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Protein

Cathepsin B

Gene

CTSB

Organism
Bos taurus (Bovine)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.1. 908.
ReactomeiR-BTA-1442490. Collagen degradation.
R-BTA-1679131. Trafficking and processing of endosomal TLR.

Protein family/group databases

MEROPSiC01.060.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin B (EC:3.4.22.1)
Alternative name(s):
BCSB
Cleaved into the following 2 chains:
Gene namesi
Name:CTSB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 8

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2323.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – 7962Activation peptidePRO_0000026138Add
BLAST
Chaini80 – 332253Cathepsin BPRO_0000026139Add
BLAST
Chaini80 – 12647Cathepsin B light chainPRO_0000026140Add
BLAST
Chaini129 – 332204Cathepsin B heavy chainPRO_0000026141Add
BLAST
Propeptidei333 – 3353PRO_0000026142

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
Disulfide bondi227 ↔ 331

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP07688.
PeptideAtlasiP07688.
PRIDEiP07688.

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

BioGridi158468. 1 interaction.
STRINGi9913.ENSBTAP00000036650.

Chemistry

BindingDBiP07688.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi86 – 894Combined sources
Helixi94 – 974Combined sources
Beta strandi104 – 1063Combined sources
Helixi108 – 12316Combined sources
Helixi135 – 1417Combined sources
Helixi143 – 1464Combined 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 – 2604Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi274 – 28815Combined sources
Beta strandi291 – 2977Combined sources
Beta strandi309 – 3135Combined sources
Helixi318 – 3203Combined sources
Turni321 – 3233Combined sources
Beta strandi324 – 3307Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITOX-ray2.29A80-335[»]
1QDQX-ray2.18A80-332[»]
1SP4X-ray2.20A80-127[»]
B128-332[»]
2DC6X-ray2.30A80-335[»]
2DC7X-ray1.94A80-335[»]
2DC8X-ray1.94A80-335[»]
2DC9X-ray1.94A80-335[»]
2DCAX-ray2.11A80-335[»]
2DCBX-ray1.94A80-335[»]
2DCCX-ray1.93A80-335[»]
2DCDX-ray2.50A80-335[»]
ProteinModelPortaliP07688.
SMRiP07688. Positions 18-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07688.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00780000121937.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP07688.
KOiK01363.
OMAiEDMLTCC.
OrthoDBiEOG7034HR.
TreeFamiTF314576.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 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.

P07688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRLLATLSC LLVLTSARSS LYFPPLSDEL VNFVNKQNTT WKAGHNFYNV
60 70 80 90 100
DLSYVKKLCG AILGGPKLPQ RDAFAADVVL PESFDAREQW PNCPTIKEIR
110 120 130 140 150
DQGSCGSCWA FGAVEAISDR ICIHSNGRVN VEVSAEDMLT CCGGECGDGC
160 170 180 190 200
NGGFPSGAWN FWTKKGLVSG GLYNSHVGCR PYSIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGDTPKCSKT CEPGYSPSYK EDKHFGCSSY SVANNEKEIM AEIYKNGPVE
260 270 280 290 300
GAFSVYSDFL LYKSGVYQHV SGEIMGGHAI RILGWGVENG TPYWLVGNSW
310 320 330
NTDWGDNGFF KILRGQDHCG IESEIVAGMP CTHQY
Length:335
Mass (Da):36,661
Last modified:May 30, 2006 - v5
Checksum:i865794C8B7F2AED1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431G → D in AAI02998 (Ref. 3) Curated
Sequence conflicti154 – 1541F → E AA sequence (PubMed:3379063).Curated
Sequence conflicti208 – 2081S → N AA sequence (PubMed:3379063).Curated
Sequence conflicti297 – 2971G → A AA sequence (PubMed:3379063).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06075 mRNA. Translation: AAA03064.1.
M64620 mRNA. Translation: AAA30434.1.
U16336
, U16337, U16338, U16339, U16341, U16342, U16343 Genomic DNA. Translation: AAA80198.1.
BC102997 mRNA. Translation: AAI02998.1.
PIRiS38328. KHBOB.
RefSeqiNP_776456.1. NM_174031.2.
XP_005209879.1. XM_005209822.3.
XP_010805998.1. XM_010807696.2.
UniGeneiBt.393.

