| peptidase D Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen. Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB. |
| Protein type: EC 3.4.13.9; Protease |
| Chromosomal Location of human Ortholog: 19q13.11 |
| Cellular Component: |
| Molecular Function: manganese ion binding; metalloaminopeptidase activity; metallocarboxypeptidase activity; peptidase activity; proline dipeptidase activity; protein binding |
| Biological Process: amino acid metabolic process; collagen catabolic process; negative regulation of programmed cell death; proteolysis |
| Disease: Prolidase Deficiency |
| Reference #: P12955 (UniProtKB) |
| Alt. Names/Synonyms: aminoacyl-L-proline hydrolase; Imidodipeptidase; MGC10905; PEPD; Peptidase D; PRD; Prolidase; Proline dipeptidase; testicular tissue protein Li 138; X-Pro dipeptidase; Xaa-Pro dipeptidase |
| Gene Symbols: PEPD |
| Molecular weight: 54,548 Da |
| Basal Isoelectric point: 5.64 Predict pI for various phosphorylation states |
| Select Structure to View Below |
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peptidase D |
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Cross-references to other databases:
AlphaFold
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STRING
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cBioPortal
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Wikipedia
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Protein Atlas
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BioGPS
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Pfam
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