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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)DescriptionActionsGraphical viewLength
Active sitei1081
Active sitei2781
Active sitei2981

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.
R-BTA-6798695. Neutrophil degranulation.

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 databases

ChEMBLiCHEMBL2323.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002613818 – 79Activation peptideAdd BLAST62
ChainiPRO_000002613980 – 332Cathepsin BAdd BLAST253
ChainiPRO_000002614080 – 126Cathepsin B light chainAdd BLAST47
ChainiPRO_0000026141129 – 332Cathepsin B heavy chainAdd BLAST204
PropeptideiPRO_0000026142333 – 3353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi93 ↔ 122
Disulfide bondi105 ↔ 150
Disulfide bondi141 ↔ 207
Disulfide bondi142 ↔ 146
Disulfide bondi179 ↔ 211
Disulfide bondi187 ↔ 198
Glycosylationi192N-linked (GlcNAc...)1 Publication1
Modified residuei220N6-acetyllysineBy similarity1
Disulfide bondi227 ↔ 331

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP07688.
PeptideAtlasiP07688.
PRIDEiP07688.

Expressioni

Gene expression databases

BgeeiENSBTAG00000012442.

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 interactor.
STRINGi9913.ENSBTAP00000036650.

Chemistry databases

BindingDBiP07688.

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi86 – 89Combined sources4
Helixi94 – 97Combined sources4
Beta strandi104 – 106Combined sources3
Helixi108 – 123Combined sources16
Helixi135 – 141Combined sources7
Helixi143 – 146Combined sources4
Helixi149 – 151Combined sources3
Helixi155 – 164Combined sources10
Beta strandi178 – 180Combined sources3
Beta strandi188 – 191Combined sources4
Beta strandi193 – 195Combined sources3
Helixi220 – 222Combined sources3
Beta strandi226 – 232Combined sources7
Helixi236 – 246Combined sources11
Beta strandi249 – 256Combined sources8
Helixi257 – 260Combined sources4
Beta strandi264 – 267Combined sources4
Beta strandi274 – 288Combined sources15
Beta strandi291 – 297Combined sources7
Beta strandi309 – 313Combined sources5
Helixi318 – 320Combined sources3
Turni321 – 323Combined sources3
Beta strandi324 – 330Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OrthoDBiEOG091G094Z.
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)DescriptionActionsGraphical viewLength
Sequence conflicti143G → D in AAI02998 (Ref. 3) Curated1
Sequence conflicti154F → E AA sequence (PubMed:3379063).Curated1
Sequence conflicti208S → N AA sequence (PubMed:3379063).Curated1
Sequence conflicti297G → A AA sequence (PubMed:3379063).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158468. 1 interactor.
STRINGi9913.ENSBTAP00000036650.

Chemistry databases

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.
OrthoDBiEOG091G094Z.
TreeFamiTF314576.

Enzyme and pathway databases

BRENDAi3.4.22.1. 908.
ReactomeiR-BTA-1442490. Collagen degradation.
R-BTA-1679131. Trafficking and processing of endosomal TLR.
R-BTA-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP07688.
PROiP07688.

Gene expression databases

BgeeiENSBTAG00000012442.

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...

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: November 30, 2016
This is version 154 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.