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Protein

Cathepsin B

Gene

Ctsb

Organism
Rattus norvegicus (Rat)
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

  • collagen binding Source: RGD
  • cysteine-type endopeptidase activity Source: CAFA
  • cysteine-type peptidase activity Source: RGD
  • endopeptidase activity Source: RGD
  • kininogen binding Source: RGD
  • peptidase activity Source: RGD
  • peptide binding Source: RGD
  • protein self-association Source: RGD
  • proteoglycan binding Source: RGD

GO - Biological processi

  • autophagy Source: RGD
  • cellular response to mechanical stimulus Source: RGD
  • cellular response to thyroid hormone stimulus Source: RGD
  • collagen catabolic process Source: RGD
  • decidualization Source: RGD
  • epithelial cell differentiation Source: RGD
  • negative regulation of cell death Source: RGD
  • proteolysis Source: CAFA
  • proteolysis involved in cellular protein catabolic process Source: RGD
  • regulation of catalytic activity Source: InterPro
  • response to amine Source: RGD
  • response to cytokine Source: RGD
  • response to ethanol Source: RGD
  • response to glucose Source: RGD
  • response to interleukin-4 Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to wounding Source: RGD
  • skeletal muscle tissue development Source: RGD
  • spermatogenesis Source: RGD
  • viral entry into host cell Source: RGD

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.1 5301
SABIO-RKiP00787

Protein family/group databases

MEROPSiC01.060

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621509 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

ChEMBLiCHEMBL2602

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002615318 – 79Activation peptide1 PublicationAdd BLAST62
ChainiPRO_000002615480 – 333Cathepsin BAdd BLAST254
ChainiPRO_000002615580 – 126Cathepsin B light chainAdd BLAST47
ChainiPRO_0000026156129 – 333Cathepsin B heavy chainAdd BLAST205
PropeptideiPRO_0000026157334 – 3396

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

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP00787
PRIDEiP00787

PTM databases

iPTMnetiP00787
PhosphoSitePlusiP00787
SwissPalmiP00787

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

GO - Molecular functioni

  • kininogen binding Source: RGD
  • protein self-association Source: RGD
  • proteoglycan binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014178

Chemistry databases

BindingDBiP00787

Structurei

Secondary structure

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 37Combined sources10
Beta strandi40 – 43Combined sources4
Helixi52 – 58Combined sources7
Turni75 – 77Combined sources3
Helixi86 – 89Combined sources4
Turni90 – 92Combined sources3
Turni94 – 97Combined sources4
Beta strandi104 – 106Combined sources3
Helixi108 – 124Combined sources17
Turni125 – 127Combined sources3
Helixi135 – 141Combined sources7
Helixi144 – 146Combined sources3
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 – 259Combined sources3
Beta strandi264 – 267Combined sources4
Beta strandi274 – 288Combined sources15
Beta strandi291 – 297Combined sources7
Beta strandi309 – 313Combined sources5
Helixi318 – 320Combined sources3
Turni321 – 323Combined sources3
Beta strandi325 – 330Combined sources6
Helixi333 – 338Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00787

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543 Eukaryota
COG4870 LUCA
HOGENOMiHOG000241341
HOVERGENiHBG003480
InParanoidiP00787
PhylomeDBiP00787

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.

P00787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV
60 70 80 90 100
DISYLKKLCG TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR
110 120 130 140 150
DQGSCGSCWA FGAVEAMSDR ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC
160 170 180 190 200
NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL PYTIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM AEIYKNGPVE
260 270 280 290 300
GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW
310 320 330
NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF
Length:339
Mass (Da):37,470
Last modified:October 1, 1996 - v2
Checksum:i925E2E58C2B03CDA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti159W → G AA sequence (PubMed:6574504).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti302V → A. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82396 mRNA Translation: CAA57792.1
M11305 mRNA Translation: AAA40993.1
PIRiS51041 KHRTB
UniGeneiRn.100909

Genome annotation databases

UCSCiRGD:621509 rat

Similar proteinsi

Entry informationi

Entry nameiCATB_RAT
AccessioniPrimary (citable) accession number: P00787
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: April 25, 2018
This is version 168 of the entry and version 2 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
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Main funding by: National Institutes of Health