Q6DJK5 · Q6DJK5_XENLA

Function

function

Catalyzes the peptide bond hydrolysis in dipeptides, displaying a non-redundant activity toward threonyl dipeptides. Mediates threonyl dipeptide catabolism in a tissue-specific way. Has high dipeptidase activity toward cysteinylglycine, an intermediate metabolite in glutathione metabolism. Metabolizes N-lactoyl-amino acids, both through hydrolysis to form lactic acid and amino acids, as well as through their formation by reverse proteolysis. Plays a role in the regulation of cell cycle arrest and apoptosis.

Catalytic activity

  • (S)-lactate + L-phenylalanine = N-[(S)-lactoyl]-L-phenylalanine + H2O
    This reaction proceeds in the forward
    and the backward
    directions.
  • L-cysteinylglycine + H2O = L-cysteine + glycine
    This reaction proceeds in the forward direction.
  • L-seryl-L-threonine + H2O = L-threonine + L-serine
    This reaction proceeds in the forward direction.
  • L-threonyl-L-serine + H2O = L-threonine + L-serine
    This reaction proceeds in the forward direction.
  • L-threonyl-L-threonine + H2O = 2 L-threonine
    This reaction proceeds in the forward direction.
  • Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.
    EC:3.4.13.18 (UniProtKB | ENZYME | Rhea)

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 manganese ions per subunit.

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site99Mn2+ 2 (UniProtKB | ChEBI)
Active site101
Binding site132Mn2+ 2 (UniProtKB | ChEBI)
Binding site132Mn2+ 1 (UniProtKB | ChEBI)
Active site166Proton acceptor
Binding site167Mn2+ 1 (UniProtKB | ChEBI)
Binding site195Mn2+ 2 (UniProtKB | ChEBI)
Binding site195substrate; ligand shared between homodimeric partners; in other chain
Binding site228substrate; ligand shared between homodimeric partners
Site228Important for catalytic activity
Binding site330substrate; ligand shared between homodimeric partners
Binding site343substrate; ligand shared between homodimeric partners; in other chain
Binding site417substrate; ligand shared between homodimeric partners; in other chain
Binding site445Mn2+ 1 (UniProtKB | ChEBI)
Binding site445substrate; ligand shared between homodimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioncarboxypeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetallodipeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytosolic non-specific dipeptidase
  • EC number
  • Alternative names
    • CNDP dipeptidase 2
    • Threonyl dipeptidase

Gene names

    • Name
      cndp2.L
    • Synonyms
      cn2
      , cndp2
      , cndp2-prov
      , cndp2a
      , cpgl
      , darmin-r

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    Q6DJK5

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Keywords

Expression

Gene expression databases

    • 446978Expressed in intestine and 19 other cell types or tissues

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain208-367Peptidase M20 dimerisation

Sequence similarities

Belongs to the peptidase M20A family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    474
  • Mass (Da)
    52,841
  • Last updated
    2004-08-16 v1
  • Checksum
    F97784E8FB36CB78
MSVLPVLFEHIDKNQDLYVKRLAEWVAIQSVSAWPEKRGEIKRMMQVAAKEIERLGGTTELVDIGKQKLPDGTEIPLPPVILGKLGSDPGKKTVCIYGHLDVQPAALEDGWDSEPFVLQERDGKLYGRGSTDDKGPVLAWLNCIEAYQQTKQELPVNLKFCFEGMEESGSEGLDDLIFARKDSFFKGVDYVCISDNYWLGKNKPCITYGLRGICYFFIEVECSCKDLHSGVYGGSVHEAMTDLIALMGSLVDKRGKILIPGINEAVAPVLKEEKDIYDAIEFDLEDFACDIGADRLLHESKEKILMHRWRFPSLSLHGIEGAFSAAGAKTVIPRKVIGKFSIRLVPDMNPEDVKKQVEEYLTKKFKELGSPNKFQVTMGHGGKPWVSDVHHPHYIAGRKAMKTVFNVEPDLTREGGSIPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRFNYIQGVKLLGAYLYEVSNLE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC075171
EMBL· GenBank· DDBJ
AAH75171.1
EMBL· GenBank· DDBJ
mRNA
BC157410
EMBL· GenBank· DDBJ
AAI57411.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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