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Protein

Dipeptidase 1

Gene

DPEP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Hydrolysis of dipeptides.PROSITE-ProRule annotation

Cofactori

Zn2+PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Inhibited by L-penicillamine.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi36Zinc 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi38Zinc 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi141Zinc 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi141Zinc 2; catalyticPROSITE-ProRule annotation1 Publication1
Binding sitei168Substrate1
Metal bindingi214Zinc 2; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi235Zinc 2; catalyticPROSITE-ProRule annotation1 Publication1
Binding sitei246Substrate1
Binding sitei304Substrate1

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  • dipeptidase activity Source: Reactome
  • dipeptidyl-peptidase activity Source: InterPro
  • GPI anchor binding Source: UniProtKB
  • metallodipeptidase activity Source: UniProtKB
  • metalloexopeptidase activity Source: UniProtKB
  • modified amino acid binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • antibiotic metabolic process Source: UniProtKB
  • cellular lactam catabolic process Source: UniProtKB
  • cellular response to calcium ion Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • cellular response to nitric oxide Source: UniProtKB
  • glutathione metabolic process Source: UniProtKB
  • homocysteine metabolic process Source: UniProtKB
  • leukotriene metabolic process Source: Reactome
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS00367-MONOMER.
ZFISH:HS00367-MONOMER.
BRENDAi3.4.13.19. 2681.
ReactomeiR-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-5423646. Aflatoxin activation and detoxification.
SABIO-RKP16444.

Protein family/group databases

MEROPSiM19.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 1 (EC:3.4.13.19)
Alternative name(s):
Dehydropeptidase-I
Microsomal dipeptidase
Renal dipeptidase
Short name:
hRDP
Gene namesi
Name:DPEP1
Synonyms:MDP, RDP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:3002. DPEP1.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • apical part of cell Source: UniProtKB
  • apical plasma membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • microvillus membrane Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi141E → D or C: Complete loss of activity. 1
Mutagenesisi141E → Q: Partial loss of activity. 1

Organism-specific databases

DisGeNETi1800.
OpenTargetsiENSG00000015413.
PharmGKBiPA144.

Chemistry databases

ChEMBLiCHEMBL1989.
DrugBankiDB01597. Cilastatin.
DB06211. Doripenem.

Polymorphism and mutation databases

BioMutaiDPEP1.
DMDMi92090943.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 163 PublicationsAdd BLAST16
ChainiPRO_000001865217 – 385Dipeptidase 1Add BLAST369
PropeptideiPRO_0000018653386 – 411Removed in mature formAdd BLAST26

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi57N-linked (GlcNAc...)2 Publications1
Disulfide bondi87 ↔ 170PROSITE-ProRule annotation1 Publication
Disulfide bondi242 ↔ 274PROSITE-ProRule annotation1 Publication
Glycosylationi279N-linked (GlcNAc...)1 Publication1
Glycosylationi332N-linked (GlcNAc...)1 Publication1
Glycosylationi358N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi377InterchainPROSITE-ProRule annotation1 Publication
Lipidationi385GPI-anchor amidated serine1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

EPDiP16444.
MaxQBiP16444.
PaxDbiP16444.
PeptideAtlasiP16444.
PRIDEiP16444.

PTM databases

iPTMnetiP16444.
PhosphoSitePlusiP16444.

Expressioni

Gene expression databases

BgeeiENSG00000015413.
CleanExiHS_DPEP1.
ExpressionAtlasiP16444. baseline and differential.
GenevisibleiP16444. HS.

Organism-specific databases

HPAiHPA009426.
HPA012783.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.PROSITE-ProRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
APPBP2Q926243EBI-749514,EBI-743771
KIF1BPQ96EK52EBI-749514,EBI-744150

Protein-protein interaction databases

BioGridi108134. 55 interactors.
IntActiP16444. 2 interactors.
MINTiMINT-5000950.
STRINGi9606.ENSP00000261615.

Chemistry databases

BindingDBiP16444.

