TAO_DROME
ID TAO_DROME Reviewed; 1039 AA.
AC Q0KHQ5; Q8T093;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase Tao {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22075147, ECO:0000269|PubMed:22075148};
GN Name=Tao {ECO:0000312|FlyBase:FBgn0031030};
GN Synonyms=Tao-1 {ECO:0000312|FlyBase:FBgn0031030};
GN ORFNames=CG14217 {ECO:0000312|FlyBase:FBgn0031030};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:BAF51959.1, ECO:0000312|EMBL:BAF51960.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND D), AND FUNCTION.
RX PubMed=17449640; DOI=10.1073/pnas.0610052104;
RA Sato K., Hayashi Y., Ninomiya Y., Shigenobu S., Arita K., Mukai M.,
RA Kobayashi S.;
RT "Maternal Nanos represses hid/skl-dependent apoptosis to maintain the germ
RT line in Drosophila embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7455-7460(2007).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [4] {ECO:0000312|EMBL:AAL39614.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39614.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL39614.1};
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 [5] {ECO:0000312|EMBL:ACV53083.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACV53083.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:ACV53083.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-56.
RX PubMed=20647372; DOI=10.1242/jcs.068726;
RA Liu T., Rohn J.L., Picone R., Kunda P., Baum B.;
RT "Tao-1 is a negative regulator of microtubule plus-end growth.";
RL J. Cell Sci. 123:2708-2716(2010).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AUTOPHOSPHORYLATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22075147; DOI=10.1016/j.devcel.2011.08.028;
RA Boggiano J.C., Vanderzalm P.J., Fehon R.G.;
RT "Tao-1 phosphorylates Hippo/MST kinases to regulate the Hippo-Salvador-
RT Warts tumor suppressor pathway.";
RL Dev. Cell 21:888-895(2011).
RN [8] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AUTOPHOSPHORYLATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF LYS-56.
RX PubMed=22075148; DOI=10.1016/j.devcel.2011.09.012;
RA Poon C.L., Lin J.I., Zhang X., Harvey K.F.;
RT "The sterile 20-like kinase Tao-1 controls tissue growth by regulating the
RT Salvador-Warts-Hippo pathway.";
RL Dev. Cell 21:896-906(2011).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21248138; DOI=10.1523/jneurosci.4416-10.2011;
RA King I., Tsai L.T., Pflanz R., Voigt A., Lee S., Jaeckle H., Lu B.,
RA Heberlein U.;
RT "Drosophila tao controls mushroom body development and ethanol-stimulated
RT behavior through par-1.";
RL J. Neurosci. 31:1139-1148(2011).
RN [10] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23266957; DOI=10.1083/jcb.201207150;
RA Gomez J.M., Wang Y., Riechmann V.;
RT "Tao controls epithelial morphogenesis by promoting Fasciclin 2
RT endocytosis.";
RL J. Cell Biol. 199:1131-1143(2012).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=23227189; DOI=10.1371/journal.pone.0050594;
RA Kapfhamer D., King I., Zou M.E., Lim J.P., Heberlein U., Wolf F.W.;
RT "JNK pathway activation is controlled by Tao/TAOK3 to modulate ethanol
RT sensitivity.";
RL PLoS ONE 7:E50594-E50594(2012).
RN [12] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25160975; DOI=10.1016/j.jgg.2014.05.007;
RA Huang X., Shi L., Cao J., He F., Li R., Zhang Y., Miao S., Jin L., Qu J.,
RA Li Z., Lin X.;
RT "The sterile 20-like kinase tao controls tissue homeostasis by regulating
RT the hippo pathway in Drosophila adult midgut.";
RL J. Genet. Genomics 41:429-438(2014).
RN [13] {ECO:0000305}
RP FUNCTION (ISOFORMS A AND D), SUBCELLULAR LOCATION (ISOFORMS A AND D),
RP DEVELOPMENTAL STAGE (ISOFORMS A AND D), DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF LYS-56.
