Q5R6D1 (CATB_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 41.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cathepsin B EC=3.4.22.1 Cleaved into the following 2 chains: | ||
| Gene names |
| ||
| Organism | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
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 transcript level |
General annotation (Comments)
| Function | Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis By similarity. |
| Catalytic activity | Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. |
| Subunit structure | Dimer of a heavy chain and a light chain cross-linked by a disulfide bond. Interacts with SRPX2 By similarity. |
| Subcellular location | Lysosome By similarity. Melanosome By similarity. |
| 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: UniProtKB-KW regulation of catalytic activityInferred from electronic annotation. Source: InterPro |
| Cellular component | lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell melanosomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 – 79 | 62 | Activation peptide By similarity | PRO_0000330880 | |||||||
| Chain | 80 – 333 | 254 | Cathepsin B | PRO_0000330881 | |||||||
| Chain | 80 – 126 | 47 | Cathepsin B light chain By similarity | PRO_0000330882 | |||||||
| Chain | 129 – 333 | 205 | Cathepsin B heavy chain By similarity | PRO_0000330883 | |||||||
| Propeptide | 334 – 339 | 6 | By similarity | PRO_0000330884 | |||||||
Sites | |||||||||||
| Active site | 108 | 1 | By similarity | ||||||||
| Active site | 278 | 1 | By similarity | ||||||||
| Active site | 298 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 192 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 93 ↔ 122 | By similarity | |||||||||
| Disulfide bond | 105 ↔ 150 | By similarity | |||||||||
| Disulfide bond | 141 ↔ 207 | By similarity | |||||||||
| Disulfide bond | 142 ↔ 146 | By similarity | |||||||||
| Disulfide bond | 179 ↔ 211 | By similarity | |||||||||
| Disulfide bond | 187 ↔ 198 | By similarity | |||||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR860464 mRNA. Translation: CAH92586.1. CR860560 mRNA. Translation: CAH92685.1. |
| RefSeq | NP_001126573.1. NM_001133101.1. |
| UniGene | Pab.17972. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1HUC based on UniProtKB P07858. |
| ProteinModelPortal | Q5R6D1. |
| SMR | Q5R6D1. Positions 18-333. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C01.060. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSPPYT00000021385; ENSPPYP00000020558; ENSPPYG00000018345. |
| GeneID | 100173564. |
| KEGG | pon:100173564. |
Organism-specific databases | |
| CTD | 1508. |
Phylogenomic databases | |
| HOVERGEN | HBG003480. |
| InParanoid | Q5R6D1. |
| OMA | TIPPCEH. |
| OrthoDB | EOG4K6G4C. |
Family and domain databases | |
| InterPro | IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR015643. Peptidase_C1A_cathepsin-B. IPR012599. Propeptide_C1A. [Graphical view] |
| KO | K01363. |
| PANTHER | PTHR12411:SF16. CathepsinB_like. 1 hit. PTHR12411. Peptidase_C1A. 1 hit. |
| Pfam | PF00112. Peptidase_C1. 1 hit. PF08127. Propeptide_C1. 1 hit. [Graphical view] |
| PRINTS | PR00705. PAPAIN. |
| 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 | CATB_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5R6D1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with