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P16444

- DPEP1_HUMAN

UniProt

P16444 - DPEP1_HUMAN

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Protein

Dipeptidase 1

Gene
DPEP1, MDP, RDP
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Cofactori

Zinc.1 Publication

Enzyme regulationi

Inhibited by L-penicillamine By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361Zinc 1; catalytic
Metal bindingi38 – 381Zinc 1; catalytic
Metal bindingi141 – 1411Zinc 1; catalytic
Metal bindingi141 – 1411Zinc 2; catalytic
Binding sitei168 – 1681Substrate
Metal bindingi214 – 2141Zinc 2; catalytic
Metal bindingi235 – 2351Zinc 2; catalytic
Binding sitei246 – 2461Substrate
Binding sitei304 – 3041Substrate

GO - Molecular functioni

  1. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  2. dipeptidyl-peptidase activity Source: InterPro
  3. GPI anchor binding Source: UniProtKB
  4. metallodipeptidase activity Source: UniProtKB
  5. metalloexopeptidase activity Source: UniProtKB
  6. modified amino acid binding Source: UniProtKB
  7. protein binding Source: IntAct
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. antibiotic metabolic process Source: UniProtKB
  2. arachidonic acid metabolic process Source: Reactome
  3. cellular lactam catabolic process Source: UniProtKB
  4. cellular response to calcium ion Source: UniProtKB
  5. cellular response to drug Source: UniProtKB
  6. cellular response to nitric oxide Source: UniProtKB
  7. glutathione metabolic process Source: UniProtKB
  8. homocysteine metabolic process Source: UniProtKB
  9. leukotriene metabolic process Source: Reactome
  10. negative regulation of apoptotic process Source: UniProtKB
  11. negative regulation of cell migration Source: UniProtKB
  12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  13. small molecule 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.
ReactomeiREACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
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
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:3002. DPEP1.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. apical part of cell Source: UniProtKB
  3. apical plasma membrane Source: UniProtKB-SubCell
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. microvillus membrane Source: UniProtKB-SubCell
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi141 – 1411E → D or C: Complete loss of activity.
Mutagenesisi141 – 1411E → Q: Partial loss of activity.

Organism-specific databases

PharmGKBiPA144.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16163 PublicationsAdd
BLAST
Chaini17 – 385369Dipeptidase 1PRO_0000018652Add
BLAST
Propeptidei386 – 41126Removed in mature formPRO_0000018653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)2 Publications
Disulfide bondi87 ↔ 1701 Publication
Disulfide bondi242 ↔ 2741 Publication
Glycosylationi279 – 2791N-linked (GlcNAc...)1 Publication
Glycosylationi332 – 3321N-linked (GlcNAc...)1 Publication
Glycosylationi358 – 3581N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi377 – 377Interchain1 Publication
Lipidationi385 – 3851GPI-anchor amidated serine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP16444.
PaxDbiP16444.
PRIDEiP16444.

PTM databases

PhosphoSiteiP16444.

Expressioni

Gene expression databases

ArrayExpressiP16444.
BgeeiP16444.
CleanExiHS_DPEP1.
GenevestigatoriP16444.

Organism-specific databases

HPAiHPA009426.
HPA012783.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KIAA1279Q96EK52EBI-749514,EBI-744150

Protein-protein interaction databases

BioGridi108134. 2 interactions.
IntActiP16444. 1 interaction.
MINTiMINT-5000950.
STRINGi9606.ENSP00000261615.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 2710
Beta strandi32 – 376
Helixi39 – 479
Helixi54 – 563
Turni58 – 603
Beta strandi63 – 653
Helixi68 – 736
Beta strandi76 – 838
Helixi87 – 893
Turni90 – 934
Helixi94 – 11118
Turni113 – 1153
Beta strandi116 – 1183
Helixi122 – 13110
Beta strandi134 – 1418
Helixi143 – 1464
Helixi150 – 1589
Beta strandi161 – 1666
Beta strandi168 – 1703
Beta strandi173 – 1753
Helixi178 – 1803
Turni181 – 1833
Beta strandi188 – 1925
Helixi194 – 20613
Beta strandi209 – 2113
Helixi217 – 22610
Beta strandi232 – 2354
Turni239 – 2413
Helixi250 – 25910
Beta strandi262 – 2654
Helixi269 – 2724
Beta strandi274 – 2763
Helixi280 – 29415
Helixi296 – 2983
Beta strandi299 – 3013
Turni305 – 3073
Helixi321 – 33010
Helixi335 – 3428
Helixi344 – 35613
Beta strandi359 – 3613
Helixi370 – 3723
Beta strandi375 – 3773
Turni381 – 3833

