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P22412

- DPEP1_PIG

UniProt

P22412 - DPEP1_PIG

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Protein
Dipeptidase 1
Gene
DPEP1, RDP
Organism
Sus scrofa (Pig)
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.

Enzyme regulationi

Inhibited by L-penicillamine By similarity.

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. GPI anchor release Source: UniProtKB
  2. antibiotic metabolic process Source: UniProtKB
  3. cellular response to calcium ion Source: UniProtKB
  4. cellular response to drug Source: UniProtKB
  5. cellular response to insulin stimulus Source: UniProtKB
  6. cellular response to nitric oxide Source: UniProtKB
  7. homocysteine metabolic process Source: UniProtKB
  8. negative regulation of apoptotic process Source: UniProtKB
  9. negative regulation of cell migration Source: UniProtKB
  10. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
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: Unplaced

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. endoplasmic reticulum membrane Source: UniProtKB
  5. extracellular space Source: UniProtKB
  6. microvillus membrane Source: UniProtKB-SubCell
  7. 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 Publication
Add
BLAST
Chaini17 – 384368Dipeptidase 1
PRO_0000018656Add
BLAST
Propeptidei385 – 40925Removed in mature form By similarity
PRO_0000018657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)1 Publication
Disulfide bondi87 ↔ 170 By similarity
Disulfide bondi242 ↔ 274 By similarity
Glycosylationi279 – 2791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi377 – 377Interchain1 Publication
Lipidationi384 – 3841GPI-anchor amidated serine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP22412.
SMRiP22412. Positions 17-385.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M19 family.

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG002339.
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

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MWTSWWLWPL VAVCAADQFR DLAVRIMQDT PVIDGHNDLP WQLLNLFNNQ    50
LQDPGANLSS LAHTHTNIPK LKAGFVGGQF WSAYVPCDTQ NRDAVKRTLE 100
QIDVIQRMCQ AYPETFACVT SSTGIRQAFR EGKVASLVGV EGGHSIDSSL 150
GVLRALYHLG MRYMTLTHSC NTPWADNWLV DTGDDKAQSQ GLSHFGQSVV 200
KEMNRLGVMI DLAHVSVATM RAALKLSQAP VIFSHSSAYS LCPHRRNVPD 250
DVLQLVKETG SLVMVNFYND YVSCSAKANL SQVADHLDHI KKVAGAAAVG 300
FGGDYDGVSR VPSGLEDVSK YPDLVAELLR RQWTEAEVRG ALADNLLRVF 350
EAVEQASNHA QVPGEEPIPL GQLEASCRTN YGYSAAPSLH LPPGSLLASL 400
VPLLLLSLP 409
Length:409
Mass (Da):44,700
Last modified:August 1, 1991 - v1
Checksum:i926B7F0044FA055F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X53730 mRNA. Translation: CAA37762.1 .
D13142 mRNA. Translation: BAA02433.1 .
PIRi JS0759.
RefSeqi NP_999273.1. NM_214108.1.
UniGenei Ssc.315.

3D structure databases

ProteinModelPortali P22412.
SMRi P22412. Positions 17-385.
ModBasei Search...

Chemistry

BindingDBi P22412.
ChEMBLi CHEMBL2626.

Protein family/group databases

MEROPSi M19.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 397196.
KEGGi ssc:397196.

Organism-specific databases

CTDi 1800.

Phylogenomic databases

HOVERGENi HBG002339.
KOi K01273.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-9981.

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

  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: September 3, 2014
This is version 112 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

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