Reviewed,
UniProtKB/Swiss-Prot P80532 (CATL3_FASHE)
Last modified
June 16, 2009.
Version 55.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative cathepsin L3 EC=3.4.22.15 Alternative name(s): Newly excysted juvenile protein 8 |
| Organism | Fasciola hepatica (Liver fluke) |
| Taxonomic identifier | 6192 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Platyhelminthes › Trematoda › Digenea › Echinostomida › Echinostomata › Echinostomatoidea › Fasciolidae › Fasciola |
Protein attributes
| Sequence length | 19 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Thiol protease. |
| 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 Potential. |
| Subcellular location | Lysosome Potential. |
| Developmental stage | Expressed at the newly excysted juvenile stage. |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Lysosome |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Disulfide bond |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Fasciola hepatica: rapid identification of newly excysted juvenile proteins." Tkalcevic J., Ashman K., Meeusen E. Biochem. Biophys. Res. Commun. 213:169-174(1995) [PubMed: 7639732] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.4.22.15. 39370. |
Family and domain databases | |
| InterPro | IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. [Graphical view] |
| PANTHER | PTHR12411. Peptidase_C1A. 1 hit. |
| Pfam | PF00112. Peptidase_C1. 1 hit. [Graphical view] |
| ProDom | PD000158. Peptidase_C1. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS00640. THIOL_PROTEASE_ASN. Partial match. PS00139. THIOL_PROTEASE_CYS. Partial match. PS00639. THIOL_PROTEASE_HIS. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CATL3_FASHE | ||||||||
| Accession | Primary (citable) accession number: P80532 | ||||||||
| Entry history |
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| 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


