation of arginine residues in a structurally related family of proteins that are expressed on the cell surface or secreted in the extracellular matrix. This gene was previously designated ART2.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
CD296 has 2 potential N-terminal glycosylation sites.
|LIGANDS AND MOLECULE ASSOCIATED WITH CD296|
CD296 associates with PDGFβ, integrins and defensin.
|CD296 catalyzes the transfer of a single ADP-ribose group from NAD onto an arginine of a target protein, thereby reversibly modifying the protein's function. Substrates of CD296 include integrin α7, defensin-1, CD11a, CD18, as well as ADP-ribosylate guanidine containing substrates such as agmatine and arginine methyl ester. CD296 can also ribosylate small soluble proteins such as the basic fibroblast growth factor (FGF-2). CD296 is involved in the regulation of cellular metabolism and associated with myocyte differentiation, inflammatory responses and inhibition of proliferation and cytotoxicity by cytotoxic T cells. |
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD296 IN INTACT ANIMAL
Mono-ADP-ribosylation is a posttranslational of proteins that is interfered with a variety of bacterial toxins including cholera, pertussis, and heat-labile enterotoxins of E. coli.
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD296: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD296: No information.
For further information see Seman, M. et al (2004) Curr. Med. Chem. 11: 857-872.
Database accession numbers
Revised June 25, 2008