Aliases for DPP4 Gene
External Ids for DPP4 Gene
Previous Symbols for DPP4 Gene
The protein encoded by this gene is identical to adenosine deaminase complexing protein-2, and to the T-cell activation antigen CD26. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. [provided by RefSeq, Jul 2008]
GeneCards Summary for DPP4 Gene
DPP4 (Dipeptidyl-Peptidase 4) is a Protein Coding gene. Diseases associated with DPP4 include nasopharyngitis and mental depression. Among its related pathways are Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein and Peptide hormone metabolism. GO annotations related to this gene include protein homodimerization activity and receptor binding. An important paralog of this gene is FAP.
UniProtKB/Swiss-Prot for DPP4 Gene
Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Dipeptidyl Peptidase IV (DPP-IV) (also known as CD26) is a ubiquitous, membrane-bound enzyme that has roles in nutrition, metabolism, the immune and endocrine systems, bone marrow mobilization, cancer growth and cell adhesion. DDP-IV catalyzes the hydrolysis of N-terminal dipeptides from polypeptides with proline or alanine in the penultimate position. This enzyme has many natural substrates including GLP-1, GIP, PACAP 38, NPY and GRP. DPP-IV exists as a homodimer and each monomer consists of two domains; an alpha/beta hydrolase domain and an eight-blade beta-propeller domain. DDP-IV binds to, but does not cleave, adenosine deaminase, kidney Na+/H+ ion exchanger and fibronectin, which localizes these molecules to the cell surface. A soluble form of DDP-IV does also exist, although it is only known to function in relation to T-cell proliferation. The human gene encoding DPP-IV is localized to chromosome 2q24.2.