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITQX-ray2.30A/B17-385[»]
1ITUX-ray2.00A/B17-385[»]
ProteinModelPortaliP16444.
SMRiP16444. Positions 17-385.

Miscellaneous databases

EvolutionaryTraceiP16444.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2355.
HOGENOMiHOG000072016.
HOVERGENiHBG002339.
InParanoidiP16444.
KOiK01273.
OMAiGHYATAM.
PhylomeDBiP16444.
TreeFamiTF324523.

Family and domain databases

InterProiIPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERiPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
PfamiPF01244. Peptidase_M19. 1 hit.
[Graphical view]
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

MWSGWWLWPL VAVCTADFFR DEAERIMRDS PVIDGHNDLP WQLLDMFNNR    50
LQDERANLTT LAGTHTNIPK LRAGFVGGQF WSVYTPCDTQ NKDAVRRTLE 100
QMDVVHRMCR MYPETFLYVT SSAGIRQAFR EGKVASLIGV EGGHSIDSSL 150
GVLRALYQLG MRYLTLTHSC NTPWADNWLV DTGDSEPQSQ GLSPFGQRVV 200
KELNRLGVLI DLAHVSVATM KATLQLSRAP VIFSHSSAYS VCASRRNVPD 250
DVLRLVKQTD SLVMVNFYNN YISCTNKANL SQVADHLDHI KEVAGARAVG 300
FGGDFDGVPR VPEGLEDVSK YPDLIAELLR RNWTEAEVKG ALADNLLRVF 350
EAVEQASNLT QAPEEEPIPL DQLGGSCRTH YGYSSGASSL HRHWGLLLAS 400
LAPLVLCLSL L 411
Length:411
Mass (Da):45,674
Last modified:March 7, 2006 - v3
Checksum:iC8C6474C3479D20D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti246 – 2461R → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036496
Natural varianti351 – 3511E → K.
Corresponds to variant rs1126464 [ dbSNP | Ensembl ].
VAR_061375
Natural varianti351 – 3511E → Q.
Corresponds to variant rs1126464 [ dbSNP | Ensembl ].
VAR_061376

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91P → S1 Publication
Sequence conflicti9 – 91P → S1 Publication
Sequence conflicti102 – 1021M → R1 Publication
Sequence conflicti125 – 1251I → R1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005256285.2.
XP_005256343.1. XM_005256286.1.
UniGeneiHs.109.

Genome annotation databases

EnsembliENST00000261615; ENSP00000261615; ENSG00000015413.
ENST00000393092; ENSP00000376807; ENSG00000015413.
ENST00000421184; ENSP00000397313; ENSG00000015413.
GeneIDi1800.
KEGGihsa:1800.
UCSCiuc002fnr.4. human.

Polymorphism databases

DMDMi92090943.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10982.1.
PIRi S29848.
RefSeqi NP_001121613.1. NM_001128141.2.
NP_004404.1. NM_004413.3.
XP_005256342.1. XM_005256285.2.
XP_005256343.1. XM_005256286.1.
UniGenei Hs.109.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ITQ X-ray 2.30 A/B 17-385 [» ]
1ITU X-ray 2.00 A/B 17-385 [» ]
ProteinModelPortali P16444.
SMRi P16444. Positions 17-385.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108134. 2 interactions.
IntActi P16444. 1 interaction.
MINTi MINT-5000950.
STRINGi 9606.ENSP00000261615.

Chemistry

BindingDBi P16444.
ChEMBLi CHEMBL1989.
DrugBanki DB01597. Cilastatin.

