Reviewed,
UniProtKB/Swiss-Prot Q28944 (CATL1_PIG)
Last modified
September 1, 2009.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cathepsin L1 EC=3.4.22.15 Cleaved into the following 2 chains: 1- Recommended name: Cathepsin L1 heavy chain 2- Recommended name: Cathepsin L1 light chain | ||||
| Gene names |
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| Organism | Sus scrofa (Pig) | ||||
| Taxonomic identifier | 9823 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 334 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Important for the overall degradation of proteins in lysosomes. |
| 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. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase C1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Lysosome |
| Domain | Signal |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| 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 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 | Potential | ||||||||
| Propeptide | 18 – 117 | 100 | Activation peptide | PRO_0000026252 | |||||||
| Chain | 118 – 289 | 172 | Cathepsin L1 heavy chain | PRO_0000026253 | |||||||
| Propeptide | 290 – 291 | 2 | By similarity | PRO_0000026254 | |||||||
| Chain | 292 – 334 | 43 | Cathepsin L1 light chain | PRO_0000026255 | |||||||
Sites | |||||||||||
| Active site | 138 | 1 | By similarity | ||||||||
| Active site | 277 | 1 | By similarity | ||||||||
| Active site | 301 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 222 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 292 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 135 ↔ 178 | By similarity | |||||||||
| Disulfide bond | 169 ↔ 212 | By similarity | |||||||||
| Disulfide bond | 270 ↔ 323 | Interchain (between heavy and light chains) By similarity | |||||||||
Sequences
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References
| [1] | "Direct evidence for the elevated synthesis and secretion of procathepsin L in the distal caput epididymis of boar." Okamura N., Tamba M., Uchiyama Y., Sugita Y., Dacheux F., Syntin P., Dacheux J.-L. Biochim. Biophys. Acta 1245:221-226(1995) [PubMed: 7492581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Epididymis. |
| [2] | "Characterization and comparative mapping of the porcine CTSL gene indicates a novel synteny between HSA9q21-->q22 and SSC10q11-->q12." Spoetter A., Droegemueller C., Kuiper H., Brenig B., Leeb T., Distl O. Cytogenet. Cell Genet. 95:92-96(2001) [PubMed: 11978977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| D37917 mRNA. Translation: BAA07140.1. AJ315771 Genomic DNA. Translation: CAC44793.1. | |
| PIR | A58195. |
| RefSeq | NP_999057.1. |
| UniGene | Ssc.54036 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ICF based on UniProtKB P07711. |
| SMR | Q28944. Positions 21-334. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C01.032. |
Genome annotation databases | |
| GeneID | 396926. |
| KEGG | ssc:396926. |
Organism-specific databases | |
| CTD | 396926. |
Phylogenomic databases | |
| HOVERGEN | Q28944. |
Enzyme and pathway databases | |
| BRENDA | 3.4.22.15. 249. |
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 | CATL1_PIG | ||||||||
| Accession | Primary (citable) accession number: Q28944 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


