KAPC1_DROME
ID KAPC1_DROME Reviewed; 353 AA.
AC P12370; A4V0I0; Q9VL99;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit 1 {ECO:0000305};
DE Short=PKA C;
DE EC=2.7.11.11 {ECO:0000305|PubMed:29473541};
DE AltName: Full=Protein kinase DC0 {ECO:0000303|PubMed:3215511};
GN Name=Pka-C1; Synonyms=CdkA, DC0; ORFNames=CG4379;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2828348; DOI=10.1016/s0021-9258(19)77929-0;
RA Foster J.L., Higgins G.C., Jackson R.F.;
RT "Cloning, sequence, and expression of the Drosophila cAMP-dependent protein
RT kinase catalytic subunit gene.";
RL J. Biol. Chem. 263:1676-1681(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=3215511; DOI=10.1101/gad.2.12a.1539;
RA Kalderon D., Rubin G.M.;
RT "Isolation and characterization of Drosophila cAMP-dependent protein kinase
RT genes.";
RL Genes Dev. 2:1539-1556(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION.
RX PubMed=29444420; DOI=10.1016/j.celrep.2018.01.049;
RA Parkhurst S.J., Adhikari P., Navarrete J.S., Legendre A., Manansala M.,
RA Wolf F.W.;
RT "Perineurial Barrier Glia Physically Respond to Alcohol in an Akap200-
RT Dependent Manner to Promote Tolerance.";
RL Cell Rep. 22:1647-1656(2018).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29473541; DOI=10.7554/elife.33007;
RA Lee P.T., Lin G., Lin W.W., Diao F., White B.H., Bellen H.J.;
RT "A kinase-dependent feedforward loop affects CREBB stability and long term
RT memory formation.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in memory formation
CC (PubMed:29473541). Promotes long-term memory by phosphorylating meng
CC and by regulating CrebB protein stability and activity
CC (PubMed:29473541). As part of ethanol response in the glia, mediates
CC ethanol-induced structural remodeling of actin cytoskeleton and
CC perineurial membrane topology when anchored to the membrane
CC (PubMed:29444420). {ECO:0000269|PubMed:29444420,
CC ECO:0000269|PubMed:29473541}.
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 Evidence={ECO:0000305|PubMed:29473541};
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; Evidence={ECO:0000305|PubMed:29473541};
CC -!- ACTIVITY REGULATION: Activated by cAMP.
CC -!- SUBUNIT: Composed of two regulatory chains and two catalytic chains.
CC -!- INTERACTION:
CC P12370; Q9VT65: CalpB; NbExp=2; IntAct=EBI-82224, EBI-132069;
CC P12370; Q03720: slo; NbExp=5; IntAct=EBI-82224, EBI-426805;
CC -!- TISSUE SPECIFICITY: More abundant in adult head than adult body.
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; M18655; AAA28412.1; -; Genomic_DNA.
DR EMBL; X16969; CAA34840.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52797.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10703.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64669.1; -; Genomic_DNA.
DR EMBL; AY069425; AAL39570.1; -; mRNA.
DR PIR; C31751; C31751.
DR RefSeq; NP_476977.1; NM_057629.4.
DR RefSeq; NP_723479.1; NM_164866.3.
DR RefSeq; NP_995672.1; NM_205950.3.
DR AlphaFoldDB; P12370; -.
DR SMR; P12370; -.
DR BioGRID; 60383; 23.
DR DIP; DIP-23727N; -.
DR IntAct; P12370; 7.
DR MINT; P12370; -.
DR STRING; 7227.FBpp0079448; -.
DR PaxDb; P12370; -.
DR PRIDE; P12370; -.
DR EnsemblMetazoa; FBtr0079851; FBpp0079448; FBgn0000273.
DR EnsemblMetazoa; FBtr0079852; FBpp0089382; FBgn0000273.
DR EnsemblMetazoa; FBtr0335495; FBpp0307466; FBgn0000273.
DR GeneID; 34284; -.
DR KEGG; dme:Dmel_CG4379; -.
DR UCSC; CG4379-RB; d. melanogaster.
DR CTD; 34284; -.
DR FlyBase; FBgn0000273; Pka-C1.
DR VEuPathDB; VectorBase:FBgn0000273; -.
DR eggNOG; KOG0616; Eukaryota.
DR GeneTree; ENSGT00940000163111; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; P12370; -.
DR OMA; WQDSRNL; -.
DR OrthoDB; 963519at2759; -.
DR PhylomeDB; P12370; -.
DR BRENDA; 2.7.11.11; 1994.
DR Reactome; R-DME-163615; PKA activation.
DR Reactome; R-DME-164378; PKA activation in glucagon signalling.
DR Reactome; R-DME-180024; DARPP-32 events.
DR Reactome; R-DME-209159; Assembly of the CI containing complexes.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DME-392517; Rap1 signalling.
DR Reactome; R-DME-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-DME-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-DME-5610787; Hedgehog 'off' state.
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DME-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DME-9634597; GPER1 signaling.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P12370; -.
DR BioGRID-ORCS; 34284; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34284; -.
DR PRO; PR:P12370; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000273; Expressed in brain and 26 other tissues.
DR Genevisible; P12370; DM.
DR GO; GO:0044297; C:cell body; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
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; IMP:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0007615; P:anesthesia-resistant memory; IMP:FlyBase.
DR GO; GO:0007448; P:anterior/posterior pattern specification, imaginal disc; IMP:FlyBase.
DR GO; GO:0019933; P:cAMP-mediated signaling; TAS:FlyBase.
DR GO; GO:0071361; P:cellular response to ethanol; IMP:UniProtKB.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0046823; P:negative regulation of nucleocytoplasmic transport; IGI:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IGI:FlyBase.
DR GO; GO:0008359; P:regulation of bicoid mRNA localization; IMP:FlyBase.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0007622; P:rhythmic behavior; IMP:FlyBase.
DR GO; GO:0048682; P:sprouting of injured axon; IMP:FlyBase.
DR GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR CDD; cd14209; STKc_PKA; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR044109; STKc_PKA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein 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 /evidence="ECO:0000250"
FT CHAIN 2..353
FT /note="cAMP-dependent protein kinase catalytic subunit 1"
FT /id="PRO_0000086069"
FT DOMAIN 46..300
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 301..353
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 52..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ 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
