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Primary Information | |
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| BoMiProt ID | Bomi9 |
| Protein Name | Cathepsin B |
| Organism | Bos taurus |
| Uniprot ID | P07688 |
| Milk Fraction | Whey |
| Ref Sequence ID | NP_776456.1 |
| Aminoacid Length | 335 |
| Molecular Weight | 36661 |
| FASTA Sequence | Download |
| Gene Name | CTSB |
| Gene ID | 281105 |
| Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | lung secretions, liver, spleen, kidney, chorion, |
| Protein Function | cysteine proteinase; degrades proteins such as caseins, insulin and collagen showing broad substrate specificity; exert an antihypertensive effect; has role in generation of thyroid hormones by proteolytic processing of thyroglobulin; role in calcium homeostasis; linked to neoplasia and metastasis; induces breakdown of cartilage proteoglycan. Cathepsin B is a cysteine-protease enzyme that plays significant role in metalloproteinase regulation. |
| Biochemical Properties | Endopeptidase; activated by DTT, optimum pH is 6; inactivated at pH above 7; broad substrate specificity; partially survived heat treatments; similar to chymosin in its cleavage sites; stable between pH 4.0 and pH 6.5, but it was very unstable at alkaline pH values. It was stable on heat treatment at 35 "C, 42 "C, and 47 "C for 15 min at pH 6.0; requires the presence of a sulfhydryl compound plus EDTA for maximal activity; inhibited by monoiodoacetate, microbial inhibitors such as leupeptin, chymostatin, and antipain, L-l-tosylamido- 2-phenylethylchloromethyl ketone, E-64 |
| Significance in milk | Cleaves ß and αS1 caseins; result in plasmin-like activity in high SCC milk and dairy products; |
| PTMs | 111th Asn is glycosylated with high mannose type sugar |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P07688|CATB_BOVIN Cathepsin B OS=Bos taurus OX=9913 GN=CTSB PE=1 SV=5 MWRLLATLSCLLVLTSARSSLYFPPLSDELVNFVNKQNTTWKAGHNFYNVDLSYVKKLCG AILGGPKLPQRDAFAADVVLPESFDAREQWPNCPTIKEIRDQGSCGSCWAFGAVEAISDR ICIHSNGRVNVEVSAEDMLTCCGGECGDGCNGGFPSGAWNFWTKKGLVSGGLYNSHVGCR PYSIPPCEHHVN*192GSRPPCTGEGDTPKCSKTCEPGYSPSYKEDKHFGCSSYSVANNEKEIM AEIYKNGPVEGAFSVYSDFLLYKSGVYQHVSGEIMGGHAIRILGWGVENGTPYWLVGNSW NTDWGDNGFFKILRGQDHCGIESEIVAGMPCTHQY |
| SCOP | Class : Alpha and beta proteins (a+b) Fold : Canonical type of Cysteine proteinases catalytic core Superfamily : Cysteine proteinases Family : Papain-like Domain Name : 2DCC A:1-253 |
| CATH | Matched CATH superfamily 1.20.5.170 3.90.70.10 |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Significance of PTMs | Mannose-6-phosphate-moities play a role as the targeting marker to the lysosomes |
| PDB ID | 1ITO, 1QDQ, 1SP4, 2DC6, 2DC7, 2DC8, 2DC9, 2DCA, 2DCB, 2DCC, 2DCD, |
| Additional Comments | Potentially influence the yield and quality of dairy products; significantly important in cancer therapy; inactivated aldolases (muscle and liver) and glucokinase as reported in rat liver; Amino acid analysis showed that crystalline cathepsin B contained hexosamine, and that the contents of glycine, aspartic acid, and glutamic acid are high and the content of methionine is low, as in cathepsin B from human liver |
| Bibliography | 1. TOWATARI, T., KAWABATA, Y., & KATUNUMA, N. (1979). Crystallization and Properties of Cathepsin B from Rat Liver. European Journal of Biochemistry, 102(1), 279–289. https://doi.org/10.1111/j.1432-1033.1979.tb06290.x. >br/> 2. Berquin, I. M., Cao, L., Fong, D., & Sloane, B. F. (1995). Identification of two new exons and multiple transcription start points in the 5’-untranslated region of the human cathepsin-B-encoding gene. Gene, 159(2), 143–149. https://doi.org/10.1016/0378-1119(95)00072-e. 3. Takio, K., Towatari, T., Katunuma, N., & Titani, K. (1980). Primary structure study of rat liver cathepsin B -----A striking resemblance to papain. Topics in Catalysis, 97(1), 340–346. https://doi.org/10.1016/S0006-291X(80)80173-2. 4. Burnett, D., Abrahamson, M., Devalia, J. L., Sapsford, R. J., Davies, R. J., & Buttle, D. J. (1995). Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: modulation of cathepsin B activity by neutrophil elastase. Archives of Biochemistry and Biophysics, 317(1), 305–310. https://doi.org/10.1006/abbi.1995.1167. 5.Akinyemi AO, Pereira GBS, Rocha FV. Role of Cathepsin B in Cancer Progression: A Potential Target for Coordination Compounds. Mini Rev Med Chem. 2021;21(13):1612-1624. doi: 10.2174/1389557521666210212152937. PMID: 33583372. |