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. Defects in PEPD are a cause of prolidase deficiency (PD). Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait. Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.13.9; Protease
Chromosomal Location of Human Ortholog: 7 B2|7 20.7 cM
Cellular Component:  nucleoplasm; nucleus
Molecular Function:  aminopeptidase activity; dipeptidase activity; hydrolase activity; manganese ion binding; metal ion binding; metallopeptidase activity; peptidase activity; proline dipeptidase activity
Biological Process:  collagen catabolic process; proteolysis
Reference #:  Q11136 (UniProtKB)
Alt. Names/Synonyms: Imidodipeptidase; Pep-4; Pep4; Pepd; Peptidase 4; Peptidase D; Prolidase; Proline dipeptidase; X-Pro dipeptidase; Xaa-Pro dipeptidase
Gene Symbols: Pepd
Molecular weight: 55,029 Da
Basal Isoelectric point: 5.5  Predict pI for various phosphorylation states
Select Structure to View Below

peptidase D

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene