AKT1_DROME
ID AKT1_DROME Reviewed; 611 AA.
AC Q8INB9; Q0KI65; Q24293; Q24469; Q24470; Q7JN11; Q8T9A5; Q9VEY7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=RAC serine/threonine-protein kinase;
DE Short=DAkt;
DE Short=DRAC-PK;
DE Short=Dakt1;
DE EC=2.7.11.1;
DE AltName: Full=Akt;
DE AltName: Full=Protein kinase B;
DE Short=PKB;
GN Name=Akt1 {ECO:0000312|FlyBase:FBgn0010379};
GN ORFNames=CG4006 {ECO:0000312|FlyBase:FBgn0010379};
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 [MRNA] (ISOFORM A).
RX PubMed=8302573;
RA Franke T.F., Tartof K.D., Tsichlis P.N.;
RT "The SH2-like Akt homology (AH) domain of c-akt is present in multiple
RT copies in the genome of vertebrate and invertebrate eucaryotes. Cloning and
RT characterisation of the Drosophila melanogaster c-akt homolog Dakt1.";
RL Oncogene 9:141-148(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE INITIATION (ISOFORMS A AND
RP C), ENZYME ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7876156; DOI=10.1074/jbc.270.8.4066;
RA Andjelkovic M., Jones P.F., Grossniklaus U., Cron P., Schier A.F., Dick M.,
RA Bilbe G., Hemmings B.A.;
RT "Developmental regulation of expression and activity of multiple forms of
RT the Drosophila RAC protein kinase.";
RL J. Biol. Chem. 270:4066-4075(1995).
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, AND ALTERNATIVE INITIATION.
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] (ISOFORM A).
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, MUTAGENESIS OF PHE-408, AND DISRUPTION PHENOTYPE.
RX PubMed=9601646; DOI=10.1016/s0960-9822(98)70231-3;
RA Staveley B.E., Ruel L., Jin J., Stambolic V., Mastronardi F.G.,
RA Heitzler P., Woodgett J.R., Manoukian A.S.;
RT "Genetic analysis of protein kinase B (AKT) in Drosophila.";
RL Curr. Biol. 8:599-602(1998).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LYS-295.
RX PubMed=10587646; DOI=10.1038/70293;
RA Verdu J., Buratovich M.A., Wilder E.L., Birnbaum M.J.;
RT "Cell-autonomous regulation of cell and organ growth in Drosophila by
RT Akt/PKB.";
RL Nat. Cell Biol. 1:500-506(1999).
RN [8]
RP FUNCTION, AND PHOSPHORYLATION AT SER-586.
RX PubMed=10962553; DOI=10.1038/sj.onc.1203739;
RA Scanga S.E., Ruel L., Binari R.C., Snow B., Stambolic V., Bouchard D.,
RA Peters M., Calvieri B., Mak T.W., Woodgett J.R., Manoukian A.S.;
RT "The conserved PI3'K/PTEN/Akt signaling pathway regulates both cell size
RT and survival in Drosophila.";
RL Oncogene 19:3971-3977(2000).
RN [9]
RP FUNCTION.
RX PubMed=11740943; DOI=10.1016/s1534-5807(01)00090-9;
RA Jin J., Anthopoulos N., Wetsch B., Binari R.C., Isaac D.D., Andrew D.J.,
RA Woodgett J.R., Manoukian A.S.;
RT "Regulation of Drosophila tracheal system development by protein kinase
RT B.";
RL Dev. Cell 1:817-827(2001).
RN [10]
RP PHOSPHORYLATION.
RX PubMed=11344272; DOI=10.1073/pnas.101596998;
RA Cho K.S., Lee J.H., Kim S., Kim D., Koh H., Lee J., Kim C., Kim J.,
RA Chung J.;
RT "Drosophila phosphoinositide-dependent kinase-1 regulates apoptosis and
RT growth via the phosphoinositide 3-kinase-dependent signaling pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6144-6149(2001).
RN [11]
RP FUNCTION.
RX PubMed=11752451; DOI=10.1073/pnas.011318098;
RA Rintelen F., Stocker H., Thomas G., Hafen E.;
RT "PDK1 regulates growth through Akt and S6K in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:15020-15025(2001).
RN [12]
RP FUNCTION.
RX PubMed=12172554; DOI=10.1038/ncb840;
RA Potter C.J., Pedraza L.G., Xu T.;
RT "Akt regulates growth by directly phosphorylating Tsc2.";
RL Nat. Cell Biol. 4:658-665(2002).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF GLY-180 AND PHE-408.
RX PubMed=11872800; DOI=10.1126/science.1068094;
RA Stocker H., Andjelkovic M., Oldham S., Laffargue M., Wymann M.P.,
RA Hemmings B.A., Hafen E.;
RT "Living with lethal PIP3 levels: viability of flies lacking PTEN restored
RT by a PH domain mutation in Akt/PKB.";
RL Science 295:2088-2091(2002).
RN [14]
RP FUNCTION.
RX PubMed=14525946; DOI=10.1096/fj.03-0040fje;
RA Lavenburg K.R., Ivey J., Hsu T., Muise-Helmericks R.C.;
RT "Coordinated functions of Akt/PKB and ETS1 in tubule formation.";
RL FASEB J. 17:2278-2280(2003).
RN [15]
RP FUNCTION.
RX PubMed=12893776; DOI=10.1101/gad.1098703;
RA Puig O., Marr M.T., Ruhf M.L., Tjian R.;
RT "Control of cell number by Drosophila FOXO: downstream and feedback
RT regulation of the insulin receptor pathway.";
RL Genes Dev. 17:2006-2020(2003).
RN [16]
RP FUNCTION.
RX PubMed=15466161; DOI=10.1101/gad.1240504;
RA Dong J., Pan D.;
RT "Tsc2 is not a critical target of Akt during normal Drosophila
RT development.";
RL Genes Dev. 18:2479-2484(2004).
RN [17]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15712201; DOI=10.1002/dvdy.20333;
RA Cavaliere V., Donati A., Hsouna A., Hsu T., Gargiulo G.;
RT "dAkt kinase controls follicle cell size during Drosophila oogenesis.";
RL Dev. Dyn. 232:845-854(2005).
RN [18]
RP DEPHOSPHORYLATION AT SER-586.
RX PubMed=15808505; DOI=10.1016/j.molcel.2005.03.008;
RA Gao T., Furnari F., Newton A.C.;
RT "PHLPP: a phosphatase that directly dephosphorylates Akt, promotes
RT apoptosis, and suppresses tumor growth.";
RL Mol. Cell 18:13-24(2005).
RN [19]
RP PHOSPHORYLATION AT SER-586.
RX PubMed=15718470; DOI=10.1126/science.1106148;
RA Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.;
RT "Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex.";
RL Science 307:1098-1101(2005).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [21]
RP PHOSPHORYLATION.
RX PubMed=22493059; DOI=10.1128/mcb.06474-11;
RA Wang T., Blumhagen R., Lao U., Kuo Y., Edgar B.A.;
RT "LST8 regulates cell growth via target-of-rapamycin complex 2 (TORC2).";
RL Mol. Cell. Biol. 32:2203-2213(2012).
RN [22]
RP DISRUPTION PHENOTYPE.
RX PubMed=24786828; DOI=10.1038/cdd.2014.63;
RA Wei Y., Lilly M.A.;
RT "The TORC1 inhibitors Nprl2 and Nprl3 mediate an adaptive response to
RT amino-acid starvation in Drosophila.";
RL Cell Death Differ. 21:1460-1468(2014).
RN [23]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24603715; DOI=10.1371/journal.pgen.1004172;
RA Liu Y., Wang W., Shui G., Huang X.;
RT "CDP-diacylglycerol synthetase coordinates cell growth and fat storage
RT through phosphatidylinositol metabolism and the insulin pathway.";
RL PLoS Genet. 10:E1004172-E1004172(2014).
RN [24]
RP FUNCTION, AND PHOSPHORYLATION AT SER-586.
RX PubMed=25329475; DOI=10.1371/journal.pone.0109530;
RA Das R., Sebo Z., Pence L., Dobens L.L.;
RT "Drosophila tribbles antagonizes insulin signaling-mediated growth and
RT metabolism via interactions with Akt kinase.";
RL PLoS ONE 9:E109530-E109530(2014).
RN [25]
RP FUNCTION, AND INTERACTION WITH TRBL.
RX PubMed=29025897; DOI=10.1242/dmm.030619;
RA Fischer Z., Das R., Shipman A., Fan J.Y., Pence L., Bouyain S.,
RA Dobens L.L.;
RT "A Drosophila model of insulin resistance associated with the human Trib3
RT Q/R polymorphism.";
RL Dis. Model. Mech. 10:1453-1464(2017).
CC -!- FUNCTION: Serine/threonine kinase involved in various developmental
CC processes (PubMed:9601646, PubMed:10587646, PubMed:10962553,
CC PubMed:11740943, PubMed:12172554, PubMed:11872800, PubMed:14525946,
CC PubMed:12893776, PubMed:15466161, PubMed:15712201). During early
CC embryogenesis, acts as a survival protein (PubMed:9601646,
CC PubMed:10962553). During mid-embryogenesis, phosphorylates and
CC activates trh, a transcription factor required for tracheal cell fate
CC determination (PubMed:11740943). Also regulates tracheal cell migration
CC (PubMed:11740943, PubMed:14525946). Later in development, acts
CC downstream of PI3K and Pk61C/PDK1 in the insulin receptor transduction
CC pathway which regulates cell growth and organ size, by phosphorylating
CC and antagonizing FOXO transcription factor (PubMed:10587646,
CC PubMed:10962553, PubMed:11752451, PubMed:12893776, PubMed:25329475,
CC PubMed:29025897, PubMed:24603715). Controls follicle cell size during
CC oogenesis (PubMed:15712201). May also stimulate cell growth by
CC phosphorylating Gig/Tsc2 and inactivating the Tsc complex
CC (PubMed:12172554, PubMed:15466161). Dephosphorylation of 'Ser-586' by
CC Phlpp triggers apoptosis and suppression of tumor growth
CC (PubMed:10962553). {ECO:0000269|PubMed:10587646,
CC ECO:0000269|PubMed:10962553, ECO:0000269|PubMed:11740943,
CC ECO:0000269|PubMed:11752451, ECO:0000269|PubMed:11872800,
CC ECO:0000269|PubMed:12172554, ECO:0000269|PubMed:12893776,
CC ECO:0000269|PubMed:14525946, ECO:0000269|PubMed:15466161,
CC ECO:0000269|PubMed:15712201, ECO:0000269|PubMed:24603715,
CC ECO:0000269|PubMed:25329475, ECO:0000269|PubMed:29025897,
CC ECO:0000269|PubMed:9601646}.
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=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:7876156};
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=2.7.11.1; Evidence={ECO:0000269|PubMed:7876156};
CC -!- SUBUNIT: Interacts with trbl. {ECO:0000269|PubMed:29025897}.
CC -!- INTERACTION:
CC Q8INB9; Q9VDE3: slmb; NbExp=4; IntAct=EBI-162210, EBI-91763;
CC Q8INB9; P68198: Ubi-p63E; NbExp=2; IntAct=EBI-162210, EBI-86340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Recruited
CC to plasma membrane upon activation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=C; Synonyms=PK85;
CC IsoId=Q8INB9-1; Sequence=Displayed;
CC Name=A; Synonyms=PK66;
CC IsoId=Q8INB9-2; Sequence=VSP_018833;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in ovary, where it
CC is concentrated at the basal side of follicle cells.
CC {ECO:0000269|PubMed:7876156}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Strongly expressed in embryo and pupa. Weakly expressed in larva.
CC Mildly expressed in adult. {ECO:0000269|PubMed:15712201,
CC ECO:0000269|PubMed:7876156}.
CC -!- DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-kinase
CC alpha (PI(3)K) results in its targeting to the plasma membrane.
CC {ECO:0000305}.
CC -!- PTM: Phosphorylated and activated by Pk61C/PDK1 (PubMed:11344272).
CC Phosphorylated on Ser-586 by the TORC2 complex (PubMed:10962553,
CC PubMed:15718470, PubMed:22493059). {ECO:0000269|PubMed:10962553,
CC ECO:0000269|PubMed:11344272, ECO:0000269|PubMed:15718470,
CC ECO:0000269|PubMed:22493059}.
CC -!- DISRUPTION PHENOTYPE: Death at the first instar larval stage
CC (PubMed:9601646). Conditional RNAi-mediated knockdown in the female
CC germline reduces ovary size (PubMed:24786828). RNAi-mediated knockdown
CC in both larval salivary glands and fat body, results in small salivary
CC glands displaying ectopic lipid storage and reduced expression of CdsA
CC (PubMed:24603715). {ECO:0000269|PubMed:24603715,
CC ECO:0000269|PubMed:24786828, ECO:0000269|PubMed:9601646}.
CC -!- MISCELLANEOUS: [Isoform A]: Major form. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. RAC subfamily. {ECO:0000305}.
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DR EMBL; Z26242; CAA81204.1; -; mRNA.
DR EMBL; X83510; CAA58499.2; -; Genomic_DNA.
DR EMBL; X83510; CAA58500.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55275.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13699.3; -; Genomic_DNA.
DR EMBL; AY069856; AAL40001.1; -; mRNA.
DR PIR; A55888; A55888.
DR RefSeq; NP_001287353.1; NM_001300424.1. [Q8INB9-2]
DR RefSeq; NP_001287354.1; NM_001300425.1. [Q8INB9-2]
DR RefSeq; NP_732113.3; NM_169705.2. [Q8INB9-1]
DR RefSeq; NP_732114.1; NM_169706.2. [Q8INB9-2]
DR RefSeq; NP_732115.1; NM_169707.2. [Q8INB9-2]
DR AlphaFoldDB; Q8INB9; -.
DR SMR; Q8INB9; -.
DR BioGRID; 67008; 202.
DR DIP; DIP-49060N; -.
DR IntAct; Q8INB9; 43.
DR MINT; Q8INB9; -.
DR STRING; 7227.FBpp0082682; -.
DR iPTMnet; Q8INB9; -.
DR PaxDb; Q8INB9; -.
DR PRIDE; Q8INB9; -.
DR EnsemblMetazoa; FBtr0083226; FBpp0082680; FBgn0010379. [Q8INB9-2]
DR EnsemblMetazoa; FBtr0083227; FBpp0082681; FBgn0010379. [Q8INB9-2]
DR EnsemblMetazoa; FBtr0083228; FBpp0082682; FBgn0010379. [Q8INB9-1]
DR EnsemblMetazoa; FBtr0344470; FBpp0310841; FBgn0010379. [Q8INB9-2]
DR EnsemblMetazoa; FBtr0344717; FBpp0311050; FBgn0010379. [Q8INB9-2]
DR GeneID; 41957; -.
DR KEGG; dme:Dmel_CG4006; -.
DR CTD; 207; -.
DR FlyBase; FBgn0010379; Akt1.
DR VEuPathDB; VectorBase:FBgn0010379; -.
DR eggNOG; KOG0690; Eukaryota.
DR GeneTree; ENSGT00940000168810; -.
DR InParanoid; Q8INB9; -.
DR PhylomeDB; Q8INB9; -.
DR Reactome; R-DME-110478; Insulin signaling pathway.
DR Reactome; R-DME-110523; TOR signaling pathway.
DR Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DME-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DME-165158; Activation of AKT2.
DR Reactome; R-DME-165159; MTOR signalling.
DR Reactome; R-DME-165181; Inhibition of TSC complex formation by PKB.
DR Reactome; R-DME-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-DME-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-DME-199418; Negative regulation of the PI3K/AKT network.
DR Reactome; R-DME-203615; eNOS activation.
DR Reactome; R-DME-211163; AKT-mediated inactivation of FOXO1A.
DR Reactome; R-DME-354192; Integrin signaling.
DR Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-DME-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-DME-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-DME-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-DME-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-DME-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR Reactome; R-DME-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-DME-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-DME-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DME-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DME-9607240; FLT3 Signaling.
DR Reactome; R-DME-9614399; Regulation of localization of FOXO transcription factors.
DR Reactome; R-DME-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR Reactome; R-DME-9755511; KEAP1-NFE2L2 pathway.
DR SignaLink; Q8INB9; -.
DR BioGRID-ORCS; 41957; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Akt1; fly.
DR GenomeRNAi; 41957; -.
DR PRO; PR:Q8INB9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010379; Expressed in wing disc and 46 other tissues.
DR ExpressionAtlas; Q8INB9; baseline and differential.
DR Genevisible; Q8INB9; DM.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:FlyBase.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0031104; P:dendrite regeneration; IMP:FlyBase.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IGI:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:FlyBase.
DR GO; GO:0035264; P:multicellular organism growth; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:FlyBase.
DR GO; GO:0090278; P:negative regulation of peptide hormone secretion; IMP:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IGI:FlyBase.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0010884; P:positive regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:FlyBase.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:FlyBase.
DR GO; GO:0043491; P:protein kinase B signaling; IDA:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:FlyBase.
DR CDD; cd01241; PH_PKB; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039026; PH_PKB.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00233; PH; 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; PS50003; PH_DOMAIN; 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 Alternative initiation; Apoptosis; ATP-binding; Cell membrane; Cytoplasm;
KW Developmental protein; Growth regulation; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..611
FT /note="RAC serine/threonine-protein kinase"
FT /id="PRO_0000045784"
FT DOMAIN 106..211
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 266..523
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 524..597
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 14..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 272..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10962553,
FT ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:25329475"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8302573"
FT /id="VSP_018833"
FT MUTAGEN 180
FT /note="G->S: Fails to be recruited at the membrane upon
FT activation."
FT /evidence="ECO:0000269|PubMed:11872800"
FT MUTAGEN 260
FT /note="K->A: Abolishes enzymatic activity."
FT MUTAGEN 295
FT /note="K->M: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10587646"
FT MUTAGEN 408
FT /note="F->I: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11872800,
FT ECO:0000269|PubMed:9601646"
FT CONFLICT 73
FT /note="A -> T (in Ref. 2; CAA58499)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..201
FT /note="QQ -> HE (in Ref. 1; CAA81204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 68485 MW; C139380152580934 CRC64;
MNYLPFVLQR RSTVVASAPA PGSASRIPES PTTTGSNIIN IIYSQSTHPN SSPTSGSAEK
FSWQQSWPSR TSAAPTHDSG TMSINTTFDL SSPSVTSGHA LTEQTQVVKE GWLMKRGEHI
KNWRQRYFVL HSDGRLMGYR SKPADSASTP SDFLLNNFTV RGCQIMTVDR PKPFTFIIRG
LQWTTVIERT FAVESELERQ QWTEAIRNVS SRLIDVGEVA MTPSEQTDMT DVDMATIAED
ELSEQFSVQG TTCNSSGVKK VTLENFEFLK VLGKGTFGKV ILCREKATAK LYAIKILKKE
VIIQKDEVAH TLTESRVLKS TNHPFLISLK YSFQTNDRLC FVMQYVNGGE LFWHLSHERI
FTEDRTRFYG AEIISALGYL HSQGIIYRDL KLENLLLDKD GHIKVADFGL CKEDITYGRT
TKTFCGTPEY LAPEVLDDND YGQAVDWWGT GVVMYEMICG RLPFYNRDHD VLFTLILVEE
VKFPRNITDE AKNLLAGLLA KDPKKRLGGG KDDVKEIQAH PFFASINWTD LVLKKIPPPF
KPQVTSDTDT RYFDKEFTGE SVELTPPDPT GPLGSIAEEP LFPQFSYQGD MASTLGTSSH
ISTSTSLASM Q
