ID KAP2_BOVIN Reviewed; 401 AA. AC P00515; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 2. DT 24-NOV-2009, entry version 91. DE RecName: Full=cAMP-dependent protein kinase type II-alpha regulatory subunit; GN Name=PRKAR2A; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE OF 2-401. RC TISSUE=Heart muscle; RX MEDLINE=82222175; PubMed=6283532; DOI=10.1073/pnas.79.8.2544; RA Takio K., Smith S.B., Krebs E.G., Walsh K.A., Titani K.; RT "Primary structure of the regulatory subunit of type II cAMP-dependent RT protein kinase from bovine cardiac muscle."; RL Proc. Natl. Acad. Sci. U.S.A. 79:2544-2548(1982). RN [2] RP PROTEIN SEQUENCE OF 155-166, AND PHOSPHORYLATION AT THR-212. RX PubMed=1654846; DOI=10.1016/0003-9861(91)90460-Z; RA Braun R.K., Vulliet P.R., Carbonaro-Hall D.A., Hall F.L.; RT "Phosphorylation of RII subunit and attenuation of cAMP-dependent RT protein kinase activity by proline-directed protein kinase."; RL Arch. Biochem. Biophys. 289:187-191(1991). RN [3] RP 3D-STRUCTURE MODELING. RX MEDLINE=87157645; PubMed=3030405; DOI=10.1021/bi00376a003; RA Weber I.T., Steitz T.A., Bubis J., Taylor S.S.; RT "Predicted structures of cAMP binding domains of type I and II RT regulatory subunits of cAMP-dependent protein kinase."; RL Biochemistry 26:343-351(1987). 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 AKAP4 and CBFA2T3 (By CC similarity). 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: A second phosphorylation site has not been located. CC -!- PTM: Phosphorylation of Thr-212 by PDPK seems to attenuate the CC activity of PKA, perhaps by strengthening interaction between the CC regulatory and the catalytic subunits. CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain CC family. CC -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR IPI; IPI00693176; -. DR PIR; A00618; OKBO2R. DR RefSeq; XP_001790337.1; -. DR UniGene; Bt.95129; -. DR PDB; 2APK; Model; -; A=2-401. DR PDB; 2BPK; Model; -; A=2-401. DR PDBsum; 2APK; -. DR PDBsum; 2BPK; -. DR SMR; P00515; 114-397. DR DIP; DIP:546N; -. DR STRING; P00515; -. DR Ensembl; ENSBTAT00000018886; ENSBTAP00000018886; ENSBTAG00000014205; Bos taurus. DR GeneID; 100139910; -. DR KEGG; bta:100139910; -. DR CTD; 100139910; -. DR HOVERGEN; P00515; -. DR OMA; DQQRCRL; -. DR OrthoDB; EOG9909VX; -. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro. DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW. DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator act...; IEA:InterPro. DR GO; GO:0001932; P:regulation of protein amino acid phosphoryl...; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR003117; cAMP-dep_prot_kin_reg_I/II_a/b. DR InterPro; IPR002373; cAMP/cGMP_kin. DR InterPro; IPR000595; cNMP_bd. DR InterPro; IPR018490; cNMP_bd-like. DR InterPro; IPR018488; cNMP_bd_CS. DR InterPro; IPR012198; PK_regulatory. DR InterPro; IPR014710; RmlC-like_jellyroll. DR Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF02197; RIIa; 1. DR PIRSF; PIRSF000548; PK_regulatory; 1. DR PRINTS; PR00103; CAMPKINASE. DR SMART; SM00100; cNMP; 2. DR SMART; SM00394; RIIa; 1. 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; Acetylation; cAMP; cAMP-binding; KW Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Repeat. FT INIT_MET 1 1 Removed. FT CHAIN 2 401 cAMP-dependent protein kinase type II- FT alpha regulatory subunit. FT /FTId=PRO_0000205384. FT NP_BIND 136 257 cAMP 1. FT NP_BIND 258 401 cAMP 2. FT REGION 2 135 Dimerization and phosphorylation. FT BINDING 205 205 cAMP 1. FT BINDING 214 214 cAMP 1. FT BINDING 335 335 cAMP 2. FT BINDING 344 344 cAMP 2. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 75 75 Phosphoserine (By similarity). FT MOD_RES 77 77 Phosphoserine (By similarity). FT MOD_RES 96 96 Phosphoserine; by PKA (By similarity). FT MOD_RES 212 212 Phosphothreonine; by PDPK. FT HELIX 144 149 FT STRAND 154 156 FT STRAND 176 184 FT STRAND 187 189 FT STRAND 192 200 FT STRAND 207 210 FT STRAND 214 217 FT STRAND 223 225 FT HELIX 230 236 FT TURN 237 239 FT HELIX 242 263 SQ SEQUENCE 401 AA; 45094 MW; 8FEA32E5B39A545A CRC64; MSHIQIPPGL TELLQGYTVE VLRQRPPDLV DFAVDYFTRL REARSRASTP PAAPPSGSQD FDPGAGLVAD AVADSESEDE EDLDVPIPGR FDRRVSVCAE TYNPDEEEED TDPRVIHPKT DQQRCRLQEA CKDILLFKNL DPEQLSQVLD AMFERTVKVD EHVIDQGDDG DNFYVIERGT YDILVTKDNQ TRSVGQYDNH GSFGELALMY NTPRAATIVA TSEGSLWGLD RVTFRRIIVK NNAKKRKMFE SFIESVPLLK SLEVSERMKI VDVIGEKVYK DGERIITQGE KADSFYIIES GEVSILIKSK TKVNKDGENQ EVEIARCHKG QYFGELALVT NKPRAASAYA VGDVKCLVMD VQAFERLLGP CMDIMKRNIS HYEEQLVKMF GSSMDLIDPG Q //