P00787 (CATB_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin B
EC=3.4.22.1

Alternative name(s):
Cathepsin B1
RSG-2

Cleaved into the following 2 chains:

1. Cathepsin B light chain
2. Cathepsin B heavy chain

Gene names

Name:

Ctsb

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.
Catalytic activity	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.
Subunit structure	Interacts with SRPX2 By similarity. Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.
Subcellular location	Lysosome. Melanosome By similarity.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	autophagy Inferred from expression pattern. Source: RGD negative regulation of cell death Inferred from mutant phenotype. Source: RGD proteolysis Inferred from direct assay. Source: RGD regulation of catalytic activity Inferred from electronic annotation. Source: InterPro response to amine stimulus Inferred from expression pattern. Source: RGD response to ethanol Inferred from expression pattern. Source: RGD response to glucose stimulus Inferred from expression pattern. Source: RGD response to interleukin-4 Inferred from expression pattern. Source: RGD response to mechanical stimulus Inferred from expression pattern. Source: RGD response to organic cyclic compound Inferred from expression pattern. Source: RGD response to peptide hormone stimulus Inferred from expression pattern. Source: RGD response to wounding Inferred from expression pattern. Source: RGD skeletal muscle tissue development Inferred from expression pattern. Source: RGD
Cellular component	apical plasma membrane Inferred from direct assay. Source: RGD external side of plasma membrane Inferred from direct assay. Source: RGD extracellular space Inferred from direct assay. Source: RGD lysosome Inferred from direct assay. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: RGD sarcolemma Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	cysteine-type endopeptidase activity Inferred from direct assay. Source: RGD kininogen binding Inferred from physical interaction. Source: RGD peptide binding Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Propeptide

18 – 79

62

Activation peptide

PRO_0000026153

Chain

80 – 333

254

Cathepsin B

PRO_0000026154

Chain

80 – 126

47

Cathepsin B light chain

PRO_0000026155

Chain

129 – 333

205

Cathepsin B heavy chain

PRO_0000026156

Propeptide

334 – 339

6

PRO_0000026157

Sites

Active site

108

1

Active site

278

1

Active site

298

1

Amino acid modifications

Glycosylation

192

1

N-linked (GlcNAc...) Ref.3

Disulfide bond

93 ↔ 122

Disulfide bond

105 ↔ 150

Disulfide bond

141 ↔ 207

Disulfide bond

142 ↔ 146

Disulfide bond

179 ↔ 211

Disulfide bond

187 ↔ 198

Natural variations

Natural variant

302

1

V → A.

Experimental info

Sequence conflict

159

1

W → G AA sequence Ref.3

Secondary structure

1

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339

Helix Strand Turn

Details...

Helix

86 – 89

4

Turn

90 – 92

3

Helix

95 – 97

3

Helix

108 – 124

17

Turn

125 – 127

3

Helix

135 – 141

7

Helix

149 – 151

3

Helix

155 – 164

10

Beta strand

188 – 191

4

Turn

219 – 222

4

Beta strand

226 – 232

7

Helix

236 – 246

11

Beta strand

249 – 252

4

Helix

257 – 259

3

Beta strand

264 – 267

4

Beta strand

274 – 276

3

Beta strand

279 – 288

10

Beta strand

291 – 297

7

Beta strand

309 – 313

5

Helix

318 – 320

3

Turn

321 – 323

3

Beta strand

325 – 330

6

Helix

333 – 338

6

Sequences

	Sequence		Length	Mass (Da)
	P00787 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 925E2E58C2B03CDA	FASTA	339	37,470
	10 20 30 40 50 60 MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV DISYLKKLCG 70 80 90 100 110 120 TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR DQGSCGSCWA FGAVEAMSDR 130 140 150 160 170 180 ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL 190 200 210 220 230 240 PYTIPPCEHH VNGSRPPCTG EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM 250 260 270 280 290 300 AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW 310 320 330 NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF

References

[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: 8001549] [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: 2986112] [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: 6574504] [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, 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: 1639824] [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: 7890671] [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: 8740363] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-339.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X82396 mRNA. Translation: CAA57792.1.
M11305 mRNA. Translation: AAA40993.1.

IPI

IPI00212811.

PIR

KHRTB. S51041.

UniGene

Rn.100909.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00787.

SMR

P00787. Positions 27-339.

ModBase

Search...

Protein-protein interaction databases

STRING

P00787.

Protein family/group databases

MEROPS

C01.060.

Proteomic databases

PRIDE

P00787.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

UCSC

NM_022597. rat.

Organism-specific databases

RGD

621509. Ctsb.

Phylogenomic databases

eggNOG

roNOG08540.

HOVERGEN

HBG003480.

InParanoid

P00787.

OrthoDB

EOG4K6G4C.

Enzyme and pathway databases

BRENDA

3.4.22.1. 5301.

Gene expression databases

ArrayExpress

P00787.

Genevestigator

P00787.

GermOnline

ENSRNOG00000010331. Rattus norvegicus.

Family and domain databases

InterPro

IPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR015643. Peptidase_C1A_cathepsin-B.
IPR012599. Propeptide_C1A.
[Graphical view]

PANTHER

PTHR12411:SF16. CathepsinB_like. 1 hit.
PTHR12411. Peptidase_C1A. 1 hit.

Pfam

PF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]

PRINTS

PR00705. PAPAIN.

SMART

SM00645. Pept_C1. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CATB_RAT

Accession

Primary (citable) accession number: P00787

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1996
Last modified:	October 19, 2011
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program