Search by BoMiProt ID - Bomi297


Primary Information

BoMiProt ID Bomi297
Protein Name cAMP-dependent protein kinase type II-alpha regulatory subunit
Organism Bos taurus
Uniprot IdP00515
Milk FractionExosome
Ref Sequence Id NP_001178296.1
Amino Acid Lenth 401
Molecular Weight 45094
Fasta Sequence https://www.uniprot.org/uniprot/P00515.fasta
Gene Name PRKAR2A
Gene Id 100139910
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry 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
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.