ID   KAPG_HUMAN     STANDARD;      PRT;   350 AA.
AC   P22612;
DT   01-AUG-1991 (Rel. 19, Created)
DT   01-AUG-1991 (Rel. 19, Last sequence update)
DT   15-DEC-1998 (Rel. 37, Last annotation update)
DE   CAMP-DEPENDENT PROTEIN KINASE, GAMMA-CATALYTIC SUBUNIT (EC 2.7.1.37)
DE   (PKA C-GAMMA).
GN   PRKACG.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=TESTIS;
RX   MEDLINE=90258940; PubMed=2342480;
RA   Beebe S.J., Oyen O., Sandberg M., Froysa A., Hansson V., Jahnsen T.;
RT   "Molecular cloning of a tissue-specific protein kinase (C gamma) from
RT   human testis -- representing a third isoform for the catalytic subunit
RT   of cAMP-dependent protein kinase.";
RL   Mol. Endocrinol. 4:465-475(1990).
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   -!- TISSUE SPECIFICITY: TESTIS-SPECIFIC. BUT IMPORTANT TISSUES SUCH
CC       AS BRAIN AND OVARY HAVE NOT BEEN ANALYZED FOR THE CONTENT OF
CC       TRANSCRIPT.
CC   -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES.
CC       CAMP SUBFAMILY.
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DR   EMBL; M34182; AAC41690.1; ALT_INIT.
DR   PIR; B34724; OKHUCG.
DR   HSSP; P05132; 1CTP.
DR   MIM; 176893; -.
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
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 (AUTO-) (BY SIMILARITY).
FT   MOD_RES     338    338       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
SQ   SEQUENCE   350 AA;  40281 MW;  D0680191896DC484 CRC64;
     GNAPAKKDTE QEESVNEFLA KARGDFLYRW GNPAQNTASS DQFERLRTLG MGSFGRVMLV
     RHQETGGHYA MKILNKQKVV KMKQVEHILN EKRILQAIDF PFLVKLQFSF KDNSYLYLVM
     EYVPGGEMFS RLQRVGRFSE PHACFYAAQV VLAVQYLHSL DLIHRDLKPE NLLIDQQGYL
     QVTDFGFAKR VKGRTWTLCG TPEYLAPEII LSKGYNKAVD WWALGVLIYE MAVGFPPFYA
     DQPIQIYEKI VSGRVRFPSK LSSDLKDLLR SLLQVDLTKR FGNLRNGVGD IKNHKWFATT
     SWIAIYEKKV EAPFIPKYTG PGDASNFDDY EEEELRISIN EKCAKEFSEF
//