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
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionHydrolase, 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-2022090 Assembly of collagen fibrils and other multimeric structures
R-BTA-2132295 MHC class II antigen presentation
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

Organism-specific databases

VGNCiVGNC:27813 CTSB

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagine1 Publication1
Modified residuei220N6-acetyllysineBy similarity1
Disulfide bondi227 ↔ 331

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP07688
PeptideAtlasiP07688
PRIDEiP07688

PTM databases

CarbonylDBiP07688
iPTMnetiP07688

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. Directly interacts with SHKBP1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi1584681 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
GeneTreeiENSGT00900000140859
HOGENOMiHOG000241341
HOVERGENiHBG003480
InParanoidiP07688
KOiK01363
OMAiHCGIESS
OrthoDBiEOG091G094Z
TreeFamiTF314576

Family and domain databases

InterProiView protein in InterPro
IPR025661 Pept_asp_AS
IPR000169 Pept_cys_AS
IPR025660 Pept_his_AS
IPR013128 Peptidase_C1A
IPR000668 Peptidase_C1A_C
IPR012599 Propeptide_C1A
PANTHERiPTHR12411 PTHR12411, 1 hit
PfamiView protein in Pfam
PF00112 Peptidase_C1, 1 hit
PF08127 Propeptide_C1, 1 hit
PRINTSiPR00705 PAPAIN
SMARTiView protein in SMART
SM00645 Pept_C1, 1 hit
PROSITEiView protein in PROSITE
PS00640 THIOL_PROTEASE_ASN, 1 hit
PS00139 THIOL_PROTEASE_CYS, 1 hit
PS00639 THIOL_PROTEASE_HIS, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCATB_BOVIN
AccessioniPrimary (citable) accession number: P07688
Secondary accession number(s): Q3ZC03
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: May 30, 2006
Last modified: March 28, 2018
This is version 162 of the entry and version 5 of the sequence. See 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