A6RBI0 · DAPB_AJECN

Function

function

Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.

Catalytic activity

  • Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
    EC:3.4.14.5 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

1922100200300400500600700800900
TypeIDPosition(s)Description
Active site756Charge relay system
Active site833Charge relay system
Active site866Charge relay system

GO annotations

AspectTerm
Cellular Componentplasma membrane
Cellular Componentvacuolar membrane
Molecular Functionaminopeptidase activity
Molecular Functiondipeptidyl-peptidase activity
Molecular Functionserine-type peptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable dipeptidyl-aminopeptidase B
  • EC number
  • Short names
    DPAP B

Gene names

    • Name
      DAPB
    • ORF names
      HCAG_06318

Organism names

Accessions

  • Primary accession
    A6RBI0

Proteomes

Organism-specific databases

Subcellular Location

Vacuole membrane
; Single-pass type II membrane protein
Note: Lysosome-like vacuoles.

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain1-99Cytoplasmic
Transmembrane100-120Helical; Signal-anchor for type II membrane protein
Topological domain121-922Vacuolar

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

Type
IDPosition(s)Description
ChainPRO_00004121261-922Probable dipeptidyl-aminopeptidase B
Glycosylation135N-linked (GlcNAc...) asparagine
Glycosylation200N-linked (GlcNAc...) asparagine
Glycosylation351N-linked (GlcNAc...) asparagine
Glycosylation574N-linked (GlcNAc...) asparagine
Glycosylation815N-linked (GlcNAc...) asparagine
Glycosylation902N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias1-19Basic and acidic residues
Region1-21Disordered

Sequence similarities

Belongs to the peptidase S9B family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    922
  • Mass (Da)
    104,147
  • Last updated
    2007-08-21 v1
  • Checksum
    34932E3C1D124CDE
MATEKGHSRDDEERVPLTRGSTEFRNSIDSFDYSSSTASLSLAVIDRINNSTQDAGLSEKGPRDDDDDRYWDDDVEYDVEDADYIPSGGKPMHKSVKIALWSLLFLSLGGWSLAFVLFIFRSHDTYQTPILSEDNISSGGLRGDRITLDDVLGEEWMPRHHFISWFPGPNGEDGLLLEKDGPGSTGYLRVEDIVSRKDTNSSKGSIVLMQKNTFTVGGETVICSQVWPSPDLKTVLVLSEKKQNWRHSFTGKYWLFDVDTQTGQPLDPAAQDQRIQLASWSHKSDAVVFTRDNNMFLRKLSSKEVITITSDGGVDLLYGVPDWVYEEEVFSGNSATWWAHDGNYIAFLRTNESAVPEYPIQYFVSRPSGEDPNLGEENYPEVREIKYPKAGAPNPIVDLQFYDIRKGEIFSVDVADRFPDDNRLIIEVLWASNGKVLVRETNRESDILIIAAIDVLSRTGKIVRKEDINALDGGWVEPTQSTRFIPADPSNDRPEDGYIDTVIHEGRDQLAYFTPLDNPKPLILTKGHSEVVNSPSGVDLKRGLVYFVVAGNEPWERHVYSVKFDGTALQPVTNVSESSYYDVSFSDGAGYALLNFRGPKVPWQKVISTPANENPFEEIIEQNNHLSRKLRLFSLESKVFQYINIDGFSLPVLERRPPNFDPTKKYPVLFYLYGGPGSQTVDKKFGVDFQSYVASTLGYIVVTVDGRGTGYIGRKSLSLVRGKLGHYEARDQIEVAKKWAAKPYVDESRMAIWGWSYGGFMTLKTIEEDGGRTFQYGMAVAPVTDWRYYDSIYAERYMHTPQHNPQGYDSSAISNTTALANSVRFLVMHGTADDNVHIQNTLTLLDKLDLANVDNYDVHVFPDSNHNINYHNAHKMVYTRLADWLVNAFNGQWLKTNNPTPNDSLFRRVATWAGLYKFKHLC

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-19Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH476661
EMBL· GenBank· DDBJ
EDN10515.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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