DPP2 is a serine protease found most abundantly in the lysosome. There is also a non-lysosomal membrane-associated form of DPP2 reported in the rat brain (DPP-II-M), and a soluble form (DPP-II-S). First discovered as an enzyme involved in the terminal steps of protein degradation, and later as an enzyme involved in cell growth and quiescence, DPP2 cleaves N-terminal dipeptides and tripeptides from proteins. DPP2 has a preference for proline in the P1 position, and processes the tripeptides generated by DPP1 (which is unable to cleave if proline is in the P1 position). Some tumor cell lines express elevated DPP2 levels, and serum levels of DPP2 are elevated in some cancer patients, making DPP2 a potential tumor marker. DPP2 levels have been also been reported to be elevated in the cerebral spinal fluid from Parkinson’s patients.
Function:
Plays an important role in the degradation of some oligopeptides.
Subunit:
Homodimer.
Subcellular Location:
Lysosome. Cytoplasmic vesicle. Secreted.
Tissue Specificity:
Detected in seminal plasma (at protein level).
Post-translational modifications:
N-glycosylated.
Similarity:
Belongs to the peptidase S28 family.
SWISS:
Q9UHL4
Gene ID:
29952
Database links:
Entrez Gene: 29952 Human
Entrez Gene: 83768 Mouse
Entrez Gene: 83799 Rat
Omim: 610537 Human
SwissProt: Q9UHL4 Human
SwissProt: Q9ET22 Mouse
SwissProt: Q9EPB1 Rat
Unigene: 37916 Human
Unigene: 3363 Rat
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