P31429 · DPEP1_RABIT
- ProteinDipeptidase 1
- GeneDPEP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids410 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Hydrolyzes a wide range of dipeptides including the conversion of leukotriene D4 to leukotriene E4. Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation. Possesses also beta lactamase activity and hydrolytically inactivates beta-lactam antibiotics.
Independently of its dipeptidase activity, acts as an adhesion receptor for neutrophil recruitment from bloodstream into inflamed lungs and liver.
Catalytic activity
- an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
- leukotriene D4 + H2O = leukotriene E4 + glycine
- L-cystine-bis-glycine + 2 H2O = L-cystine + 2 glycine
- glycyldehydrophenylalanine + H2O = 2,3-didehydrophenylalanine + glycine
Cofactor
Activity regulation
Inhibited by L-penicillamine. Beta-lactamase activity is inhibited by cilastatin.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 36 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 38 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 141 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 141 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 168 | substrate | |||
Binding site | 214 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 235 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 246 | substrate | |||
Binding site | 304 | substrate | |||
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDipeptidase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionP31429
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Apical cell membrane ; Lipid-anchor, GPI-anchor
Cell projection, microvillus membrane ; Lipid-anchor, GPI-anchor
Note: Brush border membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-16 | ||||
Chain | PRO_0000018658 | 17-384 | Dipeptidase 1 | ||
Glycosylation | 57 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 87↔170 | ||||
Disulfide bond | 242↔274 | ||||
Disulfide bond | 377 | Interchain | |||
Lipidation | 384 | GPI-anchor amidated serine | |||
Propeptide | PRO_0000018659 | 385-410 | Removed in mature form | ||
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Structure
Family & Domains
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length410
- Mass (Da)45,305
- Last updated1993-07-01 v1
- Checksum2033F7BFBBF2CC72
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X61503 EMBL· GenBank· DDBJ | CAA43720.1 EMBL· GenBank· DDBJ | mRNA |