Structurei

Secondary structure

1411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 27Combined sources10
Beta strandi32 – 37Combined sources6
Helixi39 – 47Combined sources9
Helixi54 – 56Combined sources3
Turni58 – 60Combined sources3
Beta strandi63 – 65Combined sources3
Helixi68 – 73Combined sources6
Beta strandi76 – 83Combined sources8
Helixi87 – 89Combined sources3
Turni90 – 93Combined sources4
Helixi94 – 111Combined sources18
Turni113 – 115Combined sources3
Beta strandi116 – 118Combined sources3
Helixi122 – 131Combined sources10
Beta strandi134 – 141Combined sources8
Helixi143 – 146Combined sources4
Helixi150 – 158Combined sources9
Beta strandi161 – 166Combined sources6
Beta strandi168 – 170Combined sources3
Beta strandi173 – 175Combined sources3
Helixi178 – 180Combined sources3
Turni181 – 183Combined sources3
Beta strandi188 – 192Combined sources5
Helixi194 – 206Combined sources13
Beta strandi209 – 211Combined sources3
Helixi217 – 226Combined sources10
Beta strandi232 – 235Combined sources4
Turni239 – 241Combined sources3
Helixi250 – 259Combined sources10
Beta strandi262 – 265Combined sources4
Helixi269 – 272Combined sources4
Beta strandi274 – 276Combined sources3
Helixi280 – 294Combined sources15
Helixi296 – 298Combined sources3
Beta strandi299 – 301Combined sources3
Turni305 – 307Combined sources3
Helixi321 – 330Combined sources10
Helixi335 – 342Combined sources8
Helixi344 – 356Combined sources13
Beta strandi359 – 361Combined sources3
Helixi370 – 372Combined sources3
Beta strandi375 – 377Combined sources3
Turni381 – 383Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ITQX-ray2.30A/B17-385[»]
1ITUX-ray2.00A/B17-385[»]
ProteinModelPortaliP16444.
SMRiP16444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16444.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4127. Eukaryota.
COG2355. LUCA.
GeneTreeiENSGT00390000017920.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiP16444.
KOiK01273.
OMAiAFEDQLG.
OrthoDBiEOG091G09CU.
PhylomeDBiP16444.
TreeFamiTF324523.

Family and domain databases

CDDicd01301. rDP_like. 1 hit.
InterProiIPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR032466. Metal_Hydrolase.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWSGWWLWPL VAVCTADFFR DEAERIMRDS PVIDGHNDLP WQLLDMFNNR
60 70 80 90 100
LQDERANLTT LAGTHTNIPK LRAGFVGGQF WSVYTPCDTQ NKDAVRRTLE
110 120 130 140 150
QMDVVHRMCR MYPETFLYVT SSAGIRQAFR EGKVASLIGV EGGHSIDSSL
160 170 180 190 200
GVLRALYQLG MRYLTLTHSC NTPWADNWLV DTGDSEPQSQ GLSPFGQRVV
210 220 230 240 250
KELNRLGVLI DLAHVSVATM KATLQLSRAP VIFSHSSAYS VCASRRNVPD
260 270 280 290 300
DVLRLVKQTD SLVMVNFYNN YISCTNKANL SQVADHLDHI KEVAGARAVG
310 320 330 340 350
FGGDFDGVPR VPEGLEDVSK YPDLIAELLR RNWTEAEVKG ALADNLLRVF
360 370 380 390 400
EAVEQASNLT QAPEEEPIPL DQLGGSCRTH YGYSSGASSL HRHWGLLLAS
410
LAPLVLCLSL L
Length:411
Mass (Da):45,674
Last modified:March 7, 2006 - v3
Checksum:iC8C6474C3479D20D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9P → S (PubMed:8439558).Curated1
Sequence conflicti9P → S (PubMed:7764673).Curated1
Sequence conflicti102M → R (PubMed:2303490).Curated1
Sequence conflicti125I → R (PubMed:2303490).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036496246R → H in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_061375351E → K.Corresponds to variant rs1126464dbSNPEnsembl.1
Natural variantiVAR_061376351E → Q.Corresponds to variant rs1126464dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13137 Genomic DNA. Translation: BAA02430.1.
J05257 mRNA. Translation: AAB59410.1.
D13138 mRNA. Translation: BAA02431.1.
S70330, S70329 Genomic DNA. Translation: AAC60630.2.
CH471184 Genomic DNA. Translation: EAW66719.1.
CH471184 Genomic DNA. Translation: EAW66720.1.
BC017023 mRNA. Translation: AAH17023.1.
BT006664 mRNA. Translation: AAP35310.1.
CCDSiCCDS10982.1.
PIRiS29848.
RefSeqiNP_001121613.1. NM_001128141.2.
NP_004404.1. NM_004413.3.
XP_005256342.1. XM_005256285.4.
XP_005256343.1. XM_005256286.3.
XP_011521227.1. XM_011522925.2.
UniGeneiHs.109.

