Cathepsin B (Rattus norvegicus)

Basic Information
Short Name	CSPB, CTSB
UNP ID	P00787
Organism	Rattus norvegicus
Cys Site	Cys108
Family/Domain	Peptidase C1 family
Known Ligand	Ligand list
Function Type	Protease

Summary

Protein Function

Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. (From Uniprot)
Cathepsin B (CatB) is an enzymatic protein belonging to the peptidase (or protease) families. In humans, it is coded by the CTSB gene. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene. (From Wikipedia)

Cys Function & Property

Cys108 is one of the active sites of Cathepsin B, which is very close to His278 and Asn298 in space. These three residues formed a typical catalytic triad motif.

• Hydrophobic property:

• SASA：

Cys108: 4.025 A^2

Protein Sequence

MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV
DISYLKKLCG TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR
DQGSCGSCWA FGAVEAMSDR ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC
NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL PYTIPPCEHH VNGSRPPCTG
EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM AEIYKNGPVE
GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW
NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF

Structural Information

• Known structure with covalent ligand:
  

1THE, 1CTE

• Protein structure:

Related Pathway

• Autophagy - animal
  
• Lysosome
  
• Apoptosis
  
• Antigen processing and presentation
  
• NOD-like receptor signaling pathway
  
• Renin secretion
  

Experimental Evidence

Crystallography

Reference

1. Jia Z, Hasnain S, Hirama T, et al. Crystal Structures of Recombinant Rat Cathepsin B and a Cathepsin B-Inhibitor Complex IMPLICATIONS FOR STRUCTURE-BASED INHIBITOR DESIGN[J]. Journal of Biological Chemistry, 1995, 270(10): 5527-5533. 7890671