Primary Information
BoMiProt ID	Bomi69
Protein Name	Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Organism	Bos taurus
Uniprot ID	P67774
Milk Fraction	Exosome
Ref Sequence ID	NP_851374.1
Aminoacid Length	309
Molecular Weight	35594
FASTA Sequence	Download
Gene Name	PPP2CA
Gene ID	282320
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Presence in other biological fluids/tissue/cells	PP2A is highly conserved from yeast to humans;
Protein Function	Protein phosphatase activities regulate cellular metabolism and are attributed to two types: type 1, namely PP1, and type 2, which consisted of three enzymes called PP2A, PP2B, and PP2C; PP2A plays an important role in development, cell proliferation and death, cell mobility, cytoskeleton dynamics, the control of the cell cycle, and the regulation of numerous signaling pathways; important tumor suppressor
Biochemical Properties	PP2A exists in two general forms—a heterodimeric core enzyme and a heterotrimeric holoenzyme; PP2A core enzyme consists of a scaffold subunit (also known as the A or PR65 subunit) and a catalytic subunit (C subunit); the scaffold and the catalytic subunits each have two isoforms, α and β, with the α isoform being about 10-fold more abundant than the β isoform; PP2A core enzyme interacts with a variable regulatory subunit to assemble into a holoenzyme; the catalytic subunit of PP2A is the primary target of a number of potent tumor-inducing toxins, such as okadaic acid (OA) and microcystin-LR; OA has an inhibitory constant of approximately 0.1 nM for the phosphatase activity of PP2A
Significance in milk	involved in oxytocin signalling pathway- might regulate mammary gland development
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	No TM helices
Linking IDs
Bibliography	1. Olsen, J. V, Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., & Mann, M. (2006). Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell, 127(3), 635–648. https://doi.org/10.1016/j.cell.2006.09.026. 2. MacKintosh, C., Beattie, K. A., Klumpp, S., Cohen, P., & Codd, G. A. (1990). Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. FEBS Letters, 264(2), 187–192. https://doi.org/10.1016/0014-5793(90)80245-e. 3. Ingebritsen, T. S., & Cohen, P. (1983). The Protein Phosphatases Involved in Cellular Regulation. Eur J Biochem, 132(2), 255–261.