Genome annotation databases

EnsembliENSBTAT00000036795; ENSBTAP00000036650; ENSBTAG00000012442.
GeneIDi281105.
KEGGibta:281105.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06075 mRNA. Translation: AAA03064.1.
M64620 mRNA. Translation: AAA30434.1.
U16336
, U16337, U16338, U16339, U16341, U16342, U16343 Genomic DNA. Translation: AAA80198.1.
BC102997 mRNA. Translation: AAI02998.1.
PIRiS38328. KHBOB.
RefSeqiNP_776456.1. NM_174031.2.
XP_005209879.1. XM_005209822.3.
XP_010805998.1. XM_010807696.2.
UniGeneiBt.393.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITOX-ray2.29A80-335[»]
1QDQX-ray2.18A80-332[»]
1SP4X-ray2.20A80-127[»]
B128-332[»]
2DC6X-ray2.30A80-335[»]
2DC7X-ray1.94A80-335[»]
2DC8X-ray1.94A80-335[»]
2DC9X-ray1.94A80-335[»]
2DCAX-ray2.11A80-335[»]
2DCBX-ray1.94A80-335[»]
2DCCX-ray1.93A80-335[»]
2DCDX-ray2.50A80-335[»]
ProteinModelPortaliP07688.
SMRiP07688. Positions 18-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158468. 1 interaction.
STRINGi9913.ENSBTAP00000036650.

Chemistry

BindingDBiP07688.
ChEMBLiCHEMBL2323.

Protein family/group databases

MEROPSiC01.060.

Proteomic databases

PaxDbiP07688.
PeptideAtlasiP07688.
PRIDEiP07688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000036795; ENSBTAP00000036650; ENSBTAG00000012442.
GeneIDi281105.
KEGGibta:281105.

Organism-specific databases

CTDi1508.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00780000121937.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP07688.
KOiK01363.
OMAiEDMLTCC.
OrthoDBiEOG7034HR.
TreeFamiTF314576.

Enzyme and pathway databases

BRENDAi3.4.22.1. 908.
ReactomeiR-BTA-1442490. Collagen degradation.
R-BTA-1679131. Trafficking and processing of endosomal TLR.

Miscellaneous databases

EvolutionaryTraceiP07688.
PROiP07688.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 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

« Hide 'large scale' publications
  1. "Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B."
    Bechet D.M., Ferrara M.J., Mordier S.B., Roux M.-P., Deval C., Obled A.
    J. Biol. Chem. 266:14104-14112(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Nucleotide sequence of bovine preprocathepsin B. A study of polymorphism in the protein coding region."
    Mordier S., Bechet D., Roux M.-P., Obled A., Ferrara M.
    Biochim. Biophys. Acta 1174:305-311(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Spleen.
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Thymus.
  4. "Amino acid sequence of bovine spleen cathepsin B."
    Meloun B., Baudys M., Pohl J., Pavlik M., Kostka V.
    J. Biol. Chem. 263:9087-9093(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 80-332, GLYCOSYLATION AT ASN-192.
    Tissue: Spleen.
  5. "Tentative amino acid sequence of bovine spleen cathepsin B."
    Meloun B., Pohl J., Kostka V.
    (In) Turk V. (eds.); Cysteine proteinases and their inhibitors, pp.19-29, Walter de Gruyter, Berlin and New York (1986)
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 80-332.
    Tissue: Spleen.
  6. "Identification of the active site cysteine and of the disulfide bonds in the N-terminal part of the molecule of bovine spleen cathepsin B."
    Pohl J., Baudys M., Tomasek V., Kostka V.
    FEBS Lett. 142:23-26(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 80-126.
    Tissue: Spleen.
  7. "Identification of the second (buried) cysteine residue and of the C-terminal disulfide bridge of bovine spleen cathepsin B."
    Baudys M., Meloun B., Pohl J., Kostka V.
    Biol. Chem. Hoppe-Seyler 369:169-174(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 224-237 AND 310-332, DISULFIDE BOND.
    Tissue: Spleen.
  8. "Disulfide bridges of bovine spleen cathepsin B."
    Baudys M., Meloun B., Gan-Erdene T., Pohl J., Kostka V.
    Biol. Chem. Hoppe-Seyler 371:485-491(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  9. "Substrate specificity of bovine cathepsin B and its inhibition by CA074, based on crystal structure refinement of the complex."
    Yamamoto A., Tomoo K., Hara T., Murata M., Kitamura K., Ishida T.
    J. Biochem. 127:635-643(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 80-332.

Entry informationi

Entry nameiCATB_BOVIN
AccessioniPrimary (citable) accession number: P07688
Secondary accession number(s): Q3ZC03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: May 30, 2006
Last modified: July 6, 2016
This is version 150 of the entry and version 5 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

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 one 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.