P24268 · CATD_RAT
- ProteinCathepsin D
- GeneCtsd
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids407 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 | 97 | |||||
Sequence: D | ||||||
Active site | 290 | |||||
Sequence: D |
GO annotations
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCathepsin D
- EC number
- Cleaved into 4 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP24268
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MQTPGVLLLILGLLDASSSA | ||||||
Propeptide | PRO_0000025958 | 21-64 | Activation peptide | |||
Sequence: LIRIPLRKFTSIRRTMTEVGGSVEDLILKGPITKYSMQSSPRTK | ||||||
Chain | PRO_0000025961 | 65-117 | Cathepsin D 9 kDa light chain | |||
Sequence: EPVSELLKNYLDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIAC | ||||||
Chain | PRO_0000025960 | 65-164 | Cathepsin D 12 kDa light chain | |||
Sequence: EPVSELLKNYLDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDL | ||||||
Chain | PRO_0000025959 | 65-407 | Cathepsin D | |||
Sequence: EPVSELLKNYLDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDLGGIKVEKQIFGEATKQPGVVFIAAKFDGILGMGYPFISVNKVLPVFDNLMKQKLVEKNIFSFYLNRDPTGQPGGELMLGGTDSRYYHGELSYLNVTRKAYWQVHMDQLEVGSELTLCKGGCEAIVDTGTSLLVGPVDEVKELQKAIGAVPLIQGEYMIPCEKVSSLPIITFKLGGQNYELHPEKYILKVSQAGKTICLSGFMGMDIPPPSGPLWILGDVFIGCYYTVFDREYNRVGFAKAATL | ||||||
Disulfide bond | 91↔160 | |||||
Sequence: CFTVVFDTGSSNLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPC | ||||||
Disulfide bond | 110↔117 | |||||
Sequence: CKLLDIAC | ||||||
Chain | PRO_0000025962 | 118-407 | Cathepsin D 34 kDa heavy chain | |||
Sequence: WVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDLGGIKVEKQIFGEATKQPGVVFIAAKFDGILGMGYPFISVNKVLPVFDNLMKQKLVEKNIFSFYLNRDPTGQPGGELMLGGTDSRYYHGELSYLNVTRKAYWQVHMDQLEVGSELTLCKGGCEAIVDTGTSLLVGPVDEVKELQKAIGAVPLIQGEYMIPCEKVSSLPIITFKLGGQNYELHPEKYILKVSQAGKTICLSGFMGMDIPPPSGPLWILGDVFIGCYYTVFDREYNRVGFAKAATL | ||||||
Glycosylation | 134 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000025963 | 165-407 | Cathepsin D 30 kDa heavy chain | |||
Sequence: GGIKVEKQIFGEATKQPGVVFIAAKFDGILGMGYPFISVNKVLPVFDNLMKQKLVEKNIFSFYLNRDPTGQPGGELMLGGTDSRYYHGELSYLNVTRKAYWQVHMDQLEVGSELTLCKGGCEAIVDTGTSLLVGPVDEVKELQKAIGAVPLIQGEYMIPCEKVSSLPIITFKLGGQNYELHPEKYILKVSQAGKTICLSGFMGMDIPPPSGPLWILGDVFIGCYYTVFDREYNRVGFAKAATL | ||||||
Glycosylation | 258 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 281↔285 | |||||
Sequence: CKGGC | ||||||
Disulfide bond | 324↔361 | |||||
Sequence: CEKVSSLPIITFKLGGQNYELHPEKYILKVSQAGKTIC |
Post-translational modification
N- and O-glycosylated.
Undergoes proteolytic cleavage and activation by ADAM30.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 79-402 | Peptidase A1 | ||||
Sequence: YYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDLGGIKVEKQIFGEATKQPGVVFIAAKFDGILGMGYPFISVNKVLPVFDNLMKQKLVEKNIFSFYLNRDPTGQPGGELMLGGTDSRYYHGELSYLNVTRKAYWQVHMDQLEVGSELTLCKGGCEAIVDTGTSLLVGPVDEVKELQKAIGAVPLIQGEYMIPCEKVSSLPIITFKLGGQNYELHPEKYILKVSQAGKTICLSGFMGMDIPPPSGPLWILGDVFIGCYYTVFDREYNRVGFA |
Sequence similarities
Belongs to the peptidase A1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length407
- Mass (Da)44,681
- Last updated1992-03-01 v1
- ChecksumC423AD4104D95F84
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AKF2 | A0A8I6AKF2_RAT | Ctsd | 374 | ||
A6HY44 | A6HY44_RAT | Ctsd | 407 | ||
F7F3R8 | F7F3R8_RAT | Ctsd | 405 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 15 | in Ref. 2; AA sequence | ||||
Sequence: D → A | ||||||
Sequence conflict | 163 | in Ref. 3; AA sequence | ||||
Sequence: D → T | ||||||
Sequence conflict | 205 | in Ref. 2; AA sequence | ||||
Sequence: K → N | ||||||
Sequence conflict | 262 | in Ref. 2; AA sequence | ||||
Sequence: K → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X54467 EMBL· GenBank· DDBJ | CAA38349.1 EMBL· GenBank· DDBJ | mRNA |