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Primary Information | |
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| BoMiProt ID | Bomi297 |
| Protein Name | cAMP-dependent protein kinase type II-alpha regulatory subunit |
| Organism | Bos taurus |
| Uniprot ID | P00515 |
| Milk Fraction | Exosome |
| Ref Sequence ID | NP_001178296.1 |
| Aminoacid Length | 401 |
| Molecular Weight | 45094 |
| FASTA Sequence | Download |
| Gene Name | PRKAR2A |
| Gene ID | 100139910 |
| Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
| Protein Function | the R subunits function as adapters that link the catalytic moiety via a dimerization/docking (D/D) domain to scaffold proteins termed A-kinase anchoring proteins (AKAPs); 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 | modular, multifunctional, and very stable; At the N-terminus is a D/D domain that maintains the protomer as a dimer and provides an anchoring surface on which the AKAPs dock; have no covalent bonds connecting the monomeric elements of the homodimer |
| 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 | Phosphoryaletd: linker regions contain multiple phosphorylation sites including an autophosphorylation site; site for ubiquitination; phosphorylatable Ser in their consensus recognition sequence, and this site is autophosphorylated in the holoenzyme complex |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P00515|KAP2_BOVIN cAMP-dependent protein kinase type II-alpha regulatory subunit OS=Bos taurus OX=9913 GN=PRKAR2A PE=1 SV=2 MSHIQIPPGLTELLQGYTVEVLRQRPPDLVDFAVDYFTRLREARSRASTPPAAPPSGSQD FDPGAGLVADAVADSESEDEEDLDVPIPGRFDRRVSVCAETYNPDEEEEDTDPRVIHPKT DQQRCRLQEACKDILLFKNLDPEQLSQVLDAMFERTVKVDEHVIDQGDDGDNFYVIERGT YDILVTKDNQTRSVGQYDNHGSFGELALMYNT*212PRAATIVATSEGSLWGLDRVTFRRIIVK NNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKVYKDGERIITQGEKADSFYIIES GEVSILIKSKTKVNKDGENQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMD VQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSMDLIDPGQ |
| CATH | Matched CATH superfamily n/a |
| Predicted Disorder Regions | 1-4,40-120 |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| PDB ID | 2APK, 2BPK, |
| 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. |