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UniProtKB/Swiss-Prot entry P07688


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CATB_BOVIN
Primary accession number P07688
Secondary accession number Q3ZC03
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on May 30, 2006 (Sequence version 5)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name Cathepsin B [Precursor]
Synonyms EC 3.4.22.1
BCSB
Contains Cathepsin B light chain
Cathepsin B heavy chain
Gene name
Name: CTSB
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1856234 [NCBI, ExPASy, EBI, Israel, Japan]
Bechet D.M., Ferrara M.J., Mordier S.B., Roux M.-P., Deval C., Obled A.;
"Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B.";
J. Biol. Chem. 266:14104-14112(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Spleen;
DOI=10.1016/0167-4781(93)90205-R; PubMed=8373811 [NCBI, ExPASy, EBI, Israel, Japan]
Mordier S., Bechet D., Roux M.-P., Obled A., Ferrara M.;
"Nucleotide sequence of bovine preprocathepsin B. A study of polymorphism in the protein coding region.";
Biochim. Biophys. Acta 1174:305-311(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Thymus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 80-332, AND GLYCOSYLATION AT ASN-192.
TISSUE=Spleen;
PubMed=3379063 [NCBI, ExPASy, EBI, Israel, Japan]
Meloun B., Baudys M., Pohl J., Pavlik M., Kostka V.;
"Amino acid sequence of bovine spleen cathepsin B.";
J. Biol. Chem. 263:9087-9093(1988).
[5]
PRELIMINARY PROTEIN SEQUENCE OF 80-332.
TISSUE=Spleen;
Meloun B., Pohl J., Kostka V.;
"Tentative amino acid sequence of bovine spleen cathepsin B.";
(In) Turk V. (eds.); Cysteine proteinases and their inhibitors, pp.19-29, Walter de Gruyter, Berlin and New York (1986).
[6]
PROTEIN SEQUENCE OF 80-126.
TISSUE=Spleen;
DOI=10.1016/0014-5793(82)80210-X; PubMed=7106283 [NCBI, ExPASy, EBI, Israel, Japan]
Pohl J., Baudys M., Tomasek V., Kostka V.;
"Identification of the active site cysteine and of the disulfide bonds in the N-terminal part of the molecule of bovine spleen cathepsin B.";
FEBS Lett. 142:23-26(1982).
[7]
PROTEIN SEQUENCE OF 224-237 AND 310-332, AND DISULFIDE BOND.
TISSUE=Spleen;
PubMed=3144290 [NCBI, ExPASy, EBI, Israel, Japan]
Baudys M., Meloun B., Pohl J., Kostka V.;
"Identification of the second (buried) cysteine residue and of the C-terminal disulfide bridge of bovine spleen cathepsin B.";
Biol. Chem. Hoppe-Seyler 369:169-174(1988).
[8]
DISULFIDE BONDS.
PubMed=2390214 [NCBI, ExPASy, EBI, Israel, Japan]
Baudys M., Meloun B., Gan-Erdene T., Pohl J., Kostka V.;
"Disulfide bridges of bovine spleen cathepsin B.";
Biol. Chem. Hoppe-Seyler 371:485-491(1990).
[9]
X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 80-332.
PubMed=10739956 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto A., Tomoo K., Hara T., Murata M., Kitamura K., Ishida T.;
"Substrate specificity of bovine cathepsin B and its inhibition by CA074, based on crystal structure refinement of the complex.";
J. Biochem. 127:635-643(2000).
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: Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.
  • SUBCELLULAR LOCATION: Lysosome. Melanosome (By similarity).
  • SIMILARITY: Belongs to the peptidase C1 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L06075; AAA03064.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M64620; AAA30434.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16336; AAA80198.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16337; AAA80198.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16338; AAA80198.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16339; AAA80198.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16341; AAA80198.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16342; AAA80198.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U16343; AAA80198.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC102997; AAI02998.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S38328; KHBOB.