RX PubMed=25589578; DOI=10.1098/rsob.140161;
RA Pflanz R., Voigt A., Yakulov T., Jaeckle H.;
RT "Drosophila gene tao-1 encodes proteins with and without a Ste20 kinase
RT domain that affect cytoskeletal architecture and cell migration
RT differently.";
RL Open Biol. 5:140161-140161(2015).
RN [14] {ECO:0000305}
RP INTERACTION WITH SCHIP1, AND SUBCELLULAR LOCATION.
RX PubMed=26954546; DOI=10.1016/j.devcel.2016.02.004;
RA Chung H.L., Augustine G.J., Choi K.W.;
RT "Drosophila Schip1 links Expanded and Tao-1 to regulate hippo signaling.";
RL Dev. Cell 36:511-524(2016).
CC -!- FUNCTION: Serine/threonine-protein kinase which regulates the Hippo/SWH
CC (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a
CC pivotal role in organ size control and tumor suppression by restricting
CC proliferation and promoting apoptosis. The core of this pathway is
CC composed of a kinase cascade wherein Hippo (hpo), in complex with its
CC regulatory protein Salvador (sav), phosphorylates and activates Warts
CC (wts) in complex with its regulatory protein Mats, which in turn
CC phosphorylates and inactivates the Yorkie (yki) oncoprotein
CC (PubMed:22075147, PubMed:22075148). In imaginal cells, phosphorylates
CC and activates hpo and leads to repression of yki (PubMed:22075147,
CC PubMed:22075148). In the midgut, negatively regulates the proliferation
CC of intestinal stem cells through the Hippo/SWH pathway
CC (PubMed:25160975). Independent of the hippo/SWH pathway, regulates
CC epithelial morphogenesis in follicle cells by promoting the endocytosis
CC of Fas2 and reducing lateral adhesion between epithelial cells which,
CC in turn, permits shrinking of the lateral membrane and initiates
CC morphogenesis of the squamous epithelium (PubMed:23266957). Required
CC for the development of both the mushroom body and the ellipsoid body in
CC the brain and may act as a negative regulator of the par-1 kinase
CC (PubMed:21248138). Negatively regulates the JNK pathway which increases
CC sensitivity to ethanol exposure (PubMed:23227189). Plays a role in the
CC control of cell shape by negatively regulating the growth of
CC microtubule plus-ends as they contact the actin-rich cell cortex
CC (PubMed:20647372). Required for the induction of apoptosis in pole
CC cells by promoting expression of skl which enhances activity of the
CC apoptosis activator hid (PubMed:17449640).
CC {ECO:0000269|PubMed:17449640, ECO:0000269|PubMed:20647372,
CC ECO:0000269|PubMed:21248138, ECO:0000269|PubMed:22075147,
CC ECO:0000269|PubMed:22075148, ECO:0000269|PubMed:23227189,
CC ECO:0000269|PubMed:23266957, ECO:0000269|PubMed:25160975}.
CC -!- FUNCTION: [Isoform D]: Induces in vitro expression of large, highly
CC dynamic, microtubule-dependent lamellopodia-like cytoplasmic expansions
CC which constantly probe the environment. {ECO:0000269|PubMed:25589578}.
CC -!- FUNCTION: [Isoform A]: Induces in vitro expression of actin-dependent
CC filopodia-like cytoplasmic protrusions which firmly attach to the
CC substrate. Antagonizes the activity of isoform D.
CC {ECO:0000269|PubMed:25589578}.
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:22075147, ECO:0000269|PubMed:22075148};
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:22075147,
CC ECO:0000269|PubMed:22075148};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22075147, ECO:0000269|PubMed:22075148};
CC -!- SUBUNIT: Interacts with Schip1; the interaction enhances Tao kinase
CC activity. {ECO:0000269|PubMed:26954546}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20647372}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:20647372}. Cytoplasm {ECO:0000269|PubMed:23266957,
CC ECO:0000269|PubMed:26954546}. Membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:23266957, ECO:0000269|PubMed:26954546}.
