P80209 · CATD_BOVIN

  • Protein
    Cathepsin D
  • Gene
    CTSD
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation.

Catalytic activity

  • Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.
    EC:3.4.23.5 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

139050100150200250300350
TypeIDPosition(s)Description
Active site77
Active site273

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 region
Cellular Componentlysosome
Cellular Componentmelanosome
Molecular Functionaspartic-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      CTSD

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P80209
  • Secondary accessions
    • Q9TS27

Proteomes

Subcellular Location

Phenotypes & Variants

PTM/Processing

Features

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

TypeIDPosition(s)Description
PropeptidePRO_00000259471-44Activation peptide
ChainPRO_000002594845-390Cathepsin D
Disulfide bond71↔140
Disulfide bond90↔97
Glycosylation114N-linked (GlcNAc...) asparagine
Glycosylation241N-linked (GlcNAc...) asparagine
Disulfide bond264↔268
Disulfide bond307↔344

Post-translational modification

N- and O-glycosylated.
Undergoes proteolytic cleavage and activation by ADAM30.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Consists of a light chain and a heavy chain. Interacts with ADAM30; this leads to activation of CTSD. Interacts with GRN; stabilizes CTSD; increases its proteolytic activity (By similarity).

Protein-protein interaction databases

Chemistry

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain59-385Peptidase A1

Sequence similarities

Belongs to the peptidase A1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    390
  • Mass (Da)
    42,491
  • Last updated
    2001-04-27 v2
  • Checksum
    5B38AA1C33C48D35
VIRIPLHKFTSIRRTMSEAAGXVXXLIAKGPISKYATGEPAVRQGPIPELLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSANLWVPSIHCKLLDIACWTHRKYNSDKSSTYVKNGTTFDIHYGSGSLSGYLSQDTVSVPCNPSSSSPGGVTVQRQTFGEAIKQPGVVFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDKNVFSFFLNRDPKAQPGGELMLGGTDSKYYRGSLMFHNVTRQAYWQIHMDQLDVGSSLTVCKGGCEAIVDTGTSLIVGPVEEVRELQKAIGAVPLIQGEYMIPCEKVSSLPEVTVKLGGKDYALSPEDYALKVSQAETTVCLSGFMGMDIPPPGGPLWILGDVFIGRYYTVFDRDQNRVGLAEAARL

Keywords

Sequence databases

Similar Proteins

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