Dipeptidase 1

Details

Name
Dipeptidase 1
Synonyms
  • 3.4.13.19
  • Dehydropeptidase-I
  • hRDP
  • MDP
  • Microsomal dipeptidase
  • RDP
  • Renal dipeptidase
Gene Name
DPEP1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0010801|Dipeptidase 1
MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTT
LAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETFLYVT
SSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWADNWLV
DTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVATMKATLQLSRAPVIFSHSSAYS
VCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGARAVG
FGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWTEAEVKGALADNLLRVFEAVEQASNLT
QAPEEEPIPLDQLGGSCRTHYGYSSGASSLHRHWGLLLASLAPLVLCLSLL
Number of residues
411
Molecular Weight
45673.48
Theoretical pI
6.09
GO Classification
Functions
cysteine-type endopeptidase inhibitor activity involved in apoptotic process / dipeptidyl-peptidase activity / GPI anchor binding / metallodipeptidase activity / metalloexopeptidase activity / modified amino acid binding / zinc ion binding
Processes
antibiotic metabolic process / arachidonic acid metabolic process / cellular lactam catabolic process / cellular response to calcium ion / cellular response to drug / cellular response to nitric oxide / glutathione metabolic process / homocysteine metabolic process / leukotriene metabolic process / negative regulation of apoptotic process / negative regulation of cell migration / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / small molecule metabolic process / xenobiotic metabolic process
Components
anchored component of membrane / apical part of cell / apical plasma membrane / extracellular exosome / extracellular space / microvillus membrane / plasma membrane
General Function
Zinc ion binding
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Apical cell membrane
Gene sequence
>lcl|BSEQ0010802|Dipeptidase 1 (DPEP1)
ATGTGGAGCGGATGGTGGCTGTGGCCCCTTGTGGCCGTCTGCACTGCAGACTTCTTTCGG
GACGAGGCAGAGAGGATCATGAGGGACTCCCCTGTCATTGATGGGCACAATGACCTCCCC
TGGCAGCTGCTGGATATGTTCAACAACCGGCTGCAGGACGAGAGGGCCAACCTGACCACC
TTGGCCGGCACACACACCAACATCCCCAAGCTGAGGGCCGGCTTTGTGGGAGGCCAGTTC
TGGTCCGTGTACACGCCCTGCGACACCCAGAACAAAGACGCCGTGCGGAGGACGCTGGAG
CAGATGGACGTGGTCCACCGCATGTGCCGGATGTACCCGGAGACCTTCCTGTATGTCACC
AGCAGTGCAGGCATTCGGCAGGCCTTCCGGGAAGGGAAGGTGGCCAGCCTGATCGGCGTG
GAGGGCGGCCACTCCATTGACAGCAGTTTGGGCGTCCTGCGGGCACTCTATCAGCTGGGC
ATGCGGTACCTGACCCTCACCCACAGCTGCAACACGCCCTGGGCTGACAACTGGCTGGTG
GACACGGGAGACAGCGAGCCCCAGAGCCAAGGCTTGTCACCCTTTGGGCAGCGTGTGGTG
AAGGAGCTGAACCGTCTGGGGGTCCTCATCGACTTGGCTCACGTGTCTGTGGCCACCATG
AAGGCCACCCTGCAGCTGTCCAGAGCCCCGGTCATCTTCAGCCACTCCTCGGCCTACAGC
GTGTGCGCAAGCCGGCGCAACGTGCCTGACGACGTCCTGAGGCTGGTGAAACAGACAGAC
AGCCTGGTGATGGTGAACTTCTACAACAATTACATTTCCTGCACCAACAAGGCCAACCTG
TCCCAAGTGGCCGACCATCTGGATCACATCAAGGAGGTGGCAGGAGCCAGAGCCGTGGGT
TTTGGTGGGGACTTTGATGGTGTTCCAAGGGTCCCTGAGGGGCTGGAGGACGTCTCCAAG
TATCCAGACCTGATCGCTGAGCTGCTCAGGAGGAACTGGACGGAGGCGGAGGTCAAGGGC
GCACTGGCTGACAACCTGCTGAGGGTCTTCGAGGCTGTGGAACAGGCCAGCAACCTCACA
CAGGCTCCCGAGGAGGAGCCCATCCCGCTGGACCAGCTGGGTGGCTCCTGCAGGACCCAT
TACGGCTACTCCTCTGGGGCTTCCAGCCTCCATCGCCACTGGGGGCTCCTGCTGGCCTCC
CTCGCTCCCCTGGTCCTCTGTCTGTCTCTCCTGTGA
Chromosome Location
16
Locus
16q24.3
External Identifiers
ResourceLink
UniProtKB IDP16444
UniProtKB Entry NameDPEP1_HUMAN
GenBank Protein ID219600
GenBank Gene IDD13137
GenAtlas IDDPEP1
HGNC IDHGNC:3002
General References
  1. 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. [Article]
  2. 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. [Article]
  3. 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. [Article]
  4. 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. [Article]
  5. 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. [Article]
  6. 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. [Article]
  7. 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. [Article]
  8. 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. [Article]
  9. 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. [Article]
  10. 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. [Article]
  11. 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. [Article]
  12. 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. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01597Cilastatinapproved, investigationalyesinhibitorDetails
DB06211Doripenemapproved, investigationalnosubstrateDetails
DB01598ImipenemapprovedunknownsubstrateDetails
DB03424UbenimexinvestigationalunknowninhibitorDetails
DB00760Meropenemapproved, investigationalnosubstrateDetails