RefSeq NP_776456.1; -.
UniGene Bt.393
3D structure databases
PDB
1ITO; X-ray; 2.29 A; A=80-335.[ExPASy / RCSB / EBI]
1QDQ; X-ray; 2.18 A; A=80-332.[ExPASy / RCSB / EBI]
1SP4; X-ray; 2.20 A; A=80-127, B=128-332.[ExPASy / RCSB / EBI]
2DC6; X-ray; 2.30 A; A=80-335.[ExPASy / RCSB / EBI]
2DC7; X-ray; 1.94 A; A=80-335.[ExPASy / RCSB / EBI]
2DC8; X-ray; 1.94 A; A=80-335.[ExPASy / RCSB / EBI]
2DC9; X-ray; 1.94 A; A=80-335.[ExPASy / RCSB / EBI]
2DCA; X-ray; 2.11 A; A=80-335.[ExPASy / RCSB / EBI]
2DCB; X-ray; 1.94 A; A=80-335.[ExPASy / RCSB / EBI]
2DCC; X-ray; 1.93 A; A=80-335.[ExPASy / RCSB / EBI]
2DCD; X-ray; 2.50 A; A=80-335.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ITO; -.
1QDQ; -.
1SP4; -.
2DC6; -.
2DC7; -.
2DC8; -.
2DC9; -.
2DCA; -.
2DCB; -.
2DCC; -.
2DCD; -.
SMR P07688; 18-332.
ModBase P07688.
Protein family/group databases
MEROPS C01.060; -.
Ontologies
GO
GO:0005764; Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
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 of domain structure.
PANTHER PTHR12411:SF16; CathepsinB_like; 1.
PTHR12411; Peptidase_C1A; 1.
Pfam PF00112; Peptidase_C1; 1.
PF08127; Propeptide_C1; 1.
Pfam graphical view of domain structure.
PRINTS PR00705; PAPAIN.
ProDom PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00645; Pept_C1; 1.
SMART graphical view of domain structure.
PROSITE PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.
BLOCKS P07688.
ProtoNet P07688.
Genome annotation databases
Ensembl ENSBTAG00000012442; Bos taurus. [Contig view]
GeneID 281105; -.
KEGG bta:281105; -.
Phylogenomic databases
HOVERGEN P07688; -.
Other
LinkHub P07688; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Protease; Signal; Thiol protease; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17     Potential. 
PROPEP   18    79  62     Activation peptide. 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
PROPEP   333   335  3      PRO_0000026142
ACT_SITE   108   108         
ACT_SITE   278   278         
ACT_SITE   298   298         
CARBOHYD   192   192        N-linked (GlcNAc...). 
DISULFID   93   122         
DISULFID   105   150         
DISULFID   141   207         
DISULFID   142   146         
DISULFID   179   211         
DISULFID   187   198         
DISULFID   227   331         
CONFLICT   143   143        G -> D (in Ref. 3; AAI02998). 
CONFLICT   154   154        F -> E (in Ref. 4; AA sequence). 
CONFLICT   208   208        S -> N (in Ref. 4; AA sequence). 
CONFLICT   297   297        G -> A (in Ref. 4; AA sequence). 
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      
STRAND   178   180  3      
STRAND   188   191  4      
STRAND   193   195  3      
HELIX   219   222  4      
STRAND   226   232  7      
HELIX   236   246  11      
STRAND   249   256  8      
HELIX   257   259  3      
STRAND   264   267  4      
STRAND   274   288  15      
STRAND   291   297  7      
STRAND   309   313  5      
HELIX   318   320  3      
STRAND   325   330  6      
Sequence information
Length: 335 AA [This is the length of the unprocessed precursor] Molecular weight: 36661 Da [This is the MW of the unprocessed precursor] CRC64: 865794C8B7F2AED1 [This is a checksum on the sequence]
        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 

P07688 in FASTA format

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View entry in raw text format (no links)
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