ID   KAPA_RAT       STANDARD;      PRT;   350 AA.
AC   P27791;
DT   01-AUG-1992 (Rel. 23, Created)
DT   01-AUG-1992 (Rel. 23, 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).
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=91274359; PubMed=1711374;
RA   Wiemann S., Voss H., Kinzel V., Pyerin W.;
RT   "Rat C alpha catalytic subunit of the cAMP-dependent protein kinase:
RT   cDNA sequence and evidence that it is the only isoform expressed in
RT   myoblasts.";
RL   Biochim. Biophys. Acta 1089:254-256(1991).
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; X57986; CAA41052.1; -.
DR   PIR; S16240; OKRT2C.
DR   HSSP; P05132; 1CTP.
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.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   LIPID         1      1       MYRISTATE (BY SIMILARITY).
FT   DOMAIN       43    297       PROTEIN KINASE.
FT   NP_BIND      49     57       ATP (BY SIMILARITY).
FT   BINDING      72     72       ATP (BY SIMILARITY).
FT   ACT_SITE    166    166       BY SIMILARITY.
FT   MOD_RES     197    197       PHOSPHORYLATION (BY SIMILARITY).
FT   MOD_RES     338    338       PHOSPHORYLATION (BY SIMILARITY).
SQ   SEQUENCE   350 AA;  40488 MW;  EDAC19F7FA9F35EF CRC64;
     GNAAAAKKGS EQESVKEFLA KAKEDFLKKW EDPSQNTAQL DHFDRIKTLG TGSFGRVMLV
     KHKESGNHYA 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 EKCGKEFTEF
//