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
- Functionscysteine-type endopeptidase inhibitor activity involved in apoptotic process / dipeptidyl-peptidase activity / GPI anchor binding / metallodipeptidase activity / metalloexopeptidase activity / modified amino acid binding / zinc ion bindingProcessesantibiotic 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 processComponentsanchored 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
- Peptidase_M19 (PF01244)
- 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
Resource Link UniProtKB ID P16444 UniProtKB Entry Name DPEP1_HUMAN GenBank Protein ID 219600 GenBank Gene ID D13137 GenAtlas ID DPEP1 HGNC ID HGNC:3002 - General References
- 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]
- 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]
- 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]
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- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB01597 Cilastatin approved, investigational yes inhibitor Details DB06211 Doripenem approved, investigational no substrate Details DB01598 Imipenem approved unknown substrate Details DB03424 Ubenimex investigational unknown inhibitor Details DB00760 Meropenem approved, investigational no substrate Details DB00303 Ertapenem approved, investigational unknown substrate Details