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P00787

- CATB_RAT

UniProt

P00787 - CATB_RAT

Protein

Cathepsin B

Gene

Ctsb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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

    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

    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 – 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.
    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

    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

    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:
    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: October 1, 2014
    This is version 146 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