Reviewed, UniProtKB/Swiss-Prot P07688 (CATB_BOVIN)

Names and origin

Protein names

Recommended name:
    Cathepsin B
    EC=3.4.22.1
Alternative name(s):
    BCSB
Cleaved into the following 2 chains:
    1- Recommended name:
            Cathepsin B light chain
    2- Recommended name:
            Cathepsin B heavy chain

Gene names

Name:

CTSB

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	335 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	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 Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro regulation of catalytic activity Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
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 Ref.4 Ref.5 Ref.6

PRO_0000026138

Chain

80 – 332

253

Cathepsin B

PRO_0000026139

Chain

80 – 126

47

Cathepsin B light chain

PRO_0000026140

Chain

129 – 332

204

Cathepsin B heavy chain

PRO_0000026141

Propeptide

333 – 335

3

PRO_0000026142

Sites

Active site

108

1

Active site

278

1

Active site

298

1

Amino acid modifications

Glycosylation

192

1

N-linked (GlcNAc...) Ref.4

Disulfide bond

93 ↔ 122

Ref.7 Ref.8

Disulfide bond

105 ↔ 150

Ref.7 Ref.8

Disulfide bond

141 ↔ 207

Ref.7 Ref.8

Disulfide bond

142 ↔ 146

Ref.7 Ref.8

Disulfide bond

179 ↔ 211

Ref.7 Ref.8

Disulfide bond

187 ↔ 198

Ref.7 Ref.8

Disulfide bond

227 ↔ 331

Ref.7 Ref.8

Experimental info

Sequence conflict

143

1

G → D in AAI02998. Ref.3

Sequence conflict

154

1

F → E AA sequence Ref.4

Sequence conflict

208

1

S → N AA sequence Ref.4

Sequence conflict

297

1

G → A AA sequence Ref.4

Secondary structure

1

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335

Helix Strand Turn

Details...

Helix

86 – 89

4

Helix

94 – 97

4

Helix

108 – 123

16

Helix

135 – 141

7

Helix

143 – 146

4

Helix

149 – 151

3

Helix

155 – 164

10

Beta strand

178 – 180

3

Beta strand

188 – 191

4

Beta strand

193 – 195

3

Helix

219 – 222

4

Beta strand

226 – 232

7

Helix

236 – 246

11

Beta strand

249 – 256

8

Helix

257 – 259

3

Beta strand

264 – 267

4

Beta strand

274 – 288

15

Beta strand

291 – 297

7

Beta strand

309 – 313

5

Helix

318 – 320

3

Beta strand

325 – 330

6

Sequences

	Sequence		Length	Mass (Da)
	P07688-1 [UniParc]. Last modified May 30, 2006. Version 5. Checksum: 865794C8B7F2AED1	FASTA	335	36,661
	10 20 30 40 50 60 MWRLLATLSC LLVLTSARSS LYFPPLSDEL VNFVNKQNTT WKAGHNFYNV DLSYVKKLCG 70 80 90 100 110 120 AILGGPKLPQ RDAFAADVVL PESFDAREQW PNCPTIKEIR DQGSCGSCWA FGAVEAISDR 130 140 150 160 170 180 ICIHSNGRVN VEVSAEDMLT CCGGECGDGC NGGFPSGAWN FWTKKGLVSG GLYNSHVGCR 190 200 210 220 230 240 PYSIPPCEHH VNGSRPPCTG EGDTPKCSKT CEPGYSPSYK EDKHFGCSSY SVANNEKEIM 250 260 270 280 290 300 AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV SGEIMGGHAI RILGWGVENG TPYWLVGNSW 310 320 330 NTDWGDNGFF KILRGQDHCG IESEIVAGMP CTHQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1856234] [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: 8373811] [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: 3379063] [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: 7106283] [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: 3144290] [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: 2390214] [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: 10739956] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 80-332.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00692061.

PIR

KHBOB. S38328.

RefSeq

NP_776456.1.

UniGene

Bt.393

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ITO	X-ray	2.29	A	80-335	[»]
1QDQ	X-ray	2.18	A	80-332	[»]
1SP4	X-ray	2.20	A	80-127	[»]
			B	128-332	[»]
2DC6	X-ray	2.30	A	80-335	[»]
2DC7	X-ray	1.94	A	80-335	[»]
2DC8	X-ray	1.94	A	80-335	[»]
2DC9	X-ray	1.94	A	80-335	[»]
2DCA	X-ray	2.11	A	80-335	[»]
2DCB	X-ray	1.94	A	80-335	[»]
2DCC	X-ray	1.93	A	80-335	[»]
2DCD	X-ray	2.50	A	80-335	[»]

SMR

P07688. Positions 18-332.

ModBase

Search...

Protein family/group databases

MEROPS

C01.060.

Genome annotation databases

Ensembl

ENSBTAG00000012442. Bos taurus. [Contig view]

GeneID

281105.

KEGG

bta:281105.

Phylogenomic databases

HOVERGEN

P07688.

OMA

P07688. TFLGGPK.

Enzyme and pathway databases

BRENDA

3.4.22.1. 251.

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.

ProDom

PD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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_BOVIN

Accession

Primary (citable) accession number: P07688
Secondary accession number(s): Q3ZC03

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	May 30, 2006
Last modified:	June 16, 2009
This is version 90 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)