DPP4
entrez
1803
canonical
uniprot
P27487
canonical
ensembl
ENSG00000197635
resolver
ensp
ENSP00000353731
resolver
ensp
ENSP00000503161
resolver
ensp
ENSP00000551401
resolver
ensp
ENSP00000650026
resolver
enst
ENST00000360534
resolver
enst
ENST00000676810
resolver
genesymbol
DPP4
resolver
genesymbol_syn
ADCP2
resolver
genesymbol_syn
CD26
resolver
hgnc
HGNC:3009
resolver
uniprot
A0A7I2V2X8
resolver
uniprot
Q53TN1
resolver
uniprot_entry
A0A7I2V2X8_HUMAN
resolver
uniprot_entry
DPP4_HUMAN
resolver
uniprot_sec
Q53TN1
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by GPC3 and diprotin A. {ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:18708048}.
uniprot
proteins
amino_acid_sequence
MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP
uniprot
proteins
ec_number
3.4.14.5
uniprot
proteins
function
FUNCTION: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation (PubMed:10900005, PubMed:10951221, PubMed:11772392, PubMed:17287217). Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10900005, PubMed:10951221, PubMed:11772392, PubMed:14691230). Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion (PubMed:11772392). 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 (PubMed:10593948, PubMed:16651416). May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation (PubMed:18708048). When overexpressed, enhanced cell proliferation, a process inhibited by GPC3 (PubMed:17549790). 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 (PubMed:10570924, PubMed:16254193). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (PubMed:10593948). {ECO:0000269|PubMed:10570924, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:14691230, ECO:0000269|PubMed:16254193, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:18708048}.; FUNCTION: (Microbial infection) Acts as a receptor for human coronavirus MERS-CoV-2. {ECO:0000269|PubMed:23835475}.
uniprot
proteins
mass_dalton
88279
uniprot
proteins
mutagenesis
MUTAGEN 85; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 92; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 150; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 205; /note="E->K: Inhibits dipeptidyl peptidase activity."; /evidence="ECO:0000269|PubMed:10570924"; MUTAGEN 206; /note="E->L: Inhibits dipeptidyl peptidase activity."; /evidence="ECO:0000269|PubMed:10570924"; MUTAGEN 219; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 229; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 281; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 321; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 520; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 685; /note="N->A: Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation."; /evidence="ECO:0000269|PubMed:14691230"; MUTAGEN 750; /note="H->A: Inhibits weakly homodimerization and dipeptidyl peptidase activity."; /evidence="ECO:0000269|PubMed:15448155, ECO:0000269|PubMed:17287217"; MUTAGEN 750; /note="H->E: Inhibits strongly homodimerization, dipeptidyl peptidase activity, interaction with CARD11 and T-cell costimulation activity."; /evidence="ECO:0000269|PubMed:15448155, ECO:0000269|PubMed:17287217
uniprot
proteins
post_translational_modification
PTM: 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.; PTM: N- and O-Glycosylated. {ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:11773049, ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603}.; PTM: 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. {ECO:0000269|PubMed:10900005}.
uniprot
proteins
protein_family
DPPIV subfamily
uniprot
proteins
protein_family
Peptidase S9B family
uniprot
proteins
pubmed
10570924
uniprot
proteins
pubmed
10593948
uniprot
proteins
pubmed
10880264
uniprot
proteins
pubmed
10900005
uniprot
proteins
pubmed
10951221
uniprot
proteins
pubmed
11027426
uniprot
proteins
pubmed
11772392
uniprot
proteins
pubmed
11773049
uniprot
proteins
pubmed
12483204
uniprot
proteins
pubmed
12646248
uniprot
proteins
pubmed
12676959
uniprot
proteins
pubmed
12832764
uniprot
proteins
pubmed
12906826
uniprot
proteins
pubmed
1347043
uniprot
proteins
pubmed
1352530
uniprot
proteins
pubmed
1352704
uniprot
proteins
pubmed
14691230
uniprot
proteins
pubmed
15016824
uniprot
proteins
pubmed
15448155
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16254193
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16651416
uniprot
proteins
pubmed
16670267
uniprot
proteins
pubmed
1677636
uniprot
proteins
pubmed
17287217
uniprot
proteins
pubmed
17549790
uniprot
proteins
pubmed
18708048
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19557413
uniprot
proteins
pubmed
1977364
uniprot
proteins
pubmed
20684603
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23486063
uniprot
proteins
pubmed
23835475
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
32867305
uniprot
proteins
pubmed
7487939
uniprot
proteins
pubmed
7907293
uniprot
proteins
pubmed
7927537
uniprot
proteins
pubmed
8094732
uniprot
proteins
pubmed
8096237
uniprot
proteins
pubmed
8101391
uniprot
proteins
pubmed
8526932
uniprot
proteins
pubmed
9413751
uniprot
proteins
sequence_length
766
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Dipeptidyl peptidase 4 soluble form]: Secreted {ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:16254193}. Note=Detected in the serum and the seminal fluid. {ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:16254193}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:11772392, ECO:0000305|PubMed:8101391}; Single-pass type II membrane protein. Apical cell membrane {ECO:0000269|PubMed:11773049}; Single-pass type II membrane protein. Cell projection, invadopodium membrane {ECO:0000269|PubMed:16651416}; Single-pass type II membrane protein. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:16651416}; Single-pass type II membrane protein. Cell junction {ECO:0000269|PubMed:11772392}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids (PubMed:11773049). Redistributed to membrane rafts in T-cell in an interleukin-12-dependent activation (PubMed:12676959). Its interaction with CAV1 is necessary for its translocation to membrane rafts (PubMed:17287217). Colocalized with PTPRC in membrane rafts (PubMed:12676959). Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma (PubMed:16651416). Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion (PubMed:11772392). Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface (PubMed:10900005). {ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:11773049, ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217}.
uniprot
proteins
transmembrane_region
TRANSMEM 7..28; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins