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cAMP-dependent protein kinase catalytic subunit (PKA C) (EC 2.7.11.11)

 KAPC_DROME              Reviewed;         353 AA.
P12370; A4V0I0; Q9VL99;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 186.
RecName: Full=cAMP-dependent protein kinase catalytic subunit;
Short=PKA C;
EC=2.7.11.11 {ECO:0000305|PubMed:29473541};
Name=Pka-C1; Synonyms=CdkA, DC0; ORFNames=CG4379;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2828348;
Foster J.L., Higgins G.C., Jackson R.F.;
"Cloning, sequence, and expression of the Drosophila cAMP-dependent
protein kinase catalytic subunit gene.";
J. Biol. Chem. 263:1676-1681(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Canton-S;
PubMed=3215511; DOI=10.1101/gad.2.12a.1539;
Kalderon D., Rubin G.M.;
"Isolation and characterization of Drosophila cAMP-dependent protein
kinase genes.";
Genes Dev. 2:1539-1556(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=29473541; DOI=10.7554/eLife.33007;
Lee P.T., Lin G., Lin W.W., Diao F., White B.H., Bellen H.J.;
"A kinase-dependent feedforward loop affects CREBB stability and long
term memory formation.";
Elife 7:0-0(2018).
-!- FUNCTION: Serine/threonine-protein kinase involved in memory
formation. Promotes long-term memory by phosphorylating meng and
by regulating CrebB protein stability and activity.
{ECO:0000269|PubMed:29473541}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000305|PubMed:29473541}.
-!- ENZYME REGULATION: Activated by cAMP.
-!- SUBUNIT: Composed of two regulatory chains and two catalytic
chains.
-!- INTERACTION:
Q9VT65:CalpB; NbExp=2; IntAct=EBI-82224, EBI-132069;
Q03720:slo; NbExp=5; IntAct=EBI-82224, EBI-426805;
-!- TISSUE SPECIFICITY: More abundant in adult head than adult body.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. cAMP subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M18655; AAA28412.1; -; Genomic_DNA.
EMBL; X16969; CAA34840.1; -; Genomic_DNA.
EMBL; AE014134; AAF52797.1; -; Genomic_DNA.
EMBL; AE014134; AAN10703.1; -; Genomic_DNA.
EMBL; AE014134; AAS64669.1; -; Genomic_DNA.
EMBL; AY069425; AAL39570.1; -; mRNA.
PIR; C31751; C31751.
RefSeq; NP_476977.1; NM_057629.4.
RefSeq; NP_723479.1; NM_164866.3.
RefSeq; NP_995672.1; NM_205950.3.
UniGene; Dm.2136; -.
ProteinModelPortal; P12370; -.
SMR; P12370; -.
BioGrid; 60383; 21.
DIP; DIP-23727N; -.
IntAct; P12370; 7.
MINT; P12370; -.
STRING; 7227.FBpp0079448; -.
PaxDb; P12370; -.
PRIDE; P12370; -.
EnsemblMetazoa; FBtr0079851; FBpp0079448; FBgn0000273.
EnsemblMetazoa; FBtr0079852; FBpp0089382; FBgn0000273.
EnsemblMetazoa; FBtr0335495; FBpp0307466; FBgn0000273.
GeneID; 34284; -.
KEGG; dme:Dmel_CG4379; -.
UCSC; CG4379-RB; d. melanogaster.
CTD; 34284; -.
FlyBase; FBgn0000273; Pka-C1.
eggNOG; KOG0616; Eukaryota.
eggNOG; ENOG410XPQQ; LUCA.
GeneTree; ENSGT00810000125385; -.
InParanoid; P12370; -.
KO; K04345; -.
OMA; GQHFAMK; -.
OrthoDB; EOG091G10O8; -.
PhylomeDB; P12370; -.
BRENDA; 2.7.11.11; 1994.
Reactome; R-DME-163615; PKA activation.
Reactome; R-DME-164378; PKA activation in glucagon signalling.
Reactome; R-DME-180024; DARPP-32 events.
Reactome; R-DME-209159; Assembly of the CI containing complexes.
Reactome; R-DME-209190; Phosphorylation of CI.
Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
Reactome; R-DME-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-DME-392517; Rap1 signalling.
Reactome; R-DME-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-DME-442720; CREB phosphorylation through the activation of Adenylate Cyclase.
Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-DME-5610787; Hedgehog 'off' state.
Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
SignaLink; P12370; -.
GenomeRNAi; 34284; -.
PRO; PR:P12370; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0000273; -.
Genevisible; P12370; DM.
GO; GO:0044297; C:cell body; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
GO; GO:0007615; P:anesthesia-resistant memory; IMP:FlyBase.
GO; GO:0007448; P:anterior/posterior pattern specification, imaginal disc; IMP:FlyBase.
GO; GO:0048149; P:behavioral response to ethanol; TAS:FlyBase.
GO; GO:0019933; P:cAMP-mediated signaling; TAS:FlyBase.
GO; GO:0048749; P:compound eye development; NAS:FlyBase.
GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; NAS:FlyBase.
GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0007612; P:learning; NAS:FlyBase.
GO; GO:0007611; P:learning or memory; NAS:FlyBase.
GO; GO:0045475; P:locomotor rhythm; NAS:FlyBase.
GO; GO:0007613; P:memory; NAS:FlyBase.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:FlyBase.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:FlyBase.
GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0007228; P:positive regulation of hh target transcription factor activity; IMP:FlyBase.
GO; GO:0006468; P:protein phosphorylation; IMP:FlyBase.
GO; GO:0042981; P:regulation of apoptotic process; IGI:FlyBase.
GO; GO:0008359; P:regulation of bicoid mRNA localization; IMP:FlyBase.
GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
GO; GO:0007622; P:rhythmic behavior; IMP:FlyBase.
GO; GO:0048682; P:sprouting of injured axon; IMP:FlyBase.
GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; cAMP; Complete proteome; Kinase; Lipoprotein; Myristate;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 353 cAMP-dependent protein kinase catalytic
subunit.
/FTId=PRO_0000086069.
DOMAIN 46 300 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 301 353 AGC-kinase C-terminal.
NP_BIND 52 60 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 169 169 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 75 75 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
SEQUENCE 353 AA; 40839 MW; 9611D1001C791874 CRC64;
MGNNATTSNK KVDAAETVKE FLEQAKEEFE DKWRRNPTNT AALDDFERIK TLGTGSFGRV
MIVQHKPTKD YYAMKILDKQ KVVKLKQVEH TLNEKRILQA IQFPFLVSLR YHFKDNSNLY
MVLEYVPGGE MFSHLRKVGR FSEPHSRFYA AQIVLAFEYL HYLDLIYRDL KPENLLIDSQ
GYLKVTDFGF AKRVKGRTWT LCGTPEYLAP EIILSKGYNK AVDWWALGVL VYEMAAGYPP
FFADQPIQIY EKIVSGKVRF PSHFGSDLKD LLRNLLQVDL TKRYGNLKAG VNDIKNQKWF
ASTDWIAIFQ KKIEAPFIPR CKGPGDTSNF DDYEEEALRI SSTEKCAKEF AEF


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