CC Note=Localizes to a subset of microtubules in interphase and mitotic
CC cells (PubMed:20647372). In follicle cells, accumulates in the
CC basolateral cytoplasm and at the lateral membrane (PubMed:23266957).
CC {ECO:0000269|PubMed:20647372, ECO:0000269|PubMed:23266957}.
CC -!- SUBCELLULAR LOCATION: [Isoform D]: Cytoplasm
CC {ECO:0000269|PubMed:25589578}. Perikaryon
CC {ECO:0000269|PubMed:25589578}. Note=In non-neuronal cells, distributed
CC throughout the cytoplasm and enriched at the leading edge of
CC lamellipodia-like structures. In neurons, detected in the perikaryon.
CC {ECO:0000269|PubMed:25589578}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:25589578}. Cell projection, axon
CC {ECO:0000269|PubMed:25589578}. Note=In non-neuronal cells, located
CC predominantly at the cell periphery in the cortex. In neurons, enriched
CC in the cell periphery including the axon.
CC {ECO:0000269|PubMed:25589578}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D {ECO:0000312|FlyBase:FBgn0031030}; Synonyms=E
CC {ECO:0000312|FlyBase:FBgn0031030}, F {ECO:0000312|FlyBase:FBgn0031030},
CC Tao-L {ECO:0000303|PubMed:25589578};
CC IsoId=Q0KHQ5-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0031030}; Synonyms=G
CC {ECO:0000312|FlyBase:FBgn0031030}, Tao-S {ECO:0000303|PubMed:25589578};
CC IsoId=Q0KHQ5-2; Sequence=VSP_058386;
CC -!- TISSUE SPECIFICITY: In the posterior midgut, expressed in almost all
CC intestinal cell types including intestinal stem cells and enterocytes
CC (at protein level). Maternally expressed, ubiquitously distributed in
CC the egg and early embryo and enriched in the germ plasm at the
CC posterior pole of the early embryo including the pole cells.
CC {ECO:0000269|PubMed:25160975}.
CC -!- DEVELOPMENTAL STAGE: Isoform A: Enriched in germ plasm but is degraded
CC in pole cells immediately after pole cell formation. Isoform D:
CC Enriched in germ plasm, partitions into pole cells and remains
CC detectable in pole cells until they migrate through the midgut
CC epithelium toward the overlying mesoderm.
CC {ECO:0000269|PubMed:25589578}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:22075147,
CC ECO:0000269|PubMed:22075148}.
CC -!- DISRUPTION PHENOTYPE: Morphological defects in the follicular
CC epithelium where cells in the anterior part of the epithelium stay
CC cuboidal and fail to stretch (PubMed:23266957). RNAi-mediated knockdown
CC in eye and wing imaginal disks results in tissue overgrowth
CC (PubMed:22075147, PubMed:22075148). It also gives rise to
CC transcriptional up-regulation of a number of targets of the Hippo/SWH
CC pathway (PubMed:22075147). RNAi-mediated knockdown in wing imaginal
CC disks results in strong elevation of yki activity (PubMed:22075148).
CC RNAi-mediated knockdown in the adult posterior midgut results in an
CC increased number of intestinal stem cells (PubMed:25160975). RNAi-
CC mediated knockdown in the embryo results in disordered migration of
CC primordial germ cells out of the gut epithelium, their dispersal within
CC the embryo and embryonic death (PubMed:25589578).
CC {ECO:0000269|PubMed:21248138, ECO:0000269|PubMed:22075147,
CC ECO:0000269|PubMed:22075148, ECO:0000269|PubMed:23266957,
CC ECO:0000269|PubMed:25160975, ECO:0000269|PubMed:25589578}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AB277547; BAF51959.1; -; mRNA.
DR EMBL; AB277548; BAF51960.1; -; mRNA.
DR EMBL; AE014298; AAF48973.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09504.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09505.1; -; Genomic_DNA.
DR EMBL; AE014298; ADV37754.1; -; Genomic_DNA.
