ID KAP3_MOUSE Reviewed; 416 AA. AC P31324; B1B199; Q3UTZ1; Q80ZM4; Q8BRZ7; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 14-OCT-2015, entry version 141. DE RecName: Full=cAMP-dependent protein kinase type II-beta regulatory subunit; GN Name=Prkar2b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100. RX PubMed=2069562; DOI=10.1016/0006-291X(91)91802-J; RA Singh I.S., Luo Z., Eng A., Erlichman J.; RT "Molecular cloning and characterization of the promoter region of the RT mouse regulatory subunit RII beta of type II cAMP-dependent protein RT kinase."; RL Biochem. Biophys. Res. Commun. 178:221-226(1991). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of RT electron capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-112, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH PRKACA, AND RP SUBUNIT. RX PubMed=22323819; DOI=10.1126/science.1213979; RA Zhang P., Smith-Nguyen E.V., Keshwani M.M., Deal M.S., Kornev A.P., RA Taylor S.S.; RT "Structure and allostery of the PKA RIIbeta tetrameric holoenzyme."; RL Science 335:712-716(2012). CC -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases CC involved in cAMP signaling in cells. Type II regulatory chains CC mediate membrane association by binding to anchoring proteins, CC including the MAP2 kinase. CC -!- SUBUNIT: The inactive form of the enzyme is composed of two CC regulatory chains and two catalytic chains. Activation by cAMP CC produces two active catalytic monomers and a regulatory dimer that CC binds four cAMP molecules. Interacts with the phosphorylated form CC of PJA2 (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q5S006:Lrrk2; NbExp=3; IntAct=EBI-455340, EBI-2693710; CC P05132:Prkaca; NbExp=3; IntAct=EBI-455340, EBI-400564; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane CC {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and at CC the cell membrane. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I- CC alpha, I-beta, II-alpha, and II-beta. Their expression varies CC among tissues and is in some cases constitutive and in others CC inducible. CC -!- PTM: Phosphorylated by the activated catalytic chain. CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains. CC {ECO:0000255|PROSITE-ProRule:PRU00060}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK041013; BAC30779.1; -; mRNA. DR EMBL; AK138963; BAE23838.1; -; mRNA. DR EMBL; CT010463; CAM17140.1; -; Genomic_DNA. DR EMBL; BC048710; AAH48710.1; -; mRNA. DR EMBL; M68861; AAA40057.1; -; Genomic_DNA. DR CCDS; CCDS25869.1; -. DR PIR; PQ0161; PQ0161. DR RefSeq; NP_035288.2; NM_011158.3. DR RefSeq; XP_006515077.1; XM_006515014.2. DR UniGene; Mm.25594; -. DR PDB; 3TNP; X-ray; 2.30 A; B/E=1-416. DR PDB; 3TNQ; X-ray; 3.10 A; A=1-416. DR PDB; 4WBB; X-ray; 2.80 A; A=1-416. DR PDB; 4X6Q; X-ray; 2.52 A; B=1-416. DR PDBsum; 3TNP; -. DR PDBsum; 3TNQ; -. DR PDBsum; 4WBB; -. DR PDBsum; 4X6Q; -. DR ProteinModelPortal; P31324; -. DR SMR; P31324; 8-408. DR BioGrid; 202369; 5. DR DIP; DIP-31571N; -. DR IntAct; P31324; 11. DR MINT; MINT-4099351; -. DR STRING; 10090.ENSMUSP00000003079; -. DR PhosphoSite; P31324; -. DR MaxQB; P31324; -. DR PaxDb; P31324; -. DR PRIDE; P31324; -. DR Ensembl; ENSMUST00000003079; ENSMUSP00000003079; ENSMUSG00000002997. DR Ensembl; ENSMUST00000036497; ENSMUSP00000039797; ENSMUSG00000002997. DR GeneID; 19088; -. DR KEGG; mmu:19088; -. DR UCSC; uc007nhx.2; mouse. DR CTD; 5577; -. DR MGI; MGI:97760; Prkar2b. DR eggNOG; COG0664; -. DR GeneTree; ENSGT00530000062947; -. DR HOGENOM; HOG000196668; -. DR HOVERGEN; HBG002025; -. DR InParanoid; P31324; -. DR KO; K04739; -. DR OMA; KCAVLDV; -. DR OrthoDB; EOG76T9RR; -. DR PhylomeDB; P31324; -. DR TreeFam; TF314920; -. DR Reactome; R-MMU-163615; PKA activation. DR Reactome; R-MMU-164378; PKA activation in glucagon signalling. DR Reactome; R-MMU-180024; DARPP-32 events. DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-MMU-5610787; Hedgehog 'off' state. DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR ChiTaRS; Prkar2b; mouse. DR NextBio; 295636; -. DR PRO; PR:P31324; -. DR Proteomes; UP000000589; Chromosome 12. DR Bgee; P31324; -. DR ExpressionAtlas; P31324; baseline and differential. DR Genevisible; P31324; MM. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0097546; C:ciliary base; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0043198; C:dendritic shaft; IDA:ParkinsonsUK-UCL. DR GO; GO:0043197; C:dendritic spine; IDA:ParkinsonsUK-UCL. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0045121; C:membrane raft; IEA:Ensembl. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW. DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; ISO:MGI. DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:MGI. DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI. DR GO; GO:0007612; P:learning; IMP:MGI. DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; ISO:MGI. DR GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl. DR GO; GO:0097338; P:response to clozapine; IEA:Ensembl. DR Gene3D; 2.60.120.10; -; 2. DR InterPro; IPR012198; cAMP_dep_PK_reg_su. DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b. DR InterPro; IPR018490; cNMP-bd-like. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR014710; RmlC-like_jellyroll. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF02197; RIIa; 1. DR PIRSF; PIRSF000548; PK_regulatory; 1. DR SMART; SM00100; cNMP; 2. DR SMART; SM00394; RIIa; 1. DR SUPFAM; SSF47391; SSF47391; 1. DR SUPFAM; SSF51206; SSF51206; 2. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. PE 1: Evidence at protein level; KW 3D-structure; cAMP; cAMP-binding; Cell membrane; Complete proteome; KW Cytoplasm; Membrane; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat. FT CHAIN 1 416 cAMP-dependent protein kinase type II- FT beta regulatory subunit. FT /FTId=PRO_0000205391. FT NP_BIND 152 273 cAMP 1. FT NP_BIND 274 416 cAMP 2. FT REGION 1 151 Dimerization and phosphorylation. FT BINDING 221 221 cAMP 1. {ECO:0000250}. FT BINDING 230 230 cAMP 1. {ECO:0000250}. FT BINDING 350 350 cAMP 2. {ECO:0000250}. FT BINDING 359 359 cAMP 2. {ECO:0000250}. FT MOD_RES 83 83 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 85 85 Phosphoserine. FT {ECO:0000250|UniProtKB:P31323}. FT MOD_RES 112 112 Phosphoserine. FT {ECO:0000244|PubMed:16452087, FT ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:19131326, FT ECO:0000244|PubMed:21183079}. FT CONFLICT 69 69 I -> T (in Ref. 3; AAH48710). FT {ECO:0000305}. FT HELIX 137 147 {ECO:0000244|PDB:3TNP}. FT HELIX 151 154 {ECO:0000244|PDB:3TNP}. FT HELIX 158 167 {ECO:0000244|PDB:3TNP}. FT STRAND 169 173 {ECO:0000244|PDB:3TNP}. FT STRAND 178 180 {ECO:0000244|PDB:3TNP}. FT STRAND 188 194 {ECO:0000244|PDB:3TNP}. FT STRAND 196 202 {ECO:0000244|PDB:3TNP}. FT STRAND 207 215 {ECO:0000244|PDB:3TNP}. FT HELIX 221 224 {ECO:0000244|PDB:3TNP}. FT STRAND 231 246 {ECO:0000244|PDB:3TNP}. FT HELIX 247 261 {ECO:0000244|PDB:3TNP}. FT STRAND 262 268 {ECO:0000244|PDB:3TNP}. FT HELIX 269 271 {ECO:0000244|PDB:3TNP}. FT HELIX 273 275 {ECO:0000244|PDB:3TNP}. FT HELIX 280 289 {ECO:0000244|PDB:3TNP}. FT STRAND 291 295 {ECO:0000244|PDB:3TNP}. FT STRAND 300 302 {ECO:0000244|PDB:3TNP}. FT STRAND 310 322 {ECO:0000244|PDB:3TNP}. FT STRAND 338 342 {ECO:0000244|PDB:3TNP}. FT STRAND 347 349 {ECO:0000244|PDB:3TNP}. FT HELIX 350 353 {ECO:0000244|PDB:3TNP}. FT STRAND 360 375 {ECO:0000244|PDB:3TNP}. FT HELIX 376 383 {ECO:0000244|PDB:3TNP}. FT HELIX 386 390 {ECO:0000244|PDB:3TNP}. SQ SEQUENCE 416 AA; 46167 MW; 24196C3037789827 CRC64; MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR FGHEGRTWGD AGAAAGGGIP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN APVINRFTRR ASVCAEAYNP DEEEDDAESR IIHPKTDDQR NRLQEACKDI LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI DQGDDGDNFY VIDRGTFDIY VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG ALWGLDRVTF RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ IIAQGDLADS FFIVESGEVK ITMKRKGKSE VEENGAVEIA RCFRGQYFGE LALVTNKPRA ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ LVALFGTNMD IVEPTA //