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P31428 (DPEP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Membrane-bound dipeptidase 1
Short name=MBD-1
Microsomal dipeptidase
Renal dipeptidase
Gene names
Name:Dpep1
Synonyms:Mbd1, Rdp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length410 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. Ref.4

Subunit structure

Homodimer; disulfide-linked.

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.

Biophysicochemical properties

Kinetic parameters:

KM=10 µM for leukotriene D4 Ref.4

KM=0.45 mM for cystinyl-bis-glycine

KM=111 µM for beta-lactam

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
Reference proteome
Gene Ontology (GO)
   Biological_processantibiotic metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to nitric oxide

Inferred from sequence or structural similarity. 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

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

microvillus membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGPI anchor binding

Inferred from sequence or structural similarity. 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 By similarity
Chain17 – 384368Dipeptidase 1
PRO_0000018654
Propeptide385 – 41026Removed in mature form By similarity
PRO_0000018655

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 By similarity
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) By similarity
Disulfide bond87 ↔ 170 By similarity
Disulfide bond242 ↔ 274 By similarity
Disulfide bond377Interchain By similarity

Experimental info

Sequence conflict2041N → T in BAA02432. Ref.1
Sequence conflict3581N → S in BAA02432. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P31428 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 46A454B51CA57BB5

FASTA41045,722
        10         20         30         40         50         60 
MVIIWWFWSL LAICASDSFR DQAVAIMRTT PVIDGHNDLP WQLLNLFNNQ LLRPDADLNK 

        70         80         90        100        110        120 
LAQTHTNIPK LKAGFVGGQF WSAYMPCDTQ NKDAVKRILE QMDVIHRMCQ LYPETFMCVT 

       130        140        150        160        170        180 
NSSDILQAFR RGKVASLIGV EGGHLIDSSL GVLRTLYHLG MRYLTLTHNC NTPWADNWLV 

       190        200        210        220        230        240 
DRGDDEAESH GLSPFGKRLL NEMNRLGVMI DLSHVSVATM KDALQISRAP VIFSHSSAYS 

       250        260        270        280        290        300 
LCPHRRNVPD DVLQLVKNTS SLVMVNFFSN FVSCSDSATL PQVADHLDHI KKVAGAGAVG 

       310        320        330        340        350        360 
LGGDYDGVTM LPVGLEDVSK YPDLIAELLR RNWTETEVRG LLADNLIRVF SEVELVSNNM 

       370        380        390        400        410 
QSPEEVPITL KELDGSCRTY YGYSQAHSIH LQTGALVASL ASLLFRLHLL 

« Hide

References

« Hide 'large scale' references
[1]"Purification and molecular cloning of mouse renal dipeptidase."
Satoh S., Keida Y., Konta Y., Maeda M., Matsumoto Y., Niwa M., Kohsaka M.
Biochim. Biophys. Acta 1163:234-242(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Identification of two additional members of the membrane-bound dipeptidase family."
Habib G.M., Shi Z.-Z., Cuevas A.A., Lieberman M.W.
FASEB J. 17:1313-1315(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13139 mRNA. Translation: BAA02432.1.
AC163617 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11712.1.
CCDSCCDS22750.1.
PIRS33757.
RefSeqNP_031902.2. NM_007876.2.
UniGeneMm.20388.

3D structure databases

ProteinModelPortalP31428.
SMRP31428. Positions 17-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP31428. 3 interactions.
MINTMINT-4101665.
STRING10090.ENSMUSP00000019422.

Protein family/group databases

MEROPSM19.001.

PTM databases

PhosphoSiteP31428.

Proteomic databases

PaxDbP31428.
PRIDEP31428.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019422; ENSMUSP00000019422; ENSMUSG00000019278.
GeneID13479.
KEGGmmu:13479.
UCSCuc009nui.2. mouse.

Organism-specific databases

CTD1800.
MGIMGI:94917. Dpep1.

Phylogenomic databases

eggNOGCOG2355.
GeneTreeENSGT00390000017920.
HOGENOMHOG000072016.
HOVERGENHBG002339.
InParanoidP31428.
KOK01273.
OMAGMRYMTL.
OrthoDBEOG7SJD4N.
TreeFamTF324523.

Gene expression databases

CleanExMM_DPEP1.
MM_MBD1.
GenevestigatorP31428.

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...

Other

NextBio283967.
PROP31428.
SOURCESearch...

Entry information

Entry nameDPEP1_MOUSE
AccessionPrimary (citable) accession number: P31428
Secondary accession number(s): G5E824
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 123 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot