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Protein

Dipeptidase 1

Gene

DPEP1

Organism
Sus scrofa (Pig)
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

Enzyme regulationi

Inhibited by L-penicillamine.By similarity

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-9981.

Protein family/group databases

MEROPSiM19.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidase 1 (EC:3.4.13.19)
Alternative name(s):
Microsomal dipeptidase
Renal dipeptidase
Gene namesi
Name:DPEP1
Synonyms:RDP
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • apical part of cell Source: UniProtKB
  • apical plasma membrane Source: UniProtKB-SubCell
  • endoplasmic reticulum membrane 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16161 PublicationAdd
BLAST
Chaini17 – 384368Dipeptidase 1PRO_0000018656Add
BLAST
Propeptidei385 – 40925Removed in mature formBy similarityPRO_0000018657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)1 Publication
Disulfide bondi87 ↔ 170PROSITE-ProRule annotation
Disulfide bondi242 ↔ 274PROSITE-ProRule annotation
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi377 – 377Interchain
Lipidationi384 – 3841GPI-anchor amidated serine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Structurei

3D structure databases

ProteinModelPortaliP22412.
SMRiP22412. Positions 17-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG002339.
InParanoidiP22412.
KOiK01273.

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.

P22412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWTSWWLWPL VAVCAADQFR DLAVRIMQDT PVIDGHNDLP WQLLNLFNNQ
60 70 80 90 100
LQDPGANLSS LAHTHTNIPK LKAGFVGGQF WSAYVPCDTQ NRDAVKRTLE
110 120 130 140 150
QIDVIQRMCQ AYPETFACVT SSTGIRQAFR EGKVASLVGV EGGHSIDSSL
160 170 180 190 200
GVLRALYHLG MRYMTLTHSC NTPWADNWLV DTGDDKAQSQ GLSHFGQSVV
210 220 230 240 250
KEMNRLGVMI DLAHVSVATM RAALKLSQAP VIFSHSSAYS LCPHRRNVPD
260 270 280 290 300
DVLQLVKETG SLVMVNFYND YVSCSAKANL SQVADHLDHI KKVAGAAAVG
310 320 330 340 350
FGGDYDGVSR VPSGLEDVSK YPDLVAELLR RQWTEAEVRG ALADNLLRVF
360 370 380 390 400
EAVEQASNHA QVPGEEPIPL GQLEASCRTN YGYSAAPSLH LPPGSLLASL

VPLLLLSLP
Length:409
Mass (Da):44,700
Last modified:August 1, 1991 - v1
Checksum:i926B7F0044FA055F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53730 mRNA. Translation: CAA37762.1.
D13142 mRNA. Translation: BAA02433.1.
PIRiJS0759.
RefSeqiNP_999273.1. NM_214108.1.
UniGeneiSsc.315.

Genome annotation databases

GeneIDi397196.
KEGGissc:397196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53730 mRNA. Translation: CAA37762.1.
D13142 mRNA. Translation: BAA02433.1.
PIRiJS0759.
RefSeqiNP_999273.1. NM_214108.1.
UniGeneiSsc.315.

3D structure databases

ProteinModelPortaliP22412.
SMRiP22412. Positions 17-385.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP22412.
ChEMBLiCHEMBL2626.

Protein family/group databases

MEROPSiM19.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397196.
KEGGissc:397196.

Organism-specific databases

CTDi1800.

Phylogenomic databases

HOVERGENiHBG002339.
InParanoidiP22412.
KOiK01273.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-9981.

Miscellaneous databases

PROiP22412.

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]
ProtoNetiSearch...

Publicationsi

  1. "cDNA cloning and expression in Xenopus laevis oocytes of pig renal dipeptidase, a glycosyl-phosphatidylinositol-anchored ectoenzyme."
    Rached E., Hooper N.M., James P., Semenza G., Turner A.J., Mantei N.
    Biochem. J. 271:755-760(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-57.
    Tissue: Kidney cortex.
  2. "Purification and cDNA cloning for porcine renal dipeptidase."
    Satoh S., Koyama S., Ohtuka K., Keida Y., Niwa M., Kohsaka M.
    Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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 17-39.
  4. "Site-directed mutagenesis of conserved cysteine residues in porcine membrane dipeptidase. Cys-361 alone is involved in disulfide-linked dimerization."
    Keynan S., Habgood N.T., Hooper N.M., Turner A.J.
    Biochemistry 35:12511-12517(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERCHAIN DISULFIDE BOND.
  5. "Isolation and characterization of glycosylphosphatidylinositol-anchored peptides by hydrophilic interaction chromatography and MALDI tandem mass spectrometry."
    Omaetxebarria M.J., Hagglund P., Elortza F., Hooper N.M., Arizmendi J.M., Jensen O.N.
    Anal. Chem. 78:3335-3341(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR AT SER-384, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiDPEP1_PIG
AccessioniPrimary (citable) accession number: P22412
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 29, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.