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P31429 (DPEP1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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):
43 kDa renal band 3-related protein
Microsomal dipeptidase
Gene names
Name:DPEP1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

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 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
Direct protein sequencing
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

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 Ref.1
Chain17 – 384368Dipeptidase 1
PRO_0000018658
Propeptide385 – 41026Removed in mature form By similarity
PRO_0000018659

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
Disulfide bond87 ↔ 170 By similarity
Disulfide bond242 ↔ 274 By similarity
Disulfide bond377Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
P31429 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 2033F7BFBBF2CC72

FASTA41045,305
        10         20         30         40         50         60 
MWTSWWLWPL VAVCTADSFL DQAVQILRVT PVIDGHNDLP WQLLNKFNNR LQDSRANLTV 

        70         80         90        100        110        120 
LADTHTNIPK LRAGFVGGQF WSAYTPCDTQ NKDTVRRTLE QMDVVHRMCQ LYPETFLCVT 

       130        140        150        160        170        180 
DSAGIQQAFR EGKVASLIGV EGGHSIDSSL GVLRALYRLG MRYLTLTHNC NTPWADNWLV 

       190        200        210        220        230        240 
DRGDDEAQSG GLSVFGQRVV REMNRLGVMI DLAHVSVATM KAALQLSTAP VIFSHSSAFT 

       250        260        270        280        290        300 
VCAHKRNVPD DVLQLVKETG SLVMVNFYND YVSCASEATL SQVADHLDYI KNVAGAAAVR 

       310        320        330        340        350        360 
FGGDFDGVTR LPVGLEDVSK YPDLVAELLR RGWTEAEVRG ALAENLLRVF REVEQVSNQA 

       370        380        390        400        410 
QVPEEEPISL EQLGGSCRTQ YGYSEAPSLH RRPGALLASL SLLLLSLGLL 

« Hide

References

[1]"Cloning of cDNAs encoding a rabbit renal brush border membrane protein immunologically related to band 3. Sequence similarity with microsomal dipeptidase."
Igarashi P., Karniski L.P.
Biochem. J. 280:71-78(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-40.
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61503 mRNA. Translation: CAA43720.1.
PIRS18442.
RefSeqNP_001095167.1. NM_001101697.1.
UniGeneOcu.3249.

3D structure databases

ProteinModelPortalP31429.
SMRP31429. Positions 17-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000008950.

Protein family/group databases

MEROPSM19.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009273.

Organism-specific databases

CTD1800.

Phylogenomic databases

eggNOGCOG2355.
HOGENOMHOG000072016.
HOVERGENHBG002339.

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

PMAP-CutDBP31429.

Entry information

Entry nameDPEP1_RABIT
AccessionPrimary (citable) accession number: P31429
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 106 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