Q9MZS8 · CATD_SHEEP

  • 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.

136550100150200250300350
TypeIDPosition(s)Description
Active site72
Active site268

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
  • Strain
    • White Swedish Landrace
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Caprinae > Ovis

Accessions

  • Primary accession
    Q9MZS8

Proteomes

Subcellular Location

Phenotypes & Variants

Involvement in disease

  • Defects in CTSD are a cause of congenital ovine neuronal ceroid lipofuscinosis (CONCL). CONCL is an autosomal recessive disorder. Newborn lambs are weak, trembling, and unable to rise and support their bodies. However, they are able to vocalize, support their heads, and to suckle if bottle-fed. At autopsy, the brains of affected lambs are strikingly small. The deep layers of the cerebral cortex show pronounced neuronal loss, reactive astrocytosis, and infiltration of macrophages. There is severe degeneration of hippocampal pyramidal neurons

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant268in CONCL; inactive

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
PropeptidePRO_00000259641-39Activation peptide
ChainPRO_000002596540-365Cathepsin D
Disulfide bond66↔135
Disulfide bond85↔92
Glycosylation109N-linked (GlcNAc...) asparagine
Glycosylation236N-linked (GlcNAc...) asparagine
Disulfide bond259↔263
Disulfide bond302↔339

Post-translational modification

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

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Occurs as a mixture of both a single chain form and two types of two chain (light and heavy) forms. Interacts with ADAM30; this leads to activation of CTSD (By similarity).
Interacts with GRN; stabilizes CTSD; increases its proteolytic activity (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain54-365Peptidase A1

Sequence similarities

Belongs to the peptidase A1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    365
  • Mass (Da)
    39,815
  • Last updated
    2000-10-01 v1
  • Checksum
    76A7BFE5BC45E9CB
LHKFTSNRRTMSEAMGPVEHLIAKGPISKYATREPAVRQGPIPELLTNYMDAQYYGEIGIGTPPQCFTVVFDTGSANLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTTFDIHYGSGSLSGYLSQDTVSVPCNPSSSSPGGVTVQRQTFGEAIKQPGVVFIAAKFDGILGMAYPRISVNNVLPVFDNLMRQKLVDKNVFSFFLNRDPKAQPGEELMLGGTDSKYYRGSLTYHNVTRQAYWQIHMDQLDVGSSLTVCKGGCEAIVDTGTSLMVGPVDEVRELHKAIGAVPLIQGEYMIPCEKVSSLPQVTLKLGGKDYTLSPEDYTLKVSQAGTTVCLSGFMGMDIPPPGGPLWILGDVFIGR

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue365

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF164143
EMBL· GenBank· DDBJ
AAF80494.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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