O93428 · CATD_CHIHA
- ProteinCathepsin D
- Genectsd
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids396 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Acid protease active in intracellular protein breakdown.
Catalytic activity
Activity regulation
Inhibited by pepstatin.
pH Dependence
Optimum pH is 3.0.
Temperature Dependence
Highly thermostable. Enzyme activity is maintained up to 45 degrees Celsius. Active at 50 degrees Celsius but with reduced catalytic activity.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 94 | |||||
Sequence: D | ||||||
Active site | 281 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | lysosome | |
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Notothenioidei > Channichthyidae > Chionodraco
Accessions
- Primary accessionO93428
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MKMLLLCVFSALALTNDA | ||||||
Propeptide | PRO_0000285984 | 19-61 | Activation peptide | |||
Sequence: LVRIPLKKFRSIRRQLTDSGKRAEELLADHHSLKYNLSFPASN | ||||||
Chain | PRO_5000064481 | 62-396 | Cathepsin D | |||
Sequence: APTPETLKNYLDAQYYGEIGLGTPPQPFTVVFDTGSSNLWVPSIHCSLLDIACLLHHKYNSGKSSTYVKNGTAFAIQYGSGSLSGYLSQDTCTIGDLAIDSQLFGEAIKQPGVAFIAAKFDGILGMAYPRISVDGVAPVFDNIMSQKKVEQNVFSFYLNRNPDTEPGGELLLGGTDPKYYTGDFNYVNVTRQAYWQIRVDSMAVGDQLSLCTGGCEAIVDSGTSLITGPSVEVKALQKAIGAFPLIQGEYMVNCDTVPSLPVISFTVGGQVYTLTGEQYILKVTQAGKTMCLSGFMGLDIPAPAGPLWILGDVFMGQYYTVFDRDANRVGFAKAK | ||||||
Disulfide bond | 107↔114 | |||||
Sequence: CSLLDIAC | ||||||
Glycosylation | 131 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 249 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 272↔276 | |||||
Sequence: CTGGC | ||||||
Disulfide bond | 315↔352 | |||||
Sequence: CDTVPSLPVISFTVGGQVYTLTGEQYILKVTQAGKTMC |
Keywords
- PTM
PTM databases
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 76-393 | Peptidase A1 | ||||
Sequence: YYGEIGLGTPPQPFTVVFDTGSSNLWVPSIHCSLLDIACLLHHKYNSGKSSTYVKNGTAFAIQYGSGSLSGYLSQDTCTIGDLAIDSQLFGEAIKQPGVAFIAAKFDGILGMAYPRISVDGVAPVFDNIMSQKKVEQNVFSFYLNRNPDTEPGGELLLGGTDPKYYTGDFNYVNVTRQAYWQIRVDSMAVGDQLSLCTGGCEAIVDSGTSLITGPSVEVKALQKAIGAFPLIQGEYMVNCDTVPSLPVISFTVGGQVYTLTGEQYILKVTQAGKTMCLSGFMGLDIPAPAGPLWILGDVFMGQYYTVFDRDANRVGFA |
Sequence similarities
Belongs to the peptidase A1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length396
- Mass (Da)42,958
- Last updated2007-05-01 v2
- ChecksumB660E5E7FBD023FF
Sequence caution
Keywords
- Technical term