Genome annotation databases

EnsembliENST00000261615; ENSP00000261615; ENSG00000015413.
ENST00000393092; ENSP00000376807; ENSG00000015413.
ENST00000421184; ENSP00000397313; ENSG00000015413.
GeneIDi1800.
KEGGihsa:1800.
UCSCiuc002fnr.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13137 Genomic DNA. Translation: BAA02430.1.
J05257 mRNA. Translation: AAB59410.1.
D13138 mRNA. Translation: BAA02431.1.
S70330, S70329 Genomic DNA. Translation: AAC60630.2.
CH471184 Genomic DNA. Translation: EAW66719.1.
CH471184 Genomic DNA. Translation: EAW66720.1.
BC017023 mRNA. Translation: AAH17023.1.
BT006664 mRNA. Translation: AAP35310.1.
CCDSiCCDS10982.1.
PIRiS29848.
RefSeqiNP_001121613.1. NM_001128141.2.
NP_004404.1. NM_004413.3.
XP_005256342.1. XM_005256285.4.
XP_005256343.1. XM_005256286.3.
XP_011521227.1. XM_011522925.2.
UniGeneiHs.109.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ITQX-ray2.30A/B17-385[»]
1ITUX-ray2.00A/B17-385[»]
ProteinModelPortaliP16444.
SMRiP16444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108134. 55 interactors.
IntActiP16444. 2 interactors.
MINTiMINT-5000950.
STRINGi9606.ENSP00000261615.

Chemistry databases

BindingDBiP16444.
ChEMBLiCHEMBL1989.
DrugBankiDB01597. Cilastatin.
DB06211. Doripenem.

Protein family/group databases

MEROPSiM19.001.

PTM databases

iPTMnetiP16444.
PhosphoSitePlusiP16444.

Polymorphism and mutation databases

BioMutaiDPEP1.
DMDMi92090943.

Proteomic databases

EPDiP16444.
MaxQBiP16444.
PaxDbiP16444.
PeptideAtlasiP16444.
PRIDEiP16444.

Protocols and materials databases

DNASUi1800.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261615; ENSP00000261615; ENSG00000015413.
ENST00000393092; ENSP00000376807; ENSG00000015413.
ENST00000421184; ENSP00000397313; ENSG00000015413.
GeneIDi1800.
KEGGihsa:1800.
UCSCiuc002fnr.5. human.

Organism-specific databases

CTDi1800.
DisGeNETi1800.
GeneCardsiDPEP1.
HGNCiHGNC:3002. DPEP1.
HPAiHPA009426.
HPA012783.
MIMi179780. gene.
neXtProtiNX_P16444.
OpenTargetsiENSG00000015413.
PharmGKBiPA144.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4127. Eukaryota.
COG2355. LUCA.
GeneTreeiENSGT00390000017920.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiP16444.
KOiK01273.
OMAiAFEDQLG.
OrthoDBiEOG091G09CU.
PhylomeDBiP16444.
TreeFamiTF324523.

Enzyme and pathway databases

BioCyciMetaCyc:HS00367-MONOMER.
ZFISH:HS00367-MONOMER.
BRENDAi3.4.13.19. 2681.
ReactomeiR-HSA-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-HSA-5423646. Aflatoxin activation and detoxification.
SABIO-RKP16444.

Miscellaneous databases

EvolutionaryTraceiP16444.
GeneWikiiDipeptidase_1.
GenomeRNAii1800.
PROiP16444.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000015413.
CleanExiHS_DPEP1.
ExpressionAtlasiP16444. baseline and differential.
GenevisibleiP16444. HS.

Family and domain databases

CDDicd01301. rDP_like. 1 hit.
InterProiIPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR032466. Metal_Hydrolase.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
PROSITEiPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPEP1_HUMAN
AccessioniPrimary (citable) accession number: P16444
Secondary accession number(s): D3DX80, Q96AK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: March 7, 2006
Last modified: November 30, 2016
This is version 182 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.