Entry sw: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   30-NOV-2016, entry version 139.
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;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.
RT   Cloning and characterisation of the Drosophila melanogaster c-akt
RT   homolog Dakt1.";
RL   Oncogene 9:141-148(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE INITIATION (ISOFORMS A
RP   AND 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.,
RA   Dick M., Bilbe G., Hemmings B.A.;
RT   "Developmental regulation of expression and activity of multiple forms
RT   of 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., 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
RT   size 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.,
RA   Andrew D.J., Woodgett J.R., Manoukian A.S.;
RT   "Regulation of Drosophila tracheal system development by protein
RT   kinase 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
RT   and growth via the phosphoinositide 3-kinase-dependent signaling
RT   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
RT   restored 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
RT   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
RT   complex.";
RL   Science 307:1098-1101(2005).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION
RP   BY 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   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).
CC   -!- FUNCTION: Serine/threonine kinase involved in various
CC       developmental processes. During early embryogenesis, acts as a
CC       survival protein. During mid-embryogenesis, phosphorylates and
CC       activates trh, a transcription factor required for tracheal cell
CC       fate determination. Also regulates tracheal cell migration. Later
CC       in development, acts downstream of PI3K and Pk61C/PDK1 in the
CC       insulin receptor transduction pathway which regulates cell growth
CC       and organ size, by phosphorylating and antagonizing FOXO
CC       transcription factor. Controls follicle cell size during
CC       oogenesis. May also stimulate cell growth by phosphorylating
CC       Gig/Tsc2 and inactivating the Tsc complex. Dephosphorylation of
CC       'Ser-586' by Phlpp triggers apoptosis and suppression of tumor
CC       growth. {ECO:0000269|PubMed:10587646, ECO:0000269|PubMed:10962553,
CC       ECO:0000269|PubMed:11740943, ECO:0000269|PubMed:11752451,
CC       ECO:0000269|PubMed:11872800, ECO:0000269|PubMed:12172554,
CC       ECO:0000269|PubMed:12893776, ECO:0000269|PubMed:14525946,
CC       ECO:0000269|PubMed:15466161, ECO:0000269|PubMed:15712201,
CC       ECO:0000269|PubMed:9601646}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000269|PubMed:7876156}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane.
CC       Note=Recruited 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         Note=Major form.;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in ovary,
CC       where it 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-
CC       kinase alpha (PI(3)K) results in its targeting to the plasma
CC       membrane. {ECO:0000305}.
CC   -!- PTM: Phosphorylated and activated by Pk61C/PDK1. Phosphorylated on
CC       Ser-586 by the rictor-Tor complex. {ECO:0000269|PubMed:10962553,
CC       ECO:0000269|PubMed:11344272, ECO:0000269|PubMed:15718470,
CC       ECO:0000269|PubMed:18327897}.
CC   -!- DISRUPTION PHENOTYPE: Death at the first instar larval stage
CC       (PubMed:9601646). Conditional RNAi-mediated knockdown in the
CC       female germline reduces ovary size (PubMed:24786828).
CC       {ECO:0000269|PubMed:24786828, ECO:0000269|PubMed:9601646}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. RAC subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PH domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00145}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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   UniGene; Dm.1219; -.
DR   ProteinModelPortal; Q8INB9; -.
DR   SMR; Q8INB9; -.
DR   BioGrid; 67008; 51.
DR   DIP; DIP-49060N; -.
DR   IntAct; Q8INB9; 41.
DR   MINT; MINT-291950; -.
DR   STRING; 7227.FBpp0082682; -.
DR   iPTMnet; Q8INB9; -.
DR   PaxDb; Q8INB9; -.
DR   PRIDE; Q8INB9; -.
DR   GeneID; 41957; -.
DR   KEGG; dme:Dmel_CG4006; -.
DR   CTD; 207; -.
DR   FlyBase; FBgn0010379; Akt1.
DR   eggNOG; KOG0598; Eukaryota.
DR   eggNOG; ENOG410XNPH; LUCA.
DR   InParanoid; Q8INB9; -.
