N-末端から２アミノ酸を遊離させる。
細胞質に局在するもの、膜結合型、分泌されるものなど
Dipeptidyl peptidase 1
https://www.uniprot.org/uniprot/P53634
Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII.
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro. EC:3.4.14.1
Strongly inhibited by the cysteine peptidase inhibitors mersalyl acid, iodoacetic acid and cystatin. Inhibited by N-ethylmaleimide, Gly-Phe-diazomethane, TLCK, TPCK and, at low pH, by dithiodipyridine. Not inhibited by the serine peptidase inhibitor PMSF, the aminopeptidase inhibitor bestatin, or metal ion chelators.
リソソームに局在する
Dipeptidyl peptidase 9
https://www.uniprot.org/uniprot/Q86TI2
Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:12662155, PubMed:16475979, PubMed:19667070, PubMed:30291141, PubMed:29382749).
Acts as an inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis: inhibits pyroptosis by preventing activation of NLRP1 and CARD8 via an unknown mechanism (PubMed:27820798, PubMed:30291141, PubMed:29967349, PubMed:31525884, PubMed:32796818).
9 Publications
Catalytic activityi
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.6 Publications EC:3.4.14.5
Activity regulationi
Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfluorophosphate (PubMed:12662155). Inhibited by Val-boroPro (Talabostat, PT-100), a non-selective inhibitor, which triggers pyroptosis in monocytes and macrophages (PubMed:27820798, PubMed:29967349, PubMed:32796818).
細胞質と核内
Dipeptidyl peptidase 4
https://www.uniprot.org/uniprot/P27487
Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation (PubMed:10951221, PubMed:10900005, PubMed:11772392, PubMed:17287217).
Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10951221, PubMed:10900005, 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:16651416, PubMed:10593948).
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).
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 such as brain natriuretic peptide 32 (PubMed:16254193, PubMed:10570924).
Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (PubMed:10593948).
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.PROSITE-ProRule annotation1 Publication EC:3.4.14.5
２型膜タンパク質、切り出されて可溶性になる
Dipeptidyl peptidase 2
https://www.uniprot.org/uniprot/Q9UHL4
DPP7
Plays an important role in the degradation of some oligopeptides.
Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.1 Publication EC:3.4.14.2
分泌される
Dipeptidyl peptidase 8
Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2 (PubMed:11012666, PubMed:12534281, PubMed:12662155, PubMed:15039077, PubMed:15664838, PubMed:20536396) (Probable).
Acts as an inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis: inhibits pyroptosis by preventing activation of NLRP1 and CARD8 via an unknown mechanism (PubMed:27820798, PubMed:29967349, PubMed:32796818).
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.7 Publications EC:3.4.14.5
