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P22412 (DPEP1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dipeptidase 1

EC=3.4.13.19
Alternative name(s):
Microsomal dipeptidase
Renal dipeptidase
Gene names
Name:DPEP1
Synonyms:RDP
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

Hydrolysis of dipeptides.

Cofactor

Zinc.

Enzyme regulation

Inhibited by L-penicillamine By similarity.

Subunit structure

Homodimer; disulfide-linked. Ref.4

Subcellular location

Apical cell membrane; Lipid-anchorGPI-anchor. Cell projectionmicrovillus membrane; Lipid-anchorGPI-anchor. Note: Brush border membrane.

Sequence similarities

Belongs to the peptidase M19 family.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Membrane
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionDipeptidase
Hydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGPI anchor release

Inferred from direct assay PubMed 17615681. Source: UniProtKB

antibiotic metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to calcium ion

Inferred from direct assay PubMed 11139399PubMed 17615681. Source: UniProtKB

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin stimulus

Inferred from direct assay PubMed 17615681. Source: UniProtKB

cellular response to nitric oxide

Inferred from direct assay PubMed 11988094. Source: UniProtKB

homocysteine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

apical part of cell

Inferred from sequence or structural similarity. Source: UniProtKB

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from direct assay PubMed 17615681. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 11139399. Source: UniProtKB

microvillus membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 11139399PubMed 11988094PubMed 17615681. Source: UniProtKB

   Molecular_functionGPI anchor binding

Inferred from direct assay PubMed 11139399PubMed 11988094. Source: UniProtKB

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

dipeptidyl-peptidase activity

Inferred from electronic annotation. Source: InterPro

metallodipeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

modified amino acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.3
Chain17 – 384368Dipeptidase 1
PRO_0000018656
Propeptide385 – 40925Removed in mature form By similarity
PRO_0000018657

Sites

Metal binding361Zinc 1; catalytic By similarity
Metal binding381Zinc 1; catalytic By similarity
Metal binding1411Zinc 1; catalytic By similarity
Metal binding1411Zinc 2; catalytic By similarity
Metal binding2141Zinc 2; catalytic By similarity
Metal binding2351Zinc 2; catalytic By similarity
Binding site1681Substrate By similarity
Binding site2461Substrate By similarity
Binding site3041Substrate By similarity

Amino acid modifications

Lipidation3841GPI-anchor amidated serine Ref.5
Glycosylation571N-linked (GlcNAc...) Ref.1
Glycosylation2791N-linked (GlcNAc...) Potential
Disulfide bond87 ↔ 170 By similarity
Disulfide bond242 ↔ 274 By similarity
Disulfide bond377Interchain Ref.4

Sequences

Sequence LengthMass (Da)Tools
P22412 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 926B7F0044FA055F

FASTA40944,700
        10         20         30         40         50         60 
MWTSWWLWPL VAVCAADQFR DLAVRIMQDT PVIDGHNDLP WQLLNLFNNQ LQDPGANLSS 

        70         80         90        100        110        120 
LAHTHTNIPK LKAGFVGGQF WSAYVPCDTQ NRDAVKRTLE QIDVIQRMCQ AYPETFACVT 

       130        140        150        160        170        180 
SSTGIRQAFR EGKVASLVGV EGGHSIDSSL GVLRALYHLG MRYMTLTHSC NTPWADNWLV 

       190        200        210        220        230        240 
DTGDDKAQSQ GLSHFGQSVV KEMNRLGVMI DLAHVSVATM RAALKLSQAP VIFSHSSAYS 

       250        260        270        280        290        300 
LCPHRRNVPD DVLQLVKETG SLVMVNFYND YVSCSAKANL SQVADHLDHI KKVAGAAAVG 

       310        320        330        340        350        360 
FGGDYDGVSR VPSGLEDVSK YPDLVAELLR RQWTEAEVRG ALADNLLRVF EAVEQASNHA 

       370        380        390        400 
QVPGEEPIPL GQLEASCRTN YGYSAAPSLH LPPGSLLASL VPLLLLSLP 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53730 mRNA. Translation: CAA37762.1.
D13142 mRNA. Translation: BAA02433.1.
PIRJS0759.
RefSeqNP_999273.1. NM_214108.1.
UniGeneSsc.315.

3D structure databases

ProteinModelPortalP22412.
SMRP22412. Positions 17-385.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP22412.
ChEMBLCHEMBL2626.

Protein family/group databases

MEROPSM19.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397196.
KEGGssc:397196.

Organism-specific databases

CTD1800.

Phylogenomic databases

HOVERGENHBG002339.
KOK01273.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-9981.

Family and domain databases

InterProIPR028536. Dpep1.
IPR000180. Renal_dipep_AS.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF17. PTHR10443:SF17. 1 hit.
PfamPF01244. Peptidase_M19. 1 hit.
[Graphical view]
PROSITEPS00869. RENAL_DIPEPTIDASE_1. 1 hit.
PS51365. RENAL_DIPEPTIDASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPEP1_PIG
AccessionPrimary (citable) accession number: P22412
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 11, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries