You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP01772
Secondary Accession Numbers
  • 7125
Name Xaa-Pro dipeptidase
Synonyms
  1. Imidodipeptidase
  2. Peptidase D
  3. Prolidase
  4. Proline dipeptidase
  5. X-Pro dipeptidase
Gene Name PEPD
Protein Type Unknown
Biological Properties
General Function Involved in cellular process
Specific 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
Pathways Not Available
Reactions Not Available
GO Classification
Function
manganese ion binding
metalloexopeptidase activity
exopeptidase activity
aminopeptidase activity
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
transition metal ion binding
peptidase activity
peptidase activity, acting on l-amino acid peptides
metallopeptidase activity
Process
metabolic process
macromolecule metabolic process
cellular process
protein metabolic process
proteolysis
Cellular Location
  1. Cytoplasmic
Gene Properties
Chromosome Location Chromosome:1
Locus 19q13.11
SNPs PEPD
Gene Sequence
>1482 bp
ATGGCGGCGGCCACCGGACCCTCGTTTTGGCTGGGGAATGAAACCCTGAAGGTGCCGCTG
GCGCTCTTTGCCTTGAACCGGCAGCGCCTGTGTGAGCGGCTGCGGAAGAACCCTGCTGTG
CAGGCCGGCTCCATCGTGGTCCTGCAGGGCGGGGAGGAGACTCAGCGCTACTGCACCGAC
ACCGGGGTCCTCTTCCGCCAGGAGTCCTTCTTTCACTGGGCGTTCGGTGTCACTGAGCCA
GGCTGCTATGGTGTCATCGATGTTGACACTGGGAAGTCGACCCTGTTTGTGCCCAGGCTT
CCTGCCAGCCATGCCACCTGGATGGGAAAGATCCATTCCAAGGAGCACTTCAAGGAGAAG
TATGCCGTGGACGACGTCCAGTACGTAGATGAGATTGCCAGCGTCCTGACGTCACAGAAG
CCCTCTGTCCTCCTCACTTTGCGTGGCGTCAACACGGACAGCGGCAGTGTCTGCAGGGAG
GCCTCCTTTGACGGCATCAGCAAGTTCGAAGTCAACAATACCATTCTTCACCCAGAGATC
GTTGAGTGCCGAGTGTTTAAGACGGATATGGAGCTGGAGGTTCTGCGCTATACCAATAAA
ATCTCCAGCGAGGCCCACCGTGAGGTAATGAAGGCTGTAAAAGTGGGAATGAAAGAATAT
GAGTTGGAAAGCCTCTTCGAGCACTACTGCTACTCCCGGGGCGGCATGCGCCACAGCTCC
TACACCTGCATCTGCGGCAGTGGTGAGAACTCAGCCGTGCTACACTACGGACACGCCGGA
GCTCCCAACGACCGAACGATCCAGAATGGGGATATGTGCCTGTTCGACATGGGCGGTGAG
TATTACTGCTTCGCTTCCGACATCACCTGCTCCTTTCCCGCCAACGGCAAGTTCACTGCA
GACCAGAAGGCCGTCTATGAGGCAGTGCTGCGGAGCTCCCGTGCCGTCATGGGTGCCATG
AAGCCAGGTGTCTGGTGGCCTGACATGCACCGCCTGGCTGACCGCATCCACCTGGAGGAG
CTGGCCCACATGGGCATCCTGAGCGGCAGCGTGGACGCCATGGTCCAGGCTCACCTGGGG
GCCGTGTTTATGCCTCACGGGCTTGGCCACTTCCTGGGCATTGACGTGCACGACGTGGGA
GGCTACCCAGAGGGCGTGGAGCGCATCGACGAGCCCGGCCTGCGGAGCCTGCGCACTGCA
CGGCACCTGCAGCCAGGCATGGTGCTCACCGTGGAGCCGGGCATCTACTTCATCGACCAC
CTCCTGGATGAGGCCCTGGCGGACCCGGCCCGCGCCTCCTTCCTTAACCGCGAGGTCCTG
CAGCGCTTTCGCGGTTTTGGCGGGGTCCGCATCGAGGAGGACGTCGTGGTGACTGACAGC
GGCATAGAGCTGCTGACCTGCGTGCCCCGCACTGTGGAAGAGATTGAAGCATGCATGGCA
GGCTGTGACAAGGCCTTTACCCCCTTCTCTGGCCCCAAGTAG
Protein Properties
Number of Residues 493
Molecular Weight 54547.8
Theoretical pI 5.9
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Xaa-Pro dipeptidase
MAAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQRYCTD
TGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHATWMGKIHSKEHFKEK
YAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSGSVCREASFDGISKFEVNNTILHPEI
VECRVFKTDMELEVLRYTNKISSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSS
YTCICGSGENSAVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTA
DQKAVYEAVLRSSRAVMGAMKPGVWWPDMHRLADRIHLEELAHMGILSGSVDAMVQAHLG
AVFMPHGLGHFLGIDVHDVGGYPEGVERIDEPGLRSLRTARHLQPGMVLTVEPGIYFIDH
LLDEALADPARASFLNREVLQRFRGFGGVRIEEDVVVTDSGIELLTCVPRTVEEIEACMA
GCDKAFTPFSGPK
GenBank ID Protein 13279182
UniProtKB/Swiss-Prot ID P12955
UniProtKB/Swiss-Prot Entry Name PEPD_HUMAN
PDB IDs Not Available
GenBank Gene ID BC004305
GeneCard ID PEPD
GenAtlas ID PEPD
HGNC ID HGNC:8840
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed:16097034 ]
  5. Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed:11840567 ]
  6. Endo F, Tanoue A, Nakai H, Hata A, Indo Y, Titani K, Matsuda I: Primary structure and gene localization of human prolidase. J Biol Chem. 1989 Mar 15;264(8):4476-81. [PubMed:2925654 ]
  7. Tanoue A, Endo F, Kitano A, Matsuda I: A single nucleotide change in the prolidase gene in fibroblasts from two patients with polypeptide positive prolidase deficiency. Expression of the mutant enzyme in NIH 3T3 cells. J Clin Invest. 1990 Jul;86(1):351-5. [PubMed:2365824 ]
  8. Ledoux P, Scriver C, Hechtman P: Four novel PEPD alleles causing prolidase deficiency. Am J Hum Genet. 1994 Jun;54(6):1014-21. [PubMed:8198124 ]
  9. Ledoux P, Scriver CR, Hechtman P: Expression and molecular analysis of mutations in prolidase deficiency. Am J Hum Genet. 1996 Nov;59(5):1035-9. [PubMed:8900231 ]
  10. Forlino A, Lupi A, Vaghi P, Icaro Cornaglia A, Calligaro A, Campari E, Cetta G: Mutation analysis of five new patients affected by prolidase deficiency: the lack of enzyme activity causes necrosis-like cell death in cultured fibroblasts. Hum Genet. 2002 Oct;111(4-5):314-22. Epub 2002 Aug 14. [PubMed:12384772 ]