Q6P2V1 · Q6P2V1_DANRE

Function

function

Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B.

Catalytic activity

  • Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.
    EC:3.4.14.1 (UniProtKB | ENZYME | Rhea)

Cofactor

chloride (UniProtKB | Rhea| CHEBI:17996 )

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Molecular Functioncysteine-type endopeptidase activity
Molecular Functiondipeptidyl-peptidase activity
Biological Processproteolysis involved in protein catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Dipeptidyl peptidase 1
  • EC number
  • Alternative names
    • Cathepsin C
    • Cathepsin J
    • Dipeptidyl peptidase I
    • Dipeptidyl transferase

Gene names

    • Name
      ctsc
    • Synonyms
      cb912
      , ik:tdsubc_1h2
      , sb:cb146
      , wu:fb34g12
      , wu:fj58d01

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    Q6P2V1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_503503594719-455Dipeptidyl peptidase 1

Keywords

Interaction

Subunit

Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain224-450Peptidase C1A papain C-terminal

Sequence similarities

Belongs to the peptidase C1 family.

Keywords

  • Domain
    • #Signal

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    455
  • Mass (Da)
    50,614
  • Last updated
    2004-07-05 v1
  • Checksum
    7808E1F80F48CBE8
MRALSVIVLVAFIAGAAADTPANCTYEDLLGTWIFSVSNVGQDKTINCSSTGQAVSTVTVDLQKLSVAVDDLGHTGFFTLIYNQGFEVVINDYKWFGFFKYTQQGSEVVSYCDQTLPGWVHDVLGNNWACFTGKKVQPIPPRVDRRHMLGFEHRLLMKLPYTNNMMFVDEINSVQKSWTATAYSFHETLSIHEMLRRSGGPASRIPRRVRPVTVAADSKAASGLPQHWDWRNVNGVNFVSPVRNQAQCGSCYSFATMGMLEARVRIQTNNTQQPVFSPQQVVSCSQYSQGCDGGFPYLIGKYIQDFGIVEEDCFPYTGSDSPCNLPAKCTKYYASDYHYVGGFYGGCSESAMMLELVKNGPMGVALEVYPDFMNYKEGIYHHTGLRDANNPFELTNHAVLLVGYGQCHKTGEKYWIVKNSWGSGWGENGFFRIRRGTDECAIESIAVAATPIPKL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC064286
EMBL· GenBank· DDBJ
AAH64286.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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