Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cathepsin B

Gene

Ctsb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081
Active sitei278 – 2781
Active sitei298 – 2981

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: RGD
  2. endopeptidase activity Source: RGD
  3. kininogen binding Source: RGD
  4. peptide binding Source: RGD
  5. protein complex binding Source: RGD
  6. protein self-association Source: RGD

GO - Biological processi

  1. autophagy Source: RGD
  2. cellular response to mechanical stimulus Source: RGD
  3. negative regulation of cell death Source: RGD
  4. proteolysis Source: RGD
  5. regulation of catalytic activity Source: InterPro
  6. response to amine Source: RGD
  7. response to cytokine Source: RGD
  8. response to ethanol Source: RGD
  9. response to glucose Source: RGD
  10. response to interleukin-4 Source: RGD
  11. response to mechanical stimulus Source: RGD
  12. response to organic cyclic compound Source: RGD
  13. response to peptide hormone Source: RGD
  14. response to wounding Source: RGD
  15. skeletal muscle tissue development Source: RGD
  16. spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.1. 5301.
SABIO-RKP00787.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin B (EC:3.4.22.1)
Alternative name(s):
Cathepsin B1
RSG-2
Cleaved into the following 2 chains:
Gene namesi
Name:Ctsb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621509. Ctsb.

Subcellular locationi

Lysosome. Melanosome By similarity. Secretedextracellular space By similarity

GO - Cellular componenti

  1. apical plasma membrane Source: RGD
  2. cell surface Source: RGD
  3. cytoplasm Source: RGD
  4. external side of plasma membrane Source: RGD
  5. extracellular region Source: RGD
  6. extracellular space Source: RGD
  7. lysosome Source: RGD
  8. melanosome Source: UniProtKB-SubCell
  9. mitochondrion Source: RGD
  10. sarcolemma Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 7962Activation peptide1 PublicationPRO_0000026153Add
BLAST
Chaini80 – 333254Cathepsin BPRO_0000026154Add
BLAST
Chaini80 – 12647Cathepsin B light chainPRO_0000026155Add
BLAST
Chaini129 – 333205Cathepsin B heavy chainPRO_0000026156Add
BLAST
Propeptidei334 – 3396PRO_0000026157

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi93 ↔ 122
Disulfide bondi105 ↔ 150
Disulfide bondi141 ↔ 207
Disulfide bondi142 ↔ 146
Disulfide bondi179 ↔ 211
Disulfide bondi187 ↔ 198
Glycosylationi192 – 1921N-linked (GlcNAc...)1 Publication
Modified residuei220 – 2201N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP00787.
PRIDEiP00787.

Expressioni

Gene expression databases

GenevestigatoriP00787.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

MINTiMINT-4996314.
STRINGi10116.ENSRNOP00000014178.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 3710Combined sources
Beta strandi40 – 434Combined sources
Helixi52 – 587Combined sources
Turni75 – 773Combined sources
Helixi86 – 894Combined sources
Turni90 – 923Combined sources
Turni94 – 974Combined sources
Beta strandi104 – 1063Combined sources
Helixi108 – 12417Combined sources
Turni125 – 1273Combined sources
Helixi135 – 1417Combined sources
Helixi144 – 1463Combined sources
Helixi149 – 1513Combined sources
Helixi155 – 16410Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi193 – 1953Combined sources
Helixi220 – 2223Combined sources
Beta strandi226 – 2327Combined sources
Helixi236 – 24611Combined sources
Beta strandi249 – 2568Combined sources
Helixi257 – 2593Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi274 – 28815Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi309 – 3135Combined sources
Helixi318 – 3203Combined sources
Turni321 – 3233Combined sources
Beta strandi325 – 3306Combined sources
Helixi333 – 3386Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CPJX-ray2.20A/B74-333[»]
1CTEX-ray2.10A/B80-333[»]
1MIRX-ray2.80A/B18-339[»]
1THEX-ray1.90A/B74-333[»]
ProteinModelPortaliP00787.
SMRiP00787. Positions 27-339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00787.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP00787.
PhylomeDBiP00787.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR015643. Peptidase_C1A_cathepsin-B.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF285. PTHR12411:SF285. 1 hit.
PfamiPF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV
60 70 80 90 100
DISYLKKLCG TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR
110 120 130 140 150
DQGSCGSCWA FGAVEAMSDR ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC
160 170 180 190 200
NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL PYTIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM AEIYKNGPVE
260 270 280 290 300
GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW
310 320 330
NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF
Length:339
Mass (Da):37,470
Last modified:October 1, 1996 - v2
Checksum:i925E2E58C2B03CDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591W → G AA sequence (PubMed:6574504).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti302 – 3021V → A.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82396 mRNA. Translation: CAA57792.1.
M11305 mRNA. Translation: AAA40993.1.
PIRiS51041. KHRTB.
UniGeneiRn.100909.

Genome annotation databases

UCSCiRGD:621509. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82396 mRNA. Translation: CAA57792.1.
M11305 mRNA. Translation: AAA40993.1.
PIRiS51041. KHRTB.
UniGeneiRn.100909.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CPJX-ray2.20A/B74-333[»]
1CTEX-ray2.10A/B80-333[»]
1MIRX-ray2.80A/B18-339[»]
1THEX-ray1.90A/B74-333[»]
ProteinModelPortaliP00787.
SMRiP00787. Positions 27-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4996314.
STRINGi10116.ENSRNOP00000014178.

Chemistry

BindingDBiP00787.
ChEMBLiCHEMBL2602.

Proteomic databases

PaxDbiP00787.
PRIDEiP00787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:621509. rat.

Organism-specific databases

RGDi621509. Ctsb.

Phylogenomic databases

eggNOGiCOG4870.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP00787.
PhylomeDBiP00787.

Enzyme and pathway databases

BRENDAi3.4.22.1. 5301.
SABIO-RKP00787.

Miscellaneous databases

EvolutionaryTraceiP00787.
PROiP00787.

Gene expression databases

GenevestigatoriP00787.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR015643. Peptidase_C1A_cathepsin-B.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF285. PTHR12411:SF285. 1 hit.
PfamiPF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCATB_RAT
AccessioniPrimary (citable) accession number: P00787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: March 4, 2015
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.