P31429 · DPEP1_RABIT

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

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Activity regulation

Inhibited by L-penicillamine. Beta-lactamase activity is inhibited by cilastatin.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site36Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site38Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site141Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site141Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site168substrate
Binding site214Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site235Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site246substrate
Binding site304substrate

GO annotations

AspectTerm
Cellular Componentapical part of cell
Cellular Componentapical plasma membrane
Cellular Componentextracellular space
Cellular Componentmicrovillus membrane
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular Functionbeta-lactamase activity
Molecular Functioncysteine-type endopeptidase inhibitor activity involved in apoptotic process
Molecular Functiondipeptidase activity
Molecular FunctionGPI anchor binding
Molecular Functionmetallodipeptidase activity
Molecular Functionmodified amino acid binding
Molecular Functionzinc ion binding
Biological Processantibiotic metabolic process
Biological Processcellular response to calcium ion
Biological Processcellular response to nitric oxide
Biological Processcellular response to xenobiotic stimulus
Biological Processglutathione catabolic process
Biological Processhomocysteine metabolic process
Biological Processinflammatory response
Biological Processleukotriene D4 catabolic process
Biological Processleukotriene metabolic process
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of cell migration
Biological Processnegative regulation of cysteine-type endopeptidase activity involved in apoptotic process
Biological Processneutrophil chemotaxis
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Dipeptidase 1
  • EC number
  • Alternative names
    • 43 kDa renal band 3-related protein
    • Beta-lactamase
      (EC:3.5.2.6
      ) . EC:3.5.2.6 (UniProtKB | ENZYME | Rhea)
    • Microsomal dipeptidase

Gene names

    • Name
      DPEP1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    P31429

Proteomes

Subcellular Location

Apical cell membrane
; Lipid-anchor, GPI-anchor
Cell projection, microvillus membrane
; Lipid-anchor, GPI-anchor
Note: Brush border membrane.

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, lipidation, propeptide.

Type
IDPosition(s)Description
Signal1-16
ChainPRO_000001865817-384Dipeptidase 1
Glycosylation57N-linked (GlcNAc...) asparagine
Disulfide bond87↔170
Disulfide bond242↔274
Disulfide bond377Interchain
Lipidation384GPI-anchor amidated serine
PropeptidePRO_0000018659385-410Removed in mature form

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer; disulfide-linked.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    410
  • Mass (Da)
    45,305
  • Last updated
    1993-07-01 v1
  • Checksum
    2033F7BFBBF2CC72
MWTSWWLWPLVAVCTADSFLDQAVQILRVTPVIDGHNDLPWQLLNKFNNRLQDSRANLTVLADTHTNIPKLRAGFVGGQFWSAYTPCDTQNKDTVRRTLEQMDVVHRMCQLYPETFLCVTDSAGIQQAFREGKVASLIGVEGGHSIDSSLGVLRALYRLGMRYLTLTHNCNTPWADNWLVDRGDDEAQSGGLSVFGQRVVREMNRLGVMIDLAHVSVATMKAALQLSTAPVIFSHSSAFTVCAHKRNVPDDVLQLVKETGSLVMVNFYNDYVSCASEATLSQVADHLDYIKNVAGAAAVRFGGDFDGVTRLPVGLEDVSKYPDLVAELLRRGWTEAEVRGALAENLLRVFREVEQVSNQAQVPEEEPISLEQLGGSCRTQYGYSEAPSLHRRPGALLASLSLLLLSLGLL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X61503
EMBL· GenBank· DDBJ
CAA43720.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help