ID KAPA_MOUSE STANDARD; PRT; 350 AA. AC P05132; DT 13-AUG-1987 (Rel. 05, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT (EC 2.7.1.37) DE (PKA C-ALPHA). GN PRKACA OR PKACA. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88186891; PubMed=2833513; RA Chrivia J.C., Uhler M.D., McKnight G.S.; RT "Characterization of genomic clones coding for the C alpha and C beta RT subunits of mouse cAMP-dependent protein kinase."; RL J. Biol. Chem. 263:5739-5744(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=86149293; PubMed=3456589; RA Uhler M.D., Carmichael D.F., Lee D.C., Chrivia J.C., Krebs E.G., RA McKnight G.S.; RT "Isolation of cDNA clones coding for the catalytic subunit of mouse RT cAMP-dependent protein kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1300-1304(1986). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX MEDLINE=91320112; PubMed=1862342; RA Knighton D.R., Zheng J., ten Eyck L.F., Ashford V.A., Xuong N.-H., RA Taylor S.S., Sowadski J.M.; RT "Crystal structure of the catalytic subunit of cyclic adenosine RT monophosphate-dependent protein kinase."; RL Science 253:407-414(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH INHIBITOR. RX MEDLINE=97263736; PubMed=9109651; RA Narayana N., Cox S., Shaltiel S., Taylor S.S., Xuong N.; RT "Crystal structure of a polyhistidine-tagged recombinant catalytic RT subunit of cAMP-dependent protein kinase complexed with the peptide RT inhibitor PKI(5-24) and adenosine."; RL Biochemistry 36:4438-4448(1997). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=97411697; PubMed=9261084; RA Narayana N., Cox S., Nguyen-Huu X., ten Eyck L.F., Taylor S.S.; RT "A binary complex of the catalytic subunit of cAMP-dependent protein RT kinase and adenosine further defines conformational flexibility."; RL Structure 5:921-935(1997). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ENZYME REGULATION: THIS ENZYME IS ACTIVATED BY CAMP. CC -!- SUBUNIT: COMPOSED OF TWO REGULATORY CHAINS AND TWO CATALYTIC CC CHAINS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CAMP SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19960; AAA39937.1; -. DR EMBL; M18240; AAA39937.1; JOINED. DR EMBL; M18241; AAA39937.1; JOINED. DR EMBL; M19953; AAA39937.1; JOINED. DR EMBL; M19954; AAA39937.1; JOINED. DR EMBL; M19955; AAA39937.1; JOINED. DR EMBL; M19956; AAA39937.1; JOINED. DR EMBL; M19957; AAA39937.1; JOINED. DR EMBL; M19958; AAA39937.1; JOINED. DR EMBL; M19959; AAA39937.1; JOINED. DR EMBL; M12303; AAA39936.1; -. DR PIR; A28619; OKMSCA. DR PDB; 2CPK; 15-JAN-93. DR PDB; 1APM; 15-APR-93. DR PDB; 1ATP; 15-APR-93. DR PDB; 1CTP; 31-JAN-94. DR PDB; 1FMO; 14-JAN-98. DR PDB; 1BKX; 18-MAR-98. DR MGD; MGI:97592; Pkaca. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR000961; -. DR INTERPRO; IPR002290; -. DR PFAM; PF00069; pkinase; 1. DR PFAM; PF00433; pkinase_C; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; cAMP; KW Phosphorylation; Myristate; Multigene family; 3D-structure. FT INIT_MET 0 0 FT LIPID 1 1 MYRISTATE. FT DOMAIN 43 297 PROTEIN KINASE. FT NP_BIND 49 57 ATP. FT BINDING 72 72 ATP. FT ACT_SITE 166 166 FT MOD_RES 139 139 PHOSPHORYLATION. FT MOD_RES 197 197 PHOSPHORYLATION. FT MOD_RES 338 338 PHOSPHORYLATION. FT CONFLICT 32 32 T -> D (IN REF. 2). FT CONFLICT 286 286 N -> D (IN REF. 2). FT HELIX 8 31 FT HELIX 40 42 FT STRAND 43 50 FT STRAND 55 62 FT TURN 63 65 FT STRAND 68 75 FT HELIX 76 81 FT TURN 82 83 FT HELIX 85 95 FT TURN 96 97 FT TURN 101 102 FT STRAND 103 103 FT STRAND 106 111 FT STRAND 115 121 FT TURN 124 125 FT STRAND 127 127 FT HELIX 129 135 FT HELIX 140 159 FT TURN 160 161 FT STRAND 162 163 FT HELIX 169 171 FT STRAND 172 174 FT TURN 176 177 FT STRAND 180 182 FT STRAND 189 190 FT STRAND 195 195 FT HELIX 202 204 FT HELIX 207 210 FT TURN 211 212 FT STRAND 215 215 FT TURN 217 217 FT HELIX 218 233 FT HELIX 243 252 FT TURN 253 253 FT TURN 259 260 FT HELIX 263 272 FT TURN 277 279 FT TURN 281 283 FT TURN 285 288 FT HELIX 289 292 FT TURN 293 293 FT HELIX 295 297 FT TURN 298 299 FT HELIX 302 306 FT TURN 307 308 FT TURN 344 349 SQ SEQUENCE 350 AA; 40439 MW; A837E8416515B791 CRC64; GNAAAAKKGS EQESVKEFLA KAKEDFLKKW ETPSQNTAQL DQFDRIKTLG TGSFGRVMLV KHKESGNHYA MKILDKQKVV KLKQIEHTLN EKRILQAVNF PFLVKLEFSF KDNSNLYMVM EYVAGGEMFS HLRRIGRFSE PHARFYAAQI VLTFEYLHSL DLIYRDLKPE NLLIDQQGYI QVTDFGFAKR VKGRTWTLCG TPEYLAPEII LSKGYNKAVD WWALGVLIYE MAAGYPPFFA DQPIQIYEKI VSGKVRFPSH FSSDLKDLLR NLLQVDLTKR FGNLKNGVND IKNHKWFATT DWIAIYQRKV EAPFIPKFKG PGDTSNFDDY EEEEIRVSIN EKCGKEFTEF //