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P00787 (CATB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin B

EC=3.4.22.1
Alternative name(s):
Cathepsin B1
RSG-2

Cleaved into the following 2 chains:

  1. Cathepsin B light chain
  2. Cathepsin B heavy chain
Gene names
Name:Ctsb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

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

Interacts with SRPX2 By similarity. Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.

Subcellular location

Lysosome. Melanosome By similarity. Secretedextracellular space By similarity.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
Secreted
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Disulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processautophagy

Inferred from expression pattern PubMed 18567942. Source: RGD

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 18464888. Source: RGD

negative regulation of cell death

Inferred from mutant phenotype PubMed 19420257. Source: RGD

proteolysis

Inferred from direct assay PubMed 11687729PubMed 8702598. Source: RGD

regulation of catalytic activity

Inferred from electronic annotation. Source: InterPro

response to amine

Inferred from expression pattern PubMed 17371271. Source: RGD

response to cytokine

Inferred from expression pattern PubMed 19893052. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 17935147. Source: RGD

response to glucose

Inferred from expression pattern PubMed 14722017. Source: RGD

response to interleukin-4

Inferred from expression pattern PubMed 18464888. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 17379854. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 18094625. Source: RGD

response to peptide hormone

Inferred from expression pattern PubMed 18676994. Source: RGD

response to wounding

Inferred from expression pattern PubMed 15817261. Source: RGD

skeletal muscle tissue development

Inferred from expression pattern PubMed 16497156. Source: RGD

spermatogenesis

Inferred from expression pattern PubMed 9238520. Source: RGD

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 12432075. Source: RGD

cell surface

Inferred from direct assay PubMed 12432075. Source: RGD

cytoplasm

Inferred from direct assay PubMed 19941836. Source: RGD

external side of plasma membrane

Inferred from direct assay PubMed 2432075. Source: RGD

extracellular region

Inferred from direct assay PubMed 12432075. Source: RGD

extracellular space

Inferred from direct assay PubMed 19958779PubMed 2005374. Source: RGD

lysosome

Inferred from direct assay PubMed 11687729PubMed 12432075PubMed 19696938PubMed 8702598. Source: RGD

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 18938146. Source: RGD

sarcolemma

Inferred from direct assay PubMed 7043996. Source: RGD

   Molecular_functioncysteine-type endopeptidase activity

Inferred from direct assay PubMed 16960372. Source: RGD

endopeptidase activity

Inferred from direct assay PubMed 11687729PubMed 8702598. Source: RGD

kininogen binding

Inferred from physical interaction PubMed 3356189. Source: RGD

peptide binding

Inferred from direct assay PubMed 8702598. Source: RGD

protein complex binding

Inferred from physical interaction PubMed 2470410. Source: RGD

protein self-association

Inferred from direct assay PubMed 7550115. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 7962Activation peptide
PRO_0000026153
Chain80 – 333254Cathepsin B
PRO_0000026154
Chain80 – 12647Cathepsin B light chain
PRO_0000026155
Chain129 – 333205Cathepsin B heavy chain
PRO_0000026156
Propeptide334 – 3396
PRO_0000026157

Sites

Active site1081
Active site2781
Active site2981

Amino acid modifications

Modified residue2201N6-acetyllysine By similarity
Glycosylation1921N-linked (GlcNAc...) Ref.3
Disulfide bond93 ↔ 122
Disulfide bond105 ↔ 150
Disulfide bond141 ↔ 207
Disulfide bond142 ↔ 146
Disulfide bond179 ↔ 211
Disulfide bond187 ↔ 198

Natural variations

Natural variant3021V → A.

Experimental info

Sequence conflict1591W → G AA sequence Ref.3

Secondary structure

......................................................... 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00787 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 925E2E58C2B03CDA

FASTA33937,470
        10         20         30         40         50         60 
MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV DISYLKKLCG 

        70         80         90        100        110        120 
TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR DQGSCGSCWA FGAVEAMSDR 

       130        140        150        160        170        180 
ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL 

       190        200        210        220        230        240 
PYTIPPCEHH VNGSRPPCTG EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM 

       250        260        270        280        290        300 
AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW 

       310        320        330 
NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF 

« Hide

References

[1]"Cathepsin B, a cysteine protease implicated in metastatic progression, is also expressed during regression of the rat prostate and mammary glands."
Guenette R.S., Mooibroek M., Wong K., Wong P., Tenniswood M.
Eur. J. Biochem. 226:311-321(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Mammary gland.
[2]"Identification of cDNA clones encoding a precursor of rat liver cathepsin B."
San Segundo B., Chan S.J., Steiner D.F.
Proc. Natl. Acad. Sci. U.S.A. 82:2320-2324(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-339.
[3]"Homology of amino acid sequences of rat liver cathepsins B and H with that of papain."
Takio K., Towatari T., Katunuma N., Teller D.C., Titani K.
Proc. Natl. Acad. Sci. U.S.A. 80:3666-3670(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-126 AND 129-333.
Tissue: Liver.
[4]Lubec G., Afjehi-Sadat L., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 246-263, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[5]"Rat procathepsin B. Proteolytic processing to the mature form in vitro."
Rowan A.D., Mason P., Mach L., Mort J.S.
J. Biol. Chem. 267:15993-15999(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[6]"Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design."
Jia Z., Hasnain S., Hirama T., Lee X., Mort J.S., To R., Huber C.P.
J. Biol. Chem. 270:5527-5533(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[7]"Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion."
Cygler M., Sivaraman J., Grochulski P., Coulombe R., Storer A.C., Mort J.S.
Structure 4:405-416(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-339.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82396 mRNA. Translation: CAA57792.1.
M11305 mRNA. Translation: AAA40993.1.
PIRKHRTB. S51041.
UniGeneRn.100909.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CPJX-ray2.20A/B74-333[»]
1CTEX-ray2.10A/B80-333[»]
1MIRX-ray2.80A/B18-339[»]
1THEX-ray1.90A/B74-333[»]
ProteinModelPortalP00787.
SMRP00787. Positions 27-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4996314.
STRING10116.ENSRNOP00000014178.

Chemistry

BindingDBP00787.
ChEMBLCHEMBL2602.

Proteomic databases

PaxDbP00787.
PRIDEP00787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:621509. rat.

Organism-specific databases

RGD621509. Ctsb.

Phylogenomic databases

eggNOGCOG4870.
HOGENOMHOG000241341.
HOVERGENHBG003480.
InParanoidP00787.
PhylomeDBP00787.

Enzyme and pathway databases

BRENDA3.4.22.1. 5301.
SABIO-RKP00787.

Gene expression databases

GenevestigatorP00787.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00787.
PROP00787.

Entry information

Entry nameCATB_RAT
AccessionPrimary (citable) accession number: P00787
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references