Description: Homo sapiens peptidase D (PEPD), transcript variant 1, mRNA. RefSeq Summary (NM_000285): This gene encodes a member of the peptidase family. The protein forms a homodimer that hydrolyzes dipeptides or tripeptides with C-terminal proline or hydroxyproline residues. The enzyme serves an important role in the recycling of proline, and may be rate limiting for the production of collagen. Mutations in this gene result in prolidase deficiency, which is characterized by the excretion of large amount of di- and tri-peptides containing proline. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Oct 2009]. Transcript (Including UTRs) Position: hg19 chr19:33,877,855-34,012,799 Size: 134,945 Total Exon Count: 15 Strand: - Coding Region Position: hg19 chr19:33,878,250-34,012,666 Size: 134,417 Coding Exon Count: 15
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.
Adiponectin Zari Dastani et al. PLoS genetics 2012, Novel loci for adiponectin levels and their influence on type 2 diabetes and metabolic traits: a multi-ethnic meta-analysis of 45,891 individuals., PLoS genetics.
[PubMed 22479202]
Adiponectin Zari Dastani et al. PLoS genetics 2012, Novel loci for adiponectin levels and their influence on type 2 diabetes and metabolic traits: a multi-ethnic meta-analysis of 45,891 individuals., PLoS genetics.
[PubMed 22479202]
Diabetes Mellitus, Type 2 Yoon Shin Cho et al. Nature genetics 2012, Meta-analysis of genome-wide association studies identifies eight new loci for type 2 diabetes in east Asians., Nature genetics.
[PubMed 22158537]
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
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
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.