ID   KAPCG_MACMU             Reviewed;         209 AA.
AC   O62846;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=cAMP-dependent protein kinase catalytic subunit gamma;
DE            Short=PKA C-gamma;
DE            EC=2.7.11.11;
DE   Flags: Fragment;
GN   Name=PRKACG;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9598317; DOI=10.1006/geno.1998.5240;
RA   Reinton N., Haugen T.B., Orstavik S., Skalhegg B.S., Hansson V.,
RA   Jahnsen T., Tasken K.;
RT   "The gene encoding the C gamma catalytic subunit of cAMP-dependent protein
RT   kinase is a transcribed retroposon.";
RL   Genomics 49:290-297(1998).
CC   -!- FUNCTION: Phosphorylates a large number of substrates in the cytoplasm
CC       and the nucleus.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.11;
CC   -!- ACTIVITY REGULATION: Activated by cAMP.
CC   -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced by
CC       the combination of homo- or heterodimers of the different regulatory
CC       subunits associated with two catalytic subunits. cAMP causes the
CC       dissociation of the inactive holoenzyme into a dimer of regulatory
CC       subunits bound to four cAMP and two free monomeric catalytic subunits.
CC   -!- TISSUE SPECIFICITY: Testis specific.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR   EMBL; AJ001927; CAA05098.1; -; Genomic_DNA.
DR   AlphaFoldDB; O62846; -.
DR   SMR; O62846; -.
DR   STRING; 9544.ENSMMUP00000026815; -.
DR   eggNOG; KOG0616; Eukaryota.
DR   HOGENOM; CLU_000288_63_5_1; -.
DR   InParanoid; O62846; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR039084; PKA_C-gamma.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24353:SF137; PTHR24353:SF137; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; cAMP; Kinase; Lipoprotein; Myristate; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..>209
FT                   /note="cAMP-dependent protein kinase catalytic subunit
FT                   gamma"
FT                   /id="PRO_0000086065"
FT   DOMAIN          43..>209
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         49..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         209
SQ   SEQUENCE   209 AA;  24096 MW;  9BAEB8B1363DD1A4 CRC64;
     MGNAAAKKDT EQETVNEFLA KARGDFLYRW GNPAQNTASS DQFERLKTLG TGSYGRVMLV
     RHRETGNHYA MKILDKQKVV RLKQVEHTLN EKRILQAINF PFLVKLQFSF KDNSNLYLVM
     EYVPGGEMFS HLRRVGRFSE PQACFYAAQV VLAFQYLHSL DLIHRDLKPE NLLIDQQGYL
     QVTDFGFAKR VKGRTWTLCG TPEYLAPEI