CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004465
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dipeptidase 1 
Protein Synonyms/Alias
 Dehydropeptidase-I; Microsomal dipeptidase; Renal dipeptidase; hRDP 
Gene Name
 DPEP1 
Gene Synonyms/Alias
 MDP; RDP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
320EGLEDVSKYPDLIAEubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 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. 
Sequence Annotation
 METAL 36 36 Zinc 1; catalytic.
 METAL 38 38 Zinc 1; catalytic.
 METAL 141 141 Zinc 1; catalytic.
 METAL 141 141 Zinc 2; catalytic.
 METAL 214 214 Zinc 2; catalytic.
 METAL 235 235 Zinc 2; catalytic.
 BINDING 168 168 Substrate.
 BINDING 246 246 Substrate.
 BINDING 304 304 Substrate.
 LIPID 385 385 GPI-anchor amidated serine.
 CARBOHYD 57 57 N-linked (GlcNAc...).
 CARBOHYD 279 279 N-linked (GlcNAc...).
 CARBOHYD 332 332 N-linked (GlcNAc...).
 CARBOHYD 358 358 N-linked (GlcNAc...) (Potential).
 DISULFID 87 170
 DISULFID 242 274
 DISULFID 377 377 Interchain.  
Keyword
 3D-structure; Cell membrane; Cell projection; Complete proteome; Dipeptidase; Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Signal; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 411 AA 
Protein Sequence
MWSGWWLWPL VAVCTADFFR DEAERIMRDS PVIDGHNDLP WQLLDMFNNR LQDERANLTT 60
LAGTHTNIPK LRAGFVGGQF WSVYTPCDTQ NKDAVRRTLE QMDVVHRMCR MYPETFLYVT 120
SSAGIRQAFR EGKVASLIGV EGGHSIDSSL GVLRALYQLG MRYLTLTHSC NTPWADNWLV 180
DTGDSEPQSQ GLSPFGQRVV KELNRLGVLI DLAHVSVATM KATLQLSRAP VIFSHSSAYS 240
VCASRRNVPD DVLRLVKQTD SLVMVNFYNN YISCTNKANL SQVADHLDHI KEVAGARAVG 300
FGGDFDGVPR VPEGLEDVSK YPDLIAELLR RNWTEAEVKG ALADNLLRVF EAVEQASNLT 360
QAPEEEPIPL DQLGGSCRTH YGYSSGASSL HRHWGLLLAS LAPLVLCLSL L 411 
Gene Ontology
 GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
 GO:0045177; C:apical part of cell; IDA:UniProtKB.
 GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005615; C:extracellular space; ISS:UniProtKB.
 GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
 GO:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro.
 GO:0034235; F:GPI anchor binding; ISS:UniProtKB.
 GO:0070573; F:metallodipeptidase activity; IDA:UniProtKB.
 GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0016999; P:antibiotic metabolic process; IDA:UniProtKB.
 GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome.
 GO:0072340; P:cellular lactam catabolic process; TAS:UniProtKB.
 GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
 GO:0035690; P:cellular response to drug; IDA:UniProtKB.
 GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
 GO:0006749; P:glutathione metabolic process; TAS:UniProtKB.
 GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
 GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR000180; Pept_M19_AS.
 IPR008257; Peptidase_M19. 
Pfam
 PF01244; Peptidase_M19 
SMART
  
PROSITE
 PS00869; RENAL_DIPEPTIDASE_1
 PS51365; RENAL_DIPEPTIDASE_2 
PRINTS