DR EMBL; AE014298; ADV37755.1; -; Genomic_DNA.
DR EMBL; AY069469; AAL39614.1; -; mRNA.
DR EMBL; BT099719; ACV53083.1; -; mRNA.
DR RefSeq; NP_001188672.1; NM_001201743.3. [Q0KHQ5-1]
DR RefSeq; NP_001188673.1; NM_001201744.2. [Q0KHQ5-2]
DR RefSeq; NP_608319.1; NM_134475.4. [Q0KHQ5-2]
DR RefSeq; NP_728267.1; NM_167665.2. [Q0KHQ5-1]
DR RefSeq; NP_728268.1; NM_167666.3. [Q0KHQ5-1]
DR AlphaFoldDB; Q0KHQ5; -.
DR SMR; Q0KHQ5; -.
DR IntAct; Q0KHQ5; 11.
DR STRING; 7227.FBpp0292968; -.
DR PaxDb; Q0KHQ5; -.
DR PRIDE; Q0KHQ5; -.
DR DNASU; 32948; -.
DR EnsemblMetazoa; FBtr0074771; FBpp0074540; FBgn0031030. [Q0KHQ5-1]
DR EnsemblMetazoa; FBtr0074772; FBpp0074541; FBgn0031030. [Q0KHQ5-1]
DR EnsemblMetazoa; FBtr0074774; FBpp0074543; FBgn0031030. [Q0KHQ5-2]
DR EnsemblMetazoa; FBtr0303999; FBpp0292968; FBgn0031030. [Q0KHQ5-1]
DR EnsemblMetazoa; FBtr0304000; FBpp0292969; FBgn0031030. [Q0KHQ5-2]
DR GeneID; 32948; -.
DR KEGG; dme:Dmel_CG14217; -.
DR UCSC; CG14217-RA; d. melanogaster.
DR UCSC; CG14217-RD; d. melanogaster. [Q0KHQ5-1]
DR CTD; 32948; -.
DR FlyBase; FBgn0031030; Tao.
DR VEuPathDB; VectorBase:FBgn0031030; -.
DR eggNOG; KOG0577; Eukaryota.
DR GeneTree; ENSGT00940000168060; -.
DR InParanoid; Q0KHQ5; -.
DR PhylomeDB; Q0KHQ5; -.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR SignaLink; Q0KHQ5; -.
DR BioGRID-ORCS; 32948; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Tao; fly.
DR GenomeRNAi; 32948; -.
DR PRO; PR:Q0KHQ5; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0031030; Expressed in germline cell (Drosophila) and 34 other tissues.
DR ExpressionAtlas; Q0KHQ5; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0045178; C:basal part of cell; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
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:0006915; P:apoptotic process; IMP:FlyBase.
DR GO; GO:0048036; P:central complex development; IMP:FlyBase.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:FlyBase.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IMP:FlyBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0042220; P:response to cocaine; IMP:FlyBase.
DR GO; GO:0045471; P:response to ethanol; IMP:FlyBase.
DR GO; GO:0035094; P:response to nicotine; IMP:FlyBase.
