Search by BoMiProt ID - Bomi48

Primary Information

BoMiProt ID Bomi48
Protein Name Calpain-1 catalytic subunit
Organism Bos taurus
Uniprot IdQ27970
Milk FractionMFGM, Exosome
Ref Sequence Id NP_776684.1
Amino Acid Lenth 716
Molecular Weight 82207
Fasta Sequence
Gene Name CAPN1
Gene Id 281661
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry Information

Protein Function receptor functioning , activation of enzymes , organization of cytoskeletal proteins , and myofibrillar protein turnover; involved in lysosomal rupture and the resultant release of lysosomal cathepsins into the cytoplasm during neuronal cell death; hydrophobic feature it has an important role in the membrane anchoring; Calpastatin, the ubiquitously expressed endogenous calpain inhibitor, blocks both calpain 1 and 2 with similar efficiency and does not inhibit any other protease
Biochemical Properties family of Ca2+-activated neutral thiol endopeptidases classified as tissue-specific; active at micromolar [Ca2+] concentrations; composed of 80-kDa catalytic subunits, which are products of separate genes, and a 30-kDa regulatory subunit; contains 19 amino acid residues that can be cleaved by autolysis during activation
Significance in milk responsible for mitochondrial and lysosomal membrane permeabilization during mammary gland involution
PTMs Phosphorylation - nine phosphorylated residues were identified in calpain 1
Linking IDs Bomi639
Bibliography 1. Suzuki, K., Imajoh, S., Emori, Y., Kawasaki, H., Minami, Y., & Ohno, S. (1987). Calcium-activated neutral protease and its endogenous inhibitor. Activation at the cell membrane and biological function. FEBS Letters, 220(2), 271–277.
2. Shiraha, H., Glading, A., Chou, J., Jia, Z., & Wells, A. (2002). Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain. Molecular and Cellular Biology, 22(8), 2716–2727.
3. Smith, S. D., Jia, Z., Huynh, K. K., Wells, A., & Elce, J. S. (2003). Glutamate substitutions at a PKA consensus site are consistent with inactivation of calpain by phosphorylation. FEBS Letters, 542(1–3), 115–118.
4. Zadran, S., Jourdi, H., Rostamiani, K., Qin, Q., Bi, X., & Baudry, M. (2010). Brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation. The Journal of Neuroscience : The Official Journal of the Society for Neuroscience, 30(3), 1086–1095.
5. Glading, A., Bodnar, R. J., Reynolds, I. J., Shiraha, H., Satish, L., Potter, D. A., … Wells, A. (2004). Epidermal growth factor activates m-calpain (calpain II), at least in part, by extracellular signal-regulated kinase-mediated phosphorylation. Molecular and Cellular Biology, 24(6), 2499–2512.
6. Imajoh, S., Kawasaki, H., & Suzuki, K. (1986). The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol. Journal of Biochemistry, 99(4), 1281–1284.
7. Hosfield, C. M. (1999). Crystal structure of calpain reveals the structural basis for Ca2+-dependent protease activity and a novel mode of enzyme activation. The EMBO Journal, 18(24), 6880–6889.
8. Strobl, S., Fernandez-Catalan, C., Braun, M., Huber, R., Masumoto, H., Nakagawa, K., … Bode, W. (2000). The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proceedings of the National Academy of Sciences of the United States of America, 97(2), 588–592.
9. Ilian, M. A., Gilmour, R. S., & Bickerstaffe, R. (1999). Quantification of ovine and bovine calpain I, calpain II, and calpastatin mRNA by ribonuclease protection assay. Journal of Animal Science, 77(4), 853–864.
10. Arnandis, T., Ferrer-Vicens, I., García-Trevijano, E. R., Miralles, V. J., García, C., Torres, L., … Zaragozá, R. (2012). Calpains mediate epithelial-cell death during mammary gland involution: mitochondria and lysosomal destabilization. Cell Death and Differentiation, 19(9), 1536–1548.