DR   KO; K04456; -.
DR   OrthoDB; EOG091G06FF; -.
DR   PhylomeDB; Q8INB9; -.
DR   Reactome; R-DME-114604; GPVI-mediated activation cascade.
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 alphaIIb beta3 signaling.
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-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   SignaLink; Q8INB9; -.
DR   ChiTaRS; Akt1; fly.
DR   GenomeRNAi; 41957; -.
DR   PRO; PR:Q8INB9; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0010379; -.
DR   Genevisible; Q8INB9; DM.
DR   GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; NAS:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; NAS:FlyBase.
DR   GO; GO:0004672; F:protein kinase activity; IDA:FlyBase.
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:0008362; P:chitin-based embryonic cuticle biosynthetic process; IGI: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:0006629; P:lipid metabolic process; IMP:FlyBase.
DR   GO; GO:0019915; P:lipid storage; IGI: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:0007520; P:myoblast fusion; IMP:FlyBase.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; 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 growth at neuromuscular junction; 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:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR   GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; TAS:FlyBase.
DR   GO; GO:0046622; P:positive regulation of organ growth; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR   GO; GO:0008361; P:regulation of cell size; NAS:FlyBase.
DR   GO; GO:0050773; P:regulation of dendrite development; IMP:FlyBase.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; 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:0046620; P:regulation of organ growth; NAS:FlyBase.
DR   GO; GO:0042306; P:regulation of protein import into nucleus; TAS:FlyBase.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR   GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_dom-like.
DR   InterPro; IPR001849; PH_domain.
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; SSF50729; SSF50729; 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;
KW   Complete proteome; Cytoplasm; Developmental protein;
KW   Growth regulation; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    611       RAC serine/threonine-protein kinase.
FT                                /FTId=PRO_0000045784.
FT   DOMAIN      106    211       PH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00145}.
FT   DOMAIN      266    523       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      524    597       AGC-kinase C-terminal.
FT   NP_BIND     272    280       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    389    389       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     295    295       ATP. {ECO:0000305}.
FT   MOD_RES      30     30       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     586    586       Phosphoserine.
FT                                {ECO:0000269|PubMed:10962553,
FT                                ECO:0000269|PubMed:15718470}.
FT   VAR_SEQ       1     81       Missing (in isoform A).
FT                                {ECO:0000303|PubMed:12537569,
FT                                ECO:0000303|PubMed:8302573}.
FT                                /FTId=VSP_018833.
FT   MUTAGEN     180    180       G->S: Fails to be recruited at the
FT                                membrane upon activation.
FT                                {ECO:0000269|PubMed:11872800}.
FT   MUTAGEN     260    260       K->A: Abolishes enzymatic activity.
FT   MUTAGEN     295    295       K->M: Abolishes enzymatic activity.
FT                                {ECO:0000269|PubMed:10587646}.
FT   MUTAGEN     408    408       F->I: Abolishes enzymatic activity.
FT                                {ECO:0000269|PubMed:11872800,
FT                                ECO:0000269|PubMed:9601646}.
FT   CONFLICT     73     73       A -> T (in Ref. 2; CAA58499).
FT                                {ECO:0000305}.
FT   CONFLICT    200    201       QQ -> HE (in Ref. 1; CAA81204).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       266    523       ipfam:Pkinase [T]
FT   MYHIT       524    589       ismart:S_TK_X [T]
FT   MYHIT       272    295       ipat:PROTEIN_KINASE_ATP [T]
FT   MYHIT       524    597       iprf:AGC_KINASE_CTER [T]
FT   MYHIT       385    397       ipat:PROTEIN_KINASE_ST [T]
FT   MYHIT       266    523       ismart:S_TKc [T]
FT   MYHIT       266    523       iprf:PROTEIN_KINASE_DOM [T]
FT   MYHIT       544    587       ipfam:Pkinase_C [T]
FT   MYHIT       107    213       ismart:PH [T]
FT   MYHIT       107    210       ipfam:PH [T]
FT   MYHIT       106    211       iprf:PH_DOMAIN [T]
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
//