ID   KAPA_BOVIN     STANDARD;      PRT;   350 AA.
AC   P00517;
DT   21-JUL-1986 (Rel. 01, Created)
DT   01-FEB-1996 (Rel. 33, 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.
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea;
OC   Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=HEART;
RX   MEDLINE=93042013; PubMed=1420367;
RA   Wiemann S., Kinzel V., Pyerin W.;
RT   "Cloning of the C alpha catalytic subunit of the bovine cAMP-dependent
RT   protein kinase.";
RL   Biochim. Biophys. Acta 1171:93-96(1992).
RN   [2]
RP   SEQUENCE.
RX   MEDLINE=84000375; PubMed=6311252;
RA   Shoji S., Ericsson L.H., Walsh K.A., Fischer E.H., Titani K.;
RT   "Amino acid sequence of the catalytic subunit of bovine type II
RT   adenosine cyclic 3',5'-phosphate dependent protein kinase.";
RL   Biochemistry 22:3702-3709(1983).
RN   [3]
RP   SEQUENCE.
RX   MEDLINE=81199419; PubMed=6262777;
RA   Shoji S., Parmelee D.C., Wade R.D., Kumar S., Ericsson L.H.,
RA   Walsh K.A., Neurath H., Lonh G.L., Demaille J.G., Fischer E.H.,
RA   Titani K.;
RT   "Complete amino acid sequence of the catalytic subunit of bovine
RT   cardiac muscle cyclic AMP-dependent protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:848-851(1981).
RN   [4]
RP   SEQUENCE OF 195-213, AND ACTIVE SITE.
RX   MEDLINE=82265755; PubMed=6286662;
RA   Bramson H.N., Thomas N., Matsueda R., Nelson N.C., Taylor S.S.,
RA   Kaiser E.T.;
RT   "Modification of the catalytic subunit of bovine heart cAMP-dependent
RT   protein kinase with affinity labels related to peptide substrates.";
RL   J. Biol. Chem. 257:10575-10581(1982).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   MEDLINE=96421613; PubMed=8824261;
RA   Engh R.A., Girod A., Kinzel V., Huber R., Bossemeyer D.;
RT   "Crystal structures of catalytic subunit of cAMP-dependent protein
RT   kinase in complex with isoquinolinesulfonyl protein kinase inhibitors
RT   H7, H8, and H89. Structural implications for selectivity.";
RL   J. Biol. Chem. 271:26157-26164(1996).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   MEDLINE=98104090; PubMed=9438863;
RA   Prade L., Engh R.A., Girod A., Kinzel V., Huber R., Bossemeyer D.;
RT   "Staurosporine-induced conformational changes of cAMP-dependent
RT   protein kinase catalytic subunit explain inhibitory potential.";
RL   Structure 5:1627-1637(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.
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DR   EMBL; X67154; CAA47627.1; -.
DR   PIR; A00620; OKBO2C.
DR   PDB; 1YDR; 01-APR-97.
DR   PDB; 1YDS; 01-APR-97.
DR   PDB; 1YDT; 01-APR-97.
DR   PDB; 1STC; 25-FEB-98.
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; 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       BY SIMILARITY.
FT   ACT_SITE    199    199       CLOSE TO OR AT THE PEPTIDE SUBSTRATE
FT                                BINDING SITE.
FT   MOD_RES     197    197       PHOSPHORYLATION.
FT   MOD_RES     338    338       PHOSPHORYLATION.
FT   CONFLICT    201    201       T -> N (IN REF. 4).
FT   CONFLICT    203    203       E -> Q (IN REF. 4).
FT   CONFLICT    205    205       L -> S (IN REF. 4).
FT   CONFLICT    286    286       N -> D (IN REF. 2 AND 3).
SQ   SEQUENCE   350 AA;  40488 MW;  F31267005CEAF836 CRC64;
     GNAAAAKKGS EQESVKEFLA KAKEDFLKKW ENPAQNTAHL DQFERIKTLG TGSFGRVMLV
     KHMETGNHYA MKILDKQKVV KLKQIEHTLN EKRILQAVNF PFLVKLEFSF KDNSNLYMVM
     EYVPGGEMFS HLRRIGRFSE PHARFYAAQI VLTFEYLHSL DLIYRDLKPE NLLIDQQGYI
     QVTDFGFAKR VKGRTWTLCG TPEYLAPEII LSKGYNKAVD WWALGVLIYE MAAGYPPFFA
     DQPIQIYEKI VSGKVRFPSH FSSDLKDLLR NLLQVDLTKR FGNLKNGVND IKNHKWFATT
     DWIAIYQRKV EAPFIPKFKG PGDTSNFDDY EEEEIRVSIN EKCGKEFSEF
//