ID:PEPD_HUMAN DESCRIPTION: RecName: Full=Xaa-Pro dipeptidase; Short=X-Pro dipeptidase; EC=3.4.13.9; AltName: Full=Imidodipeptidase; AltName: Full=Peptidase D; AltName: Full=Proline dipeptidase; Short=Prolidase; FUNCTION: 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. CATALYTIC ACTIVITY: Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro. COFACTOR: Binds 2 manganese ions per subunit. SUBUNIT: Homodimer. MASS SPECTROMETRY: Mass=54251.73; Method=MALDI; Range=2-493; Source=PubMed:11840567; DISEASE: Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:170100]. 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. SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P12955
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.