Protein family/group databases

MEROPSi M19.001.

PTM databases

PhosphoSitei P16444.

Polymorphism databases

DMDMi 92090943.

Proteomic databases

MaxQBi P16444.
PaxDbi P16444.
PRIDEi P16444.

Protocols and materials databases

DNASUi 1800.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261615 ; ENSP00000261615 ; ENSG00000015413 .
ENST00000393092 ; ENSP00000376807 ; ENSG00000015413 .
ENST00000421184 ; ENSP00000397313 ; ENSG00000015413 .
GeneIDi 1800.
KEGGi hsa:1800.
UCSCi uc002fnr.4. human.

Organism-specific databases

CTDi 1800.
GeneCardsi GC16P089679.
HGNCi HGNC:3002. DPEP1.
HPAi HPA009426.
HPA012783.
MIMi 179780. gene.
neXtProti NX_P16444.
PharmGKBi PA144.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2355.
HOGENOMi HOG000072016.
HOVERGENi HBG002339.
InParanoidi P16444.
KOi K01273.
OMAi GHYATAM.
PhylomeDBi P16444.
TreeFami TF324523.

Enzyme and pathway databases

BioCyci MetaCyc:HS00367-MONOMER.
Reactomei REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
SABIO-RK P16444.

Miscellaneous databases

EvolutionaryTracei P16444.
GeneWikii Dipeptidase_1.
GenomeRNAii 1800.
NextBioi 7331.
PROi P16444.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16444.
Bgeei P16444.
CleanExi HS_DPEP1.
Genevestigatori P16444.

Family and domain databases

InterProi IPR000180. Dipep_AS.
IPR028536. Dpep1.
IPR008257. Renal_dipep_fam.
[Graphical view ]
PANTHERi PTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
Pfami PF01244. Peptidase_M19. 1 hit.
[Graphical view ]
PROSITEi PS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and structural analysis of genomic DNA for human renal dipeptidase."
    Satoh S., Kusunoki C., Konta Y., Niwa M., Kohsaka M.
    Biochim. Biophys. Acta 1172:181-183(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  2. "Primary structure of human microsomal dipeptidase deduced from molecular cloning."
    Adachi H., Tawaragi Y., Inuzuka C., Kubota I., Tsujimoto M., Nishihara T., Nakazato H.
    J. Biol. Chem. 265:3992-3995(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Gene structural analysis and expression of human renal dipeptidase."
    Satoh S., Ohtsuka K., Keida Y., Kusunoki C., Konta Y., Niwa M., Kohsaka M.
    Biotechnol. Prog. 10:134-140(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  7. "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme."
    Hooper N.M., Keen J.N., Turner A.J.
    Biochem. J. 265:429-433(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-56; 111-121 AND 298-310.
  8. "Purification and characterization of human microsomal dipeptidase."
    Adachi H., Kubota I., Okamura N., Iwata H., Tsujimoto M., Nakazato H., Nishihara T., Noguchi T.
    J. Biochem. 105:957-961(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-39.
  9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 17-31.
  10. "Identification of membrane anchoring site of human renal dipeptidase and construction and expression of a cDNA for its secretory form."
    Adachi H., Katayama T., Inuzuka C., Oikawa S., Tsujimoto M., Nakazato H.
    J. Biol. Chem. 265:15341-15345(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR AT SER-385.
  11. "Importance of Glu-125 in the catalytic activity of human renal dipeptidase."
    Adachi H., Katayama T., Nakazato H., Tsujimoto M.
    Biochim. Biophys. Acta 1163:42-48(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY CHEMICAL MODIFICATION.
  12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57 AND ASN-279.
    Tissue: Liver.
  13. "Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis."
    Nitanai Y., Satow Y., Adachi H., Tsujimoto M.
    J. Mol. Biol. 321:177-184(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 17-385 IN COMPLEX WITH ZINC AND CILASTATIN, SUBUNIT, COFACTOR, DISULFIDE BONDS, GLYCOSYLATION AT ASN-57 AND ASN-332.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-246.

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: September 3, 2014
This is version 160 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

External Data

Dasty 3

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