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P31430 (DPEP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

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
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

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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

dipeptidase activity

Traceable author statement Ref.1. Source: RGD

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
Chain17 – 384368Dipeptidase 1
PRO_0000018660
Propeptide385 – 41026Removed in mature form By similarity
PRO_0000018661

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
Glycosylation571N-linked (GlcNAc...) By similarity
Glycosylation1211N-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 conflict4091L → P in AAA41093. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P31430 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 6DD618B44523862C

FASTA41045,522
        10         20         30         40         50         60 
MLIIWWFWSL LAICASDSFR NQAENIMRTT PVIDGHNDLP WQMLTLFNNQ LRKSEANLSA 

        70         80         90        100        110        120 
LAETHTNIPK LRAGFVGGQF WSAYMPCDTQ NKDAVKRILE QIDVIHRMCQ LYPETFECVT 

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

       190        200        210        220        230        240 
DKGDDEAESQ GLSPFGKLVL NEMNRLGVMI DLSHVSVATM KDALQLSKAP VIFSHSSAYS 

       250        260        270        280        290        300 
VCPHRRNVPD DVLQLVKSTN SLVMVNFYNQ FVSCSDSATL SQVADHLDHI KKVAGAGAVG 

       310        320        330        340        350        360 
LGGDYDGVTN LPVGLEDVSK YPDLIAELLR RNWTETEVRG LLAENLLRVF SAVELVSNIM 

       370        380        390        400        410 
QVPEEETIPV EKLDGSCRTF YGHSRAPSIH LQIGALLASL ASLVFSLHLL 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of rat renal dipeptidase and expression of its mRNA in rat tissues and COS-1 cells."
Adachi H., Ishida N., Tsujimoto M.
Biochim. Biophys. Acta 1132:311-314(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Kidney.
[2]"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: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M94056 mRNA. Translation: AAA41093.1.
L07315 mRNA. Translation: AAA41094.1.
L07316 mRNA. Translation: AAA41095.1.
BC072476 mRNA. Translation: AAH72476.1.
PIRS27204.
RefSeqNP_446043.1. NM_053591.2.
XP_006255845.1. XM_006255783.1.
XP_006255846.1. XM_006255784.1.
UniGeneRn.6051.

3D structure databases

ProteinModelPortalP31430.
SMRP31430. Positions 17-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021397.

Protein family/group databases

MEROPSM19.001.

PTM databases

PhosphoSiteP31430.

Proteomic databases

PaxDbP31430.
PRIDEP31430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021397; ENSRNOP00000021397; ENSRNOG00000015880.
GeneID94199.
KEGGrno:94199.
UCSCRGD:620324. rat.

Organism-specific databases

CTD1800.
RGD620324. Dpep1.

Phylogenomic databases

eggNOGCOG2355.
GeneTreeENSGT00390000017920.
HOGENOMHOG000072016.
HOVERGENHBG002339.
InParanoidP31430.
KOK01273.
OMAHIMHIAN.
OrthoDBEOG7SJD4N.
PhylomeDBP31430.
TreeFamTF324523.

Enzyme and pathway databases

SABIO-RKP31430.

Gene expression databases

GenevestigatorP31430.

Family and domain databases

InterProIPR028536. Dpep1-like.
IPR000180. Renal_dipep_AS.
IPR008257. Renal_dipep_fam.
[Graphical view]
PANTHERPTHR10443. PTHR10443. 1 hit.
PTHR10443:SF12. PTHR10443:SF12. 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

NextBio617866.
PROP31430.

Entry information

Entry nameDPEP1_RAT
AccessionPrimary (citable) accession number: P31430
Secondary accession number(s): Q6IN35
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 122 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