DR GO; GO:0001894; P:tissue homeostasis; IMP:FlyBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Kinase; Magnesium; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1039
FT /note="Serine/threonine-protein kinase Tao"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436542"
FT DOMAIN 27..280
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 324..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 631..765
FT /evidence="ECO:0000255"
FT COILED 835..993
FT /evidence="ECO:0000255"
FT COMPBIAS 339..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..568
FT /note="MPSARPGSLKDPEIADLFNKHDPEKIFEDLREIGHGSFGAVYYARCNLTREI
FT VAIKKMSYTGKQSQEKWQDILKEIRFLRQLNHPNTIEYKGCYLRESTAWLVMEYCVGSA
FT SDIIEVHKKPLHEDEIAAICLGVLSGLSYLHSLGRIHRDIKAGNILLTDNGVVKLADFG
FT SAAIKCPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPYFNMNA
FT MSALYHIAQNESPTLPKNDWSDAFCSFVELCLKKMPAERPSSAKLLTHAYVTRPRSDTV
FT LLELIARTKSAVRELDNLNYRKMKKILMVDTCETESAVGDTDDQQDDHAGGDSSKSNSI
FT TSEHSIHSVGVSAASSQSSSSNSIPAAAQNHHHIAAHHHQQAASAAVAAAMHHHHHPHQ
FT QPPPSWPSGQQGQPVPPGAVSRNSSRHRNRPPLPNIMHSMNNNVTPTNSASVVPAPAPA
FT PVLPPPISVLPHLSAMGHVGGGGTGTGGSGGGSPASGGPLADRIQPVQPRYLTTPAAQA
FT AVYAASSASSQQAISNAVNDHGPNNFATIRTTSIVTKQQKEHMQ -> MFWPRFAPVEV
FT MVELEFGSGF (in isoform A)"
FT /id="VSP_058386"
FT MUTAGEN 56
FT /note="K->A: Induces the formation of microtubule-rich
FT protrusions. Abolishes repression of Yki. Causes an isoform
FT A-like cellular phenotype with development of filopodia-
FT like structures."
FT /evidence="ECO:0000269|PubMed:20647372,
FT ECO:0000269|PubMed:22075148, ECO:0000269|PubMed:25589578"
SQ SEQUENCE 1039 AA; 118298 MW; 391D15216D295F3A CRC64;
MPSARPGSLK DPEIADLFNK HDPEKIFEDL REIGHGSFGA VYYARCNLTR EIVAIKKMSY
TGKQSQEKWQ DILKEIRFLR QLNHPNTIEY KGCYLRESTA WLVMEYCVGS ASDIIEVHKK
PLHEDEIAAI CLGVLSGLSY LHSLGRIHRD IKAGNILLTD NGVVKLADFG SAAIKCPANS
FVGTPYWMAP EVILAMDEGQ YDGKVDVWSL GITCIELAER KPPYFNMNAM SALYHIAQNE
SPTLPKNDWS DAFCSFVELC LKKMPAERPS SAKLLTHAYV TRPRSDTVLL ELIARTKSAV
RELDNLNYRK MKKILMVDTC ETESAVGDTD DQQDDHAGGD SSKSNSITSE HSIHSVGVSA
ASSQSSSSNS IPAAAQNHHH IAAHHHQQAA SAAVAAAMHH HHHPHQQPPP SWPSGQQGQP
VPPGAVSRNS SRHRNRPPLP NIMHSMNNNV TPTNSASVVP APAPAPVLPP PISVLPHLSA
MGHVGGGGTG TGGSGGGSPA SGGPLADRIQ PVQPRYLTTP AAQAAVYAAS SASSQQAISN
AVNDHGPNNF ATIRTTSIVT KQQKEHMQEE MHEQMSGYKR MRREHQAHLV KLEEKCKVDM
EAHKTALDKE YDTLLHNFTR DLDRLETKHQ QDVERRAKQT SAAEKKLHKE ITLKQENDRK
VYDLNRKKEY KANKERWKRE LSMDESTPKR QRDLTLQSQK DNLKQHEAQE EQRMLQAQKQ
YIELEMRKFK RKRMIMQHEH EDQQLRDELG KKEQQLQQAH AMLLKHHEKT QELEYRQQKS
VHQLREEQIN KQHDTELHNQ KDYMDRIKKE LVRKHAVELR QQPKSLKQKE LQIRKQFRET
CKTQTKQYKR YKAQVLQTTP KEQQKEVIKQ LKEEKHRKLT LLGEQYEQSI ADMFQSQSYK
LDESQVIECQ RTHEQLEYEL EMLTAYQNKN KKQAQEQRDR ERRELENRVS VRRGLLENKM
DAELQQFNQE RAERLRMKHE KHTKELEAFD NESIALGFST LSLIEVSREA YADEEGSLSG
SMISLAHSNS STSFPAGSL
