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Gene Symbol |
DPP4 |
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Aliases |
ADABP, ADCP2, CD26, DPPIV, TP103 |
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Entrez Gene ID |
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Gene Name |
Dipeptidyl peptidase 4 |
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Chromosomal Location |
2q24.2 |
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HGNC ID |
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Summary |
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]
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e!Ensembl
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Gene Ontology (GO)
GO ID |
Ontology |
Function |
Evidence |
Reference |
GO:0001666 |
Biological process |
Response to hypoxia |
IDA |
16670267 |
GO:0006508 |
Biological process |
Proteolysis |
IDA |
27198182 |
GO:0008284 |
Biological process |
Positive regulation of cell proliferation |
IDA |
17549790 |
GO:0010716 |
Biological process |
Negative regulation of extracellular matrix disassembly |
IDA |
16651416 |
GO:0031295 |
Biological process |
T cell costimulation |
IDA |
10900005, 17287217 |
GO:0033632 |
Biological process |
Regulation of cell-cell adhesion mediated by integrin |
IDA |
11772392 |
GO:0042110 |
Biological process |
T cell activation |
IDA |
7594462 |
GO:0043542 |
Biological process |
Endothelial cell migration |
IDA |
16651416 |
GO:0005765 |
Cellular component |
Lysosomal membrane |
HDA |
17897319 |
GO:0005886 |
Cellular component |
Plasma membrane |
IDA |
16670267 |
GO:0005925 |
Cellular component |
Focal adhesion |
HDA |
21423176 |
GO:0009986 |
Cellular component |
Cell surface |
IDA |
7594462, 8101391, 10900005, 11772392 |
GO:0016020 |
Cellular component |
Membrane |
HDA |
19946888 |
GO:0016324 |
Cellular component |
Apical plasma membrane |
IDA |
15052268 |
GO:0030027 |
Cellular component |
Lamellipodium |
IDA |
16651416 |
GO:0030139 |
Cellular component |
Endocytic vesicle |
IDA |
10900005 |
GO:0070062 |
Cellular component |
Extracellular exosome |
HDA |
11487543, 19056867, 19199708, 20458337, 21362503, 23533145 |
GO:0071438 |
Cellular component |
Invadopodium membrane |
IDA |
16651416 |
GO:0001618 |
Molecular function |
Virus receptor activity |
IDA |
23486063 |
GO:0002020 |
Molecular function |
Protease binding |
IPI |
16651416 |
GO:0004252 |
Molecular function |
Serine-type endopeptidase activity |
EXP |
8100523, 8798518, 15584901 |
GO:0005102 |
Molecular function |
Signaling receptor binding |
IPI |
10900005 |
GO:0005515 |
Molecular function |
Protein binding |
IPI |
7594462, 8101391, 14684150, 17287217, 17549790, 18275857, 21314817, 22001206, 23486063, 23831647 |
GO:0008236 |
Molecular function |
Serine-type peptidase activity |
IDA |
14684150 |
GO:0008239 |
Molecular function |
Dipeptidyl-peptidase activity |
IDA |
10593948, 14684150, 16651416, 17549790, 27198182 |
GO:0042802 |
Molecular function |
Identical protein binding |
IPI |
22001206 |
GO:0042803 |
Molecular function |
Protein homodimerization activity |
IPI |
14684150, 15448155 |
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Protein Information |
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Protein Name |
Dipeptidyl peptidase 4, ADCP-2, DPP IV, T-cell activation antigen CD26, adenosine deaminase complexing protein 2, dipeptidyl peptidase IV, dipeptidylpeptidase 4, dipeptidylpeptidase IV (CD26, adenosine deaminase complexing protein 2) |
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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. 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. |
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UniProt |
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PDB |
1J2E, 1N1M, 1NU6, 1NU8, 1PFQ, 1R9M, 1R9N, 1RWQ, 1TK3, 1TKR, 1U8E, 1W1I, 1WCY, 1X70, 2AJL, 2BGN, 2BGR, 2BUB, 2FJP, 2G5P, 2G5T, 2G63, 2HHA, 2I03, 2I78, 2IIT, 2IIV, 2JID, 2OAG, 2OGZ, 2OLE, 2ONC, 2OPH, 2OQI, 2OQV, 2P8S, 2QJR, 2QKY, 2QOE, 2QT9, 2QTB, 2RGU, 2RIP, 3BJM, 3C43, 3C45, 3CCB, 3CCC, 3D4L, 3EIO, 3F8S, |
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Associated Diseases
Disease group | Disease Name | References |
Endocrine System Diseases |
PCOS |
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Immune System Diseases |
Rheumatoid Arthritis |
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Psychiatric/Brain disorders |
Mental Depression |
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References |
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PubMed ID |
Associated gene/s |
Associated condition |
Genetic Mutation |
Diagnostic Criteria |
Association with PCOS |
Ethnicity |
Conclusion |
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HbA1c, HDL-c , SHBG, Testosterone, androstenedione, DHEA-S , LH, FA |
PCOS |
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Rotterdam criteria |
Direct
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30 PCOS patients and 28 healthy women. |
Although PCOS was well characterized as IR and hyperandrogenic, DPP4 was not different in this group. However, a relationship between DPP4 and markers of IR were found. |
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