Dpp4
entrez
25253
canonical
uniprot
P14740
canonical
ensembl
ENSRNOG00000030763
resolver
ensp
ENSRNOP00000068881
resolver
genesymbol
Dpp4
resolver
genesymbol_syn
Cd26
resolver
uniprot_entry
DPP4_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by GPC3 and diprotin A. {ECO:0000269|PubMed:16768443}.
uniprot
proteins
amino_acid_sequence
MKTPWKVLLGLLGVAALVTIITVPVVLLNKDEAAADSRRTYTLADYLKNTFRVKSYSLRWVSDSEYLYKQENNILLFNAEHGNSSIFLENSTFEIFGDSISDYSVSPDRLFVLLEYNYVKQWRHSYTASYSIYDLNKRQLITEEKIPNNTQWITWSQEGHKLAYVWKNDIYVKIEPHLPSHRITSTGKENVIFNGINDWVYEEEIFGAYSALWWSPNGTFLAYAQFNDTGVPLIEYSFYSDESLQYPKTVWIPYPKAGAVNPTVKFFIVNTDSLSSTTTTIPMQITAPASVTTGDHYLCDVAWVSEDRISLQWLRRIQNYSVMAICDYDKTTLVWNCPTTQEHIETSATGWCGRFRPAEPHFTSDGSSFYKIVSDKDGYKHICQFQKDRKPEQVCTFITKGAWEVISIEALTSDYLYYISNEYKEMPGGRNLYKIQLTDHTNKKCLSCDLNPERCQYYSVSLSKEAKYYQLGCRGPGLPLYTLHRSTDQKELRVLEDNSALDKMLQDVQMPSKKLDFIVLNETRFWYQMILPPHFDKSKKYPLLIDVYAGPCSQKADAAFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINKRLGTLEVEDQIEAARQFLKMGFVDSKRVAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDAGVDFQAMWYTDEDHGIASSTAHQHIYSHMSHFLQQCFSLR
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. 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. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. {ECO:0000250|UniProtKB:P27487}.
uniprot
proteins
mass_dalton
88089
uniprot
proteins
mutagenesis
MUTAGEN 629; /note="G->A: Reduced activity."; /evidence="ECO:0000269|PubMed:7905271"; MUTAGEN 629; /note="G->R: Reduced activity."; /evidence="ECO:0000269|PubMed:7905271"; MUTAGEN 630; /note="W->E: No effect on activity."; /evidence="ECO:0000269|PubMed:7905271"; MUTAGEN 631; /note="S->A: Reduced activity."; /evidence="ECO:0000269|PubMed:7905271"; MUTAGEN 632; /note="Y->F: No effect on activity."; /evidence="ECO:0000269|PubMed:7905271"; MUTAGEN 632; /note="Y->G: Reduced activity."; /evidence="ECO:0000269|PubMed:7905271"; MUTAGEN 632; /note="Y->L: Reduced activity."; /evidence="ECO:0000269|PubMed:7905271"; MUTAGEN 633; /note="G->A: Reduced activity."; /evidence="ECO:0000269|PubMed:7905271"; MUTAGEN 633; /note="G->S: Reduced activity."; /evidence="ECO:0000269|PubMed:7905271
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. {ECO:0000250}.; PTM: N- and O-Glycosylated. {ECO:0000250}.; 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 (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
DPPIV subfamily
uniprot
proteins
protein_family
Peptidase S9B family
uniprot
proteins
pubmed
1347701
uniprot
proteins
pubmed
16768443
uniprot
proteins
pubmed
1970322
uniprot
proteins
pubmed
1974258
uniprot
proteins
pubmed
2563382
uniprot
proteins
pubmed
3182821
uniprot
proteins
pubmed
3479775
uniprot
proteins
pubmed
7905271
uniprot
proteins
sequence_length
767
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Dipeptidyl peptidase 4 soluble form]: Secreted. Note=Detected in the serum and the seminal fluid. {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Apical cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell projection, invadopodium membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Membrane raft {ECO:0000250}. 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. Redistributed to membrane rafts in T-cell in an interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. 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. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface (By similarity). {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 7..28; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins