Q9MZS8 · CATD_SHEEP
- ProteinCathepsin D
- GeneCTSD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids365 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 72 | |||||
Sequence: D | ||||||
Active site | 268 | |||||
Sequence: D |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | lysosome | |
Cellular Component | melanosome | |
Molecular Function | aspartic-type endopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCathepsin D
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Caprinae > Ovis
Accessions
- Primary accessionQ9MZS8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 268 | in CONCL; inactive | ||||
Sequence: D → N |
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.
Keywords
- Disease
PTM/Processing
Features
Showing features for propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000025964 | 1-39 | Activation peptide | |||
Sequence: LHKFTSNRRTMSEAMGPVEHLIAKGPISKYATREPAVRQ | ||||||
Chain | PRO_0000025965 | 40-365 | Cathepsin D | |||
Sequence: GPIPELLTNYMDAQYYGEIGIGTPPQCFTVVFDTGSANLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTTFDIHYGSGSLSGYLSQDTVSVPCNPSSSSPGGVTVQRQTFGEAIKQPGVVFIAAKFDGILGMAYPRISVNNVLPVFDNLMRQKLVDKNVFSFFLNRDPKAQPGEELMLGGTDSKYYRGSLTYHNVTRQAYWQIHMDQLDVGSSLTVCKGGCEAIVDTGTSLMVGPVDEVRELHKAIGAVPLIQGEYMIPCEKVSSLPQVTLKLGGKDYTLSPEDYTLKVSQAGTTVCLSGFMGMDIPPPGGPLWILGDVFIGR | ||||||
Disulfide bond | 66↔135 | |||||
Sequence: CFTVVFDTGSANLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTTFDIHYGSGSLSGYLSQDTVSVPC | ||||||
Disulfide bond | 85↔92 | |||||
Sequence: CKLLDIAC | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 236 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 259↔263 | |||||
Sequence: CKGGC | ||||||
Disulfide bond | 302↔339 | |||||
Sequence: CEKVSSLPQVTLKLGGKDYTLSPEDYTLKVSQAGTTVC |
Post-translational modification
N- and O-glycosylated.
Undergoes proteolytic cleavage and activation by ADAM30.
Keywords
- PTM
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).
Interacts with GRN; stabilizes CTSD; increases its proteolytic activity (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 54-365 | Peptidase A1 | ||||
Sequence: YYGEIGIGTPPQCFTVVFDTGSANLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTTFDIHYGSGSLSGYLSQDTVSVPCNPSSSSPGGVTVQRQTFGEAIKQPGVVFIAAKFDGILGMAYPRISVNNVLPVFDNLMRQKLVDKNVFSFFLNRDPKAQPGEELMLGGTDSKYYRGSLTYHNVTRQAYWQIHMDQLDVGSSLTVCKGGCEAIVDTGTSLMVGPVDEVRELHKAIGAVPLIQGEYMIPCEKVSSLPQVTLKLGGKDYTLSPEDYTLKVSQAGTTVCLSGFMGMDIPPPGGPLWILGDVFIGR |
Sequence similarities
Belongs to the peptidase A1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length365
- Mass (Da)39,815
- Last updated2000-10-01 v1
- Checksum76A7BFE5BC45E9CB
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: L | ||||||
Non-terminal residue | 365 | |||||
Sequence: R |
Keywords
- Technical term