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Protein Page:
peptidase D

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; Protease
Chromosomal Location of Human Ortholog: 19q13.11
Molecular Function: metallocarboxypeptidase activity; protein binding
Biological Process: amino acid metabolic process
Disease: Prolidase Deficiency
Reference #:  P12955 (UniProtKB)
Alt. Names/Synonyms: aminoacyl-L-proline hydrolase; Imidodipeptidase; MGC10905; PEPD; Peptidase D; PRD; Prolidase; Proline dipeptidase; 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
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peptidase D

Protein Structure Not Found.
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