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Identification
HMDB Protein ID HMDBP02684
Secondary Accession Numbers
  • 8187
Name Dipeptidase 1
Synonyms
  1. Dehydropeptidase-I
  2. Microsomal dipeptidase
  3. Renal dipeptidase
  4. hRDP
Gene Name DPEP1
Protein Type Unknown
Biological Properties
General Function Involved in metalloexopeptidase activity
Specific Function Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity
Pathways Not Available
Reactions Not Available
GO Classification
Function
metalloexopeptidase activity
exopeptidase activity
catalytic activity
hydrolase activity
dipeptidase activity
dipeptidyl-peptidase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
metallopeptidase activity
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Lipid-anchor
  2. Lipid-anchor
  3. Apical cell membrane
  4. GPI- anchor
  5. GPI- anchor
  6. Cell projection
  7. microvillus membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 16q24.3
SNPs DPEP1
Gene Sequence
>1236 bp
ATGTGGAGCGGATGGTGGCTGTGGCCCCTTGTGGCCGTCTGCACTGCAGACTTCTTTCGG
GACGAGGCAGAGAGGATCATGAGGGACTCCCCTGTCATTGATGGGCACAATGACCTCCCC
TGGCAGCTGCTGGATATGTTCAACAACCGGCTGCAGGACGAGAGGGCCAACCTGACCACC
TTGGCCGGCACACACACCAACATCCCCAAGCTGAGGGCCGGCTTTGTGGGAGGCCAGTTC
TGGTCCGTGTACACGCCCTGCGACACCCAGAACAAAGACGCCGTGCGGAGGACGCTGGAG
CAGATGGACGTGGTCCACCGCATGTGCCGGATGTACCCGGAGACCTTCCTGTATGTCACC
AGCAGTGCAGGCATTCGGCAGGCCTTCCGGGAAGGGAAGGTGGCCAGCCTGATCGGCGTG
GAGGGCGGCCACTCCATTGACAGCAGTTTGGGCGTCCTGCGGGCACTCTATCAGCTGGGC
ATGCGGTACCTGACCCTCACCCACAGCTGCAACACGCCCTGGGCTGACAACTGGCTGGTG
GACACGGGAGACAGCGAGCCCCAGAGCCAAGGCTTGTCACCCTTTGGGCAGCGTGTGGTG
AAGGAGCTGAACCGTCTGGGGGTCCTCATCGACTTGGCTCACGTGTCTGTGGCCACCATG
AAGGCCACCCTGCAGCTGTCCAGAGCCCCGGTCATCTTCAGCCACTCCTCGGCCTACAGC
GTGTGCGCAAGCCGGCGCAACGTGCCTGACGACGTCCTGAGGCTGGTGAAACAGACAGAC
AGCCTGGTGATGGTGAACTTCTACAACAATTACATTTCCTGCACCAACAAGGCCAACCTG
TCCCAAGTGGCCGACCATCTGGATCACATCAAGGAGGTGGCAGGAGCCAGAGCCGTGGGT
TTTGGTGGGGACTTTGATGGTGTTCCAAGGGTCCCTGAGGGGCTGGAGGACGTCTCCAAG
TATCCAGACCTGATCGCTGAGCTGCTCAGGAGGAACTGGACGGAGGCGGAGGTCAAGGGC
GCACTGGCTGACAACCTGCTGAGGGTCTTCGAGGCTGTGGAACAGGCCAGCAACCTCACA
CAGGCTCCCGAGGAGGAGCCCATCCCGCTGGACCAGCTGGGTGGCTCCTGCAGGACCCAT
TACGGCTACTCCTCTGGGGCTTCCAGCCTCCATCGCCACTGGGGGCTCCTGCTGGCCTCC
CTCGCTCCCCTGGTCCTCTGTCTGTCTCTCCTGTGA
Protein Properties
Number of Residues 411
Molecular Weight 45673.5
Theoretical pI 6.09
Pfam Domain Function
Signals
  • 1-16
Transmembrane Regions
  • None
Protein Sequence
>Dipeptidase 1
MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTT
LAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETFLYVT
SSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWADNWLV
DTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVATMKATLQLSRAPVIFSHSSAYS
VCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGARAVG
FGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWTEAEVKGALADNLLRVFEAVEQASNLT
QAPEEEPIPLDQLGGSCRTHYGYSSGASSLHRHWGLLLASLAPLVLCLSLL
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P16444
UniProtKB/Swiss-Prot Entry Name DPEP1_HUMAN
PDB IDs
GenBank Gene ID J05257
GeneCard ID DPEP1
GenAtlas ID DPEP1
HGNC ID HGNC:3002
References
General References
  1. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218 ]
  2. 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 ]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
  4. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed:15340161 ]
  5. Satoh S, Kusunoki C, Konta Y, Niwa M, Kohsaka M: Cloning and structural analysis of genomic DNA for human renal dipeptidase. Biochim Biophys Acta. 1993 Feb 20;1172(1-2):181-3. [PubMed:8439558 ]
  6. Adachi H, Tawaragi Y, Inuzuka C, Kubota I, Tsujimoto M, Nishihara T, Nakazato H: Primary structure of human microsomal dipeptidase deduced from molecular cloning. J Biol Chem. 1990 Mar 5;265(7):3992-5. [PubMed:2303490 ]
  7. Satoh S, Ohtsuka K, Keida Y, Kusunoki C, Konta Y, Niwa M, Kohsaka M: Gene structural analysis and expression of human renal dipeptidase. Biotechnol Prog. 1994 Mar-Apr;10(2):134-40. [PubMed:7764673 ]
  8. Hooper NM, Keen JN, Turner AJ: Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme. Biochem J. 1990 Jan 15;265(2):429-33. [PubMed:2137335 ]
  9. Adachi H, Kubota I, Okamura N, Iwata H, Tsujimoto M, Nakazato H, Nishihara T, Noguchi T: Purification and characterization of human microsomal dipeptidase. J Biochem. 1989 Jun;105(6):957-61. [PubMed:2768222 ]
  10. Adachi H, Katayama T, Inuzuka C, Oikawa S, Tsujimoto M, Nakazato H: Identification of membrane anchoring site of human renal dipeptidase and construction and expression of a cDNA for its secretory form. J Biol Chem. 1990 Sep 5;265(25):15341-5. [PubMed:2168407 ]
  11. Adachi H, Katayama T, Nakazato H, Tsujimoto M: Importance of Glu-125 in the catalytic activity of human renal dipeptidase. Biochim Biophys Acta. 1993 Apr 21;1163(1):42-8. [PubMed:8097406 ]
  12. Nitanai Y, Satow Y, Adachi H, Tsujimoto M: Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis. J Mol Biol. 2002 Aug 9;321(2):177-84. [PubMed:12144777 ]