Reviewed,
UniProtKB/Swiss-Prot P25326 (CATS_BOVIN)
Last modified
June 16, 2009.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cathepsin S EC=3.4.22.27 | ||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 331 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 | Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N. |
| Catalytic activity | Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound. |
| Subunit structure | Monomer. |
| 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 |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro protein bindingInferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 16 | 16 | Potential | ||||||||
| Propeptide | 17 – 114 | 98 | Activation peptide Ref.2 Ref.3 Ref.4 | PRO_0000238120 | |||||||
| Chain | 115 – 331 | 217 | Cathepsin S | PRO_0000050543 | |||||||
Sites | |||||||||||
| Active site | 139 | 1 | By similarity | ||||||||
| Active site | 278 | 1 | By similarity | ||||||||
| Active site | 298 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 104 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 126 ↔ 224 | By similarity | |||||||||
| Disulfide bond | 136 ↔ 180 | By similarity | |||||||||
| Disulfide bond | 170 ↔ 213 | By similarity | |||||||||
| Disulfide bond | 272 ↔ 320 | By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum. |
| [2] | "The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L." Ritonja A., Colic A., Dolenc I., Ogrinc T., Podobnik M., Turk V. FEBS Lett. 283:329-331(1991) [PubMed: 2044774] [Abstract] Cited for: PROTEIN SEQUENCE OF 115-331. Tissue: Spleen. |
| [3] | "Bovine cathepsins S and L: isolation and amino acid sequences." Dolenc I., Ritonja A., Colic A., Podobnik M., Ogrinc T., Turk V. Biol. Chem. Hoppe-Seyler 373:407-412(1992) [PubMed: 1515067] [Abstract] Cited for: PROTEIN SEQUENCE OF 115-331. Tissue: Spleen. |
| [4] | "Primary structure of bovine cathepsin S. Comparison to cathepsins L, H, B and papain." Wiederanders B., Broemme D., Kirschke H., Kalkkinen N., Rinne A., Paquette T., Toothman P. FEBS Lett. 286:189-192(1991) [PubMed: 1864368] [Abstract] Cited for: PROTEIN SEQUENCE OF 115-331, NUCLEOTIDE SEQUENCE [MRNA] OF 136-331. Tissue: Spleen. |
| [5] | "The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B." Broemme D., Steinert A., Friebe S., Fittkau S., Wiederanders B., Kirschke H. Biochem. J. 264:475-481(1989) [PubMed: 2604727] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| BC102245 mRNA. Translation: AAI02246.1. M95211 mRNA. Translation: AAA30435.1. X62001 mRNA. Translation: CAA43971.1. | |
| IPI | IPI00702008. |
| PIR | S15844. |
| RefSeq | NP_001028787.1. |
| UniGene | Bt.7938 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1MS6 based on UniProtKB P25774. |
| SMR | P25326. Positions 18-331. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C01.034. |
Genome annotation databases | |
| Ensembl | ENSBTAG00000017135. Bos taurus. [Contig view] |
| GeneID | 327711. |
| KEGG | bta:327711. |
Phylogenomic databases | |
| HOVERGEN | P25326. |
Enzyme and pathway databases | |
| BRENDA | 3.4.22.27. 251. |
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 | CATS_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P25326 Secondary accession number(s): Q3T0V8 | ||||||||
| 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


