Search by BoMiProt ID - Bomi117

Primary Information

BoMiProt ID Bomi117
Protein Name Cathepsin L1
Organism Bos taurus
Uniprot IDP25975
Milk FractionWhey
Ref Sequence ID NP_776457.1
Aminoacid Length 334
Molecular Weight 37347
FASTA Sequence Download
Gene Name CTSL
Gene ID 281108
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells Ubiquitously expressed, highly expressed in osteoclasts;
Protein Function regulation of cell-cycle progression; proteolytic processing of the N-terminus of the histone H3 tail; cleaves elastin; special role in bone resorption under normal and pathological conditions
Biochemical Properties interact with the histones H2A.Z, H2B, H3 and the protease inhibitor stefin B; optimally active in a slightly acidic pH and are mostly unstable at neutral pH; cathepsin L, the most unstable of the cathepsins at neutral pH; GAGs potentially inhibit the collagenase activity of cathepsins L
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Bibliography 1. Turk, B., Dolenc, I., Turk, V., & Bieth, J. G. (1993). Kinetics of the pH-induced inactivation of human cathepsin L. Biochemistry, 32(1), 375–380. https://doi.org/10.1021/bi00052a046.
2. Yasuda, Y., Li, Z., Greenbaum, D., Bogyo, M., Weber, E., & Brömme, D. (2004). Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. The Journal of Biological Chemistry, 279(35), 36761–36770. https://doi.org/10.1074/jbc.M403986200.
3. Brömme, D., Okamoto, K., Wang, B. B., & Biroc, S. (1996). Human cathepsin O2, a matrix protein-degrading cysteine protease expressed in osteoclasts. Functional expression of human cathepsin O2 in Spodoptera frugiperda and characterization of the enzyme. The Journal of Biological Chemistry, 271(4), 2126–2132. https://doi.org/10.1074/jbc.271.4.2126.
4. Drake, F. H., Dodds, R. A., James, I. E., Connor, J. R., Debouck, C., Richardson, S., … Gowen, M. (1996). Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts. The Journal of Biological Chemistry, 271(21), 12511–12516. https://doi.org/10.1074/jbc.271.21.12511.
5. Goulet, B., Baruch, A., Moon, N.-S., Poirier, M., Sansregret, L. L., Erickson, A., … Nepveu, A. (2004). A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Molecular Cell, 14(2), 207–219. https://doi.org/10.1016/s1097-2765(04)00209-6.
6. Duncan, E. M., Muratore-Schroeder, T. L., Cook, R. G., Garcia, B. A., Shabanowitz, J., Hunt, D. F., & Allis, C. D. (2008). Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation. Cell, 135(2), 284–294. https://doi.org/10.1016/j.cell.2008.09.055.
7. Ceru, S., Konjar, S., Maher, K., Repnik, U., Krizaj, I., Bencina, M., … Kopitar-Jerala, N. (2010). Stefin B interacts with histones and cathepsin L in the nucleus. The Journal of Biological Chemistry, 285(13), 10078–10086. https://doi.org/10.1074/jbc.M109.034793.