Search by BoMiProt ID - Bomi298

Primary Information

BoMiProt ID Bomi298
Protein Name cAMP-dependent protein kinase catalytic subunit alpha
Organism Bos taurus
Uniprot IDP00517
Milk FractionExosome
Ref Sequence ID NP_777009.1
Aminoacid Length 351
Molecular Weight 40620
FASTA Sequence Download
Gene Name PRKACA
Gene ID 282322
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Protein Function cAMP exerts its effects in mammalian cells primarily through the activation of cAMP-dependent protein kinase (cAK),1 a tetrameric enzyme consisting of two catalytic (C) and two regulatory (R) subunits; important role in a wide range of cellular processes, including transcription, metabolism , cell cycle progression , apoptosis and hippocampal long term potentiation
Biochemical Properties comprised of two different types of subunits that can dissociate upon activation by cAMP; catalytic subunit of cAPK is comprised of a bilobal core that is shared by all members of the protein kinase superfamily; the conserved core is flanked by a 40-residue acylated and mostly helical motif at the N-terminus and by a 50-residue extended tail at the C-terminus that spans the surface of both core domains and is highly disordered near the end in the absence of ligands; Phosphoryl transfer for the catalytic subunit is extremely fast, greater than 500 s^-1;
Significance in milk A protein kinase activity fraction was defined in cytosols and membranes of mammary tissue isolated from rats during pregnancy lactation, and weaning; preferential substrate is casein
PTMs  Myristoyilation at Gly-2, Phosphorylation at Thr-198 and Ser-339
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
SCOP Class : Alpha and beta proteins (a+b)
Fold : Protein kinase-like (PK-like)
Superfamily : Protein kinase-like (PK-like)
Family : Protein kinases catalytic domain-like
Domain Name : 1XH8 A:14-350

CATH Matched CATH superfamily
Predicted Disorder Regions (1-33)
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Autophosphorylated. Phosphorylation is enhanced by vitamin K2. Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity.Phosphorylated at Tyr-331 by activated receptor tyrosine kinases EGFR and PDGFR; this increases catalytic efficiency.
PDB ID 1Q24, 1Q61, 1Q62, 1Q8T, 1Q8U, 1Q8W, 1SMH, 1STC, 1SVE, 1SVG, 1SVH, 1SZM, 1VEB, 1XH4, 1XH5, 1XH6, 1XH7, 1XH8, 1XH8, 1XH9, 1XHA, 1YDR, 1YDS, 1YDT, 2C1A, 2C1B, 2F7E, 2F7X, 2F7Z, 2GFC, 2GNF, 2GNG, 2GNH, 2GNI, 2GNJ, 2GNL, 2JDS, 2JDT, 2JDV, 2OH0, 2OJF, 2UVX, 2UVY, 2UVZ, 2UW0, 2UW3, 2UW4, 2UW5, 2UW6, 2UW7, 2UW8, 2UZT, 2UZU, 2UZV, 2UZW, 2VNW, 2VNY, 2VO0, 2VO3, 2VO6, 2VO7, 3AG9, 3BWJ, 3DND, 3DNE, 3E8C, 3E8E, 3KKV, 3ZO2, 3ZO3, 3ZO4, 4AXA, 4C33, 4C34, 4C35, 4C36, 4C37, 4C38, 4IE9, 4IJ9, 4YXR, 4YXS, 4Z83, 4Z,
Bibliography 1. Gamm, D. M., Baude, E. J. and Uhler, M. D. (1996) ‘The Major Catalytic Subunit Isoforms of cAMP-dependent Protein Kinase Have Distinct Biochemical Properties in Vitro and in Vivo’, Journal of Biological Chemistry, 271(26), pp. 15736–15742. doi: 10.1074/jbc.271.26.15736.
2. SHARONI, Y. et al. (1984) ‘Protein Kinase Activity in the Rat Mammary Gland during Pregnancy, Lactation, and Weaning: A Correlation with Growth but not with Progesterone Receptor Levels *’, Endocrinology, 115(5), pp. 1918–1924. doi: 10.1210/endo-115-5-1918. 3.Shoji S, Parmelee DC, Wade RD, Kumar S, Ericsson LH, Walsh KA, Neurath H, Long GL, Demaille JG, Fischer EH, Titani K. Complete amino acid sequence of the catalytic subunit of bovine cardiac muscle cyclic AMP-dependent protein kinase. Proc Natl Acad Sci U S A. 1981 Feb;78(2):848-51. doi: 10.1073/pnas.78.2.848. PMID: 6262777; PMCID: PMC319900.