| Tissue Specificity | Expressed specifically in lymphatic vessels but not in blood vessels in the skin, small intestine, esophagus, ovary, breast and prostate glands. Not detected in lymphatic vessels in the lung, kidney, uterus, liver and stomach (at protein level). Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon. |
| Post Translational Modifications | The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing. N- and O-Glycosylated. Phosphorylated. Mannose 6-phosphate residues in the carbohydrate moiety are necessary for interaction with IGF2R in activated T-cells. Mannose 6-phosphorylation is induced during T-cell activation. |
| Function | 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. Also acts 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 such as brain natriuretic peptide 32. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. (Microbial infection) Acts as a receptor for human coronavirus MERS-CoV-2. |
| Protein Name | Dipeptidyl Peptidase 4AdabpAdenosine Deaminase Complexing Protein 2Adcp-2Dipeptidyl Peptidase IvDpp IvT-Cell Activation Antigen Cd26Tp103Cd Antigen Cd26 Cleaved Into - Dipeptidyl Peptidase 4 Membrane FormDipeptidyl Peptidase Iv Membrane Form - Dipeptidyl Peptidase 4 Soluble FormDipeptidyl Peptidase Iv Soluble Form |
| Database Links | Reactome: R-HSA-381771Reactome: R-HSA-400511 |
| Cellular Localisation | Dipeptidyl Peptidase 4 Soluble Form: SecretedDetected In The Serum And The Seminal FluidCell MembraneSingle-Pass Type Ii Membrane ProteinApical Cell MembraneCell ProjectionInvadopodium MembraneLamellipodium MembraneCell JunctionMembrane RaftTranslocated To The Apical Membrane Through The Concerted Action Of N- And O-Glycans And Its Association With Lipid Microdomains Containing Cholesterol And SphingolipidsRedistributed To Membrane Rafts In T-Cell In An Interleukin-12-Dependent ActivationIts Interaction With Cav1 Is Necessary For Its Translocation To Membrane RaftsColocalized With Ptprc In Membrane RaftsColocalized With Fap In Invadopodia And Lamellipodia Of Migratory Activated Endothelial Cells In Collagenous MatrixColocalized With Fap On Endothelial Cells Of Capillary-Like Microvessels But Not Large Vessels Within Invasive Breast Ductal CarcinomaColocalized With Ada At The Cell Junction In Lymphocyte-Epithelial Cell AdhesionColocalized With Igf2r In Internalized Cytoplasmic Vesicles Adjacent To The Cell Surface |
| Alternative Protein Names | Dipeptidyl Peptidase 4 proteinAdabp proteinAdenosine Deaminase Complexing Protein 2 proteinAdcp-2 proteinDipeptidyl Peptidase Iv proteinDpp Iv proteinT-Cell Activation Antigen Cd26 proteinTp103 proteinCd Antigen Cd26 Cleaved Into - Dipeptidyl Peptidase 4 Membrane Form proteinDipeptidyl Peptidase Iv Membrane Form - Dipeptidyl Peptidase 4 Soluble Form proteinDipeptidyl Peptidase Iv Soluble Form proteinDPP4 proteinADCP2 proteinCD26 protein |
Information sourced from Uniprot.org
