Reviewed,
UniProtKB/Swiss-Prot Q26636 (CATL_SARPE)
Last modified
June 16, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cathepsin L EC=3.4.22.15 Cleaved into the following 2 chains: 1- Recommended name: Cathepsin L heavy chain 2- Recommended name: Cathepsin L light chain |
| Organism | Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina) |
| Taxonomic identifier | 7386 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Oestroidea › Sarcophagidae › Sarcophaga › Boettcherisca |
Protein attributes
| Sequence length | 339 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Important for the overall degradation of proteins in lysosomes. Required for differentiation of imaginal disks. Ref.1 |
| Catalytic activity | Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity. |
| Subunit structure | Dimer of a heavy and a light chain linked by disulfide bonds By similarity. |
| Subcellular location | |
| Developmental stage | Highly expressed during embryonic development with higher levels in first instar than in third instar. Ref.1 |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Differentiation |
| Cellular component | Lysosome |
| Domain | Signal |
| Molecular function | Developmental protein Hydrolase Protease Thiol protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal developmentInferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Ref.1 | ||||||||
| Propeptide | 18 – 121 | 104 | Activation peptide | PRO_0000026269 | |||||||
| Chain | 122 – 294 | 173 | Cathepsin L heavy chain | PRO_0000026270 | |||||||
| Propeptide | 295 – 298 | 4 | By similarity | PRO_0000026271 | |||||||
| Chain | 299 – 339 | 41 | Cathepsin L light chain | PRO_0000026272 | |||||||
Sites | |||||||||||
| Active site | 146 | 1 | By similarity | ||||||||
| Active site | 285 | 1 | By similarity | ||||||||
| Active site | 306 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 96 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 143 ↔ 186 | By similarity | |||||||||
| Disulfide bond | 177 ↔ 219 | By similarity | |||||||||
| Disulfide bond | 278 ↔ 328 | Interchain (between heavy and light chains) By similarity | |||||||||
Sequences
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References
| [1] | "Purification, characterization, and cDNA cloning of procathepsin L from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly), and its involvement in the differentiation of imaginal discs." Homma K., Kurata S., Natori S. J. Biol. Chem. 269:15258-15264(1994) [PubMed: 8195162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-27; 122-135; 139-154; 200-208; 224-239 AND 306-319, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE. |
Cross-references
Sequence databases | |
|---|---|
| D16533 mRNA. Translation: BAA03970.1. | |
| PIR | A53810. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CJL based on UniProtKB P07711. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C01.092. |
Enzyme and pathway databases | |
| BRENDA | 3.4.22.15. 67068. |
Family and domain databases | |
| InterPro | IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view] |
| PANTHER | PTHR12411. Peptidase_C1A. 1 hit. |
| Pfam | PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view] |
| PRINTS | PR00705. PAPAIN. |
| ProDom | PD000158. Peptidase_C1. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00645. Pept_C1. 1 hit. [Graphical view] |
| PROSITE | PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CATL_SARPE | ||||||||
| Accession | Primary (citable) accession number: Q26636 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


