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P00787

- CATB_RAT

UniProt

P00787 - CATB_RAT

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Protein

Cathepsin B

Gene
Ctsb
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 binding Source: RGD
  6. protein complex binding Source: RGD
  7. 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 – 1717 Reviewed predictionAdd
BLAST
Propeptidei18 – 7962Activation peptidePRO_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-acetyllysine By 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.

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 – 3710
Beta strandi40 – 434
Helixi52 – 587
Turni75 – 773
Helixi86 – 894
Turni90 – 923
Turni94 – 974
Beta strandi104 – 1063
Helixi108 – 12417
Turni125 – 1273
Helixi135 – 1417
Helixi144 – 1463
Helixi149 – 1513
Helixi155 – 16410
Beta strandi178 – 1803
Beta strandi188 – 1914
Beta strandi193 – 1953
Helixi220 – 2223
Beta strandi226 – 2327
Helixi236 – 24611
Beta strandi249 – 2568
Helixi257 – 2593
Beta strandi264 – 2674
Beta strandi274 – 28815
Beta strandi291 – 2977
Beta strandi309 – 3135
Helixi318 – 3203
Turni321 – 3233
Beta strandi325 – 3306
Helixi333 – 3386

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00787.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

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

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MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV    50
DISYLKKLCG TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR 100
DQGSCGSCWA FGAVEAMSDR ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC 150
NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL PYTIPPCEHH VNGSRPPCTG 200
EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM AEIYKNGPVE 250
GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW 300
NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF 339
Length:339
Mass (Da):37,470
Last modified:October 1, 1996 - v2
Checksum:i925E2E58C2B03CDA
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591W → G AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X82396 mRNA. Translation: CAA57792.1 .
M11305 mRNA. Translation: AAA40993.1 .
PIRi S51041. KHRTB.
UniGenei Rn.100909.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CPJ X-ray 2.20 A/B 74-333 [» ]
1CTE X-ray 2.10 A/B 80-333 [» ]
1MIR X-ray 2.80 A/B 18-339 [» ]
1THE X-ray 1.90 A/B 74-333 [» ]
ProteinModelPortali P00787.
SMRi P00787. Positions 27-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4996314.
STRINGi 10116.ENSRNOP00000014178.

Chemistry

BindingDBi P00787.
ChEMBLi CHEMBL2602.

Proteomic databases

PaxDbi P00787.
PRIDEi P00787.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:621509. rat.

Organism-specific databases

RGDi 621509. Ctsb.

Phylogenomic databases

eggNOGi COG4870.
HOGENOMi HOG000241341.
HOVERGENi HBG003480.
InParanoidi P00787.
PhylomeDBi P00787.

Enzyme and pathway databases

BRENDAi 3.4.22.1. 5301.
SABIO-RK P00787.

Miscellaneous databases

EvolutionaryTracei P00787.
PROi P00787.

Gene expression databases

Genevestigatori P00787.

Family and domain databases

InterProi IPR025661. 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 ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
PTHR12411:SF285. PTHR12411:SF285. 1 hit.
Pfami PF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 145 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

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