Reviewed,
UniProtKB/Swiss-Prot A0E358 (CATL2_PARTE)
Last modified
June 16, 2009.
Version 18.
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 2 EC=3.4.22.15 | ||
| Gene names |
| ||
| Organism | Paramecium tetraurelia | ||
| Taxonomic identifier | 5888 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Alveolata › Ciliophora › Intramacronucleata › Oligohymenophorea › Peniculida › Parameciidae › Paramecium |
Protein attributes
| Sequence length | 314 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | May be involved in extracellular digestion By similarity. |
| 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. |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Disulfide bond Zymogen |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region 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 – 24 | 24 | Potential | ||||||||
| Propeptide | 25 – 109 | 85 | Activation peptide By similarity | PRO_0000307837 | |||||||
| Chain | 110 – 314 | 205 | Cathepsin L 2 | PRO_0000307838 | |||||||
Sites | |||||||||||
| Active site | 135 | 1 | By similarity | ||||||||
| Active site | 265 | 1 | By similarity | ||||||||
| Active site | 282 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 132 ↔ 175 | By similarity | |||||||||
| Disulfide bond | 166 ↔ 207 | By similarity | |||||||||
| Disulfide bond | 259 ↔ 302 | By similarity | |||||||||
Sequences
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References
| [1] | "Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia." Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R. Wincker P.Nature 444:171-178(2006) [PubMed: 17086204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Stock d4-2. |
Cross-references
Sequence databases | |
|---|---|
| CT868656 Genomic DNA. Translation: CAK89725.1. Different initiation. | |
| UniGene | Pte.20873 |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C01.113. |
Enzyme and pathway databases | |
| BRENDA | 3.4.22.15. 21526. |
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. False negative. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CATL2_PARTE | ||||||||
| Accession | Primary (citable) accession number: A0E358 | ||||||||
| 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


