Search by BoMiProt ID - Bomi49


Primary Information

BoMiProt ID Bomi49
Protein Name Caspase 3
Organism Bos taurus
Uniprot IdQ08DY9
Milk FractionExosome
Ref Sequence Id NP_001071308.1
Amino Acid Lenth 275
Molecular Weight 31136
Fasta Sequence https://www.uniprot.org/uniprot/Q08DY9.fasta
Gene Name CASP3
Gene Id 408016
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondry Information

Protein Function Caspases are members of cysteinyl dependent aspartate directed proteases family which plays essential roles in regulating apoptosis at cellular level, and finally causes cellular demise through a cascade of molecular events; involved in disassembly of the cells into apoptotic bodies during apoptosis; member of the apoptosis executioner group
Biochemical Properties intracellular proteases; activation is also appears to be associated with the increased mitochondrial transmembrane potential; Optimal pH for caspase-3 is 7.4; activity is relatively stable between 0 and 150 mM NaCl; caspases lose over 40% of their activity upon removal of CHAPS from the buffer, and the effect is more dramatic with caspase-6 than with caspases-3; active over a broader pH range with an optimum slightly higher than the other caspases; there is a faster than expected drop-off in activity at low pH, most clearly observed with caspases-3 and -6
Significance in milk PMNs isolated from milk of mastitic cows showed revealing activities of caspase-3 which indicated that the milk PMNs undergo induced apoptosis and the process is programmed via the activation of initiator and executioner caspases
PTMs phosphorylation at the highly conserved position S150; PKCd phosphorylates caspase-3 at S26; DEVD phosphorylates at the +3 (P3) position
Significance of PTMs negatively controlled by p38 MAPK in neutrophils via phosphorylation at the highly conserved position S150; PKCd enhances caspase-3 activity and increase apoptotic cell death; DEVD promotes proteolysis of procaspase-3 by caspase-8 , demonstrating a functional significance of caspase-3 activation through phosphorylation for the execution step of apoptosis
Linking IDs Bomi648
Bibliography 1. Swain, D. K., Kushwah, M. S., Kaur, M., & Dang, A. K. (2015). Elucidation of Molecular Basis of Neutrophil Apoptosis during Staphylococcal Mastitis in Crossbred Cows . Journal of Animal Research, 5(1), 53. https://doi.org/10.5958/2277-940x.2015.00009.1.
2. Jolivel, V., Arthaud, S., Botia, B., Portal, C., Delest, B., Clavé, G., … Vaudry, D. (2014). Biochemical characterization of a Caspase-3 far-red fluorescent probe for non-invasive optical imaging of neuronal apoptosis. Journal of Molecular Neuroscience : MN, 54(3), 451–462. https://doi.org/10.1007/s12031-014-0325-4.
3. Alvarado-Kristensson, M., & Andersson, T. (2005). Protein phosphatase 2A regulates apoptosis in neutrophils by dephosphorylating both p38 MAPK and its substrate caspase 3. The Journal of Biological Chemistry, 280(7), 6238–6244. https://doi.org/10.1074/jbc.M409718200.
4. Alvarado-Kristensson, M., Melander, F., Leandersson, K., Rönnstrand, L., Wernstedt, C., & Andersson, T. (2004). p38-MAPK Signals Survival by Phosphorylation of Caspase-8 and Caspase-3 in Human Neutrophils. Journal of Experimental Medicine, 199(4), 449–458. https://doi.org/10.1084/jem.20031771.