SGG_DROME
ID SGG_DROME Reviewed; 514 AA.
AC P18431; O76881; P23646; Q27603; Q27604; Q27605; Q8MRF7; Q9NF42; Q9U094;
AC Q9W4X3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 3.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Protein kinase shaggy;
DE EC=2.7.11.1;
DE AltName: Full=Protein zeste-white 3;
GN Name=sgg; Synonyms=gsk3, zw3; ORFNames=CG2621;
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 ZYGOTIC), FUNCTION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=DP CN BW; TISSUE=Embryo;
RX PubMed=2118107; DOI=10.1002/j.1460-2075.1990.tb07477.x;
RA Bourouis M., Moore P., Ruel L., Grau Y., Heitzler P., Simpson P.;
RT "An early embryonic product of the gene shaggy encodes a serine/threonine
RT protein kinase related to the CDC28/cdc2+ subfamily.";
RL EMBO J. 9:2877-2884(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SGG39; SGG46 AND ZYGOTIC), FUNCTION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8467811; DOI=10.1002/j.1460-2075.1993.tb05811.x;
RA Ruel L., Pantesco V., Lutz Y., Simpson P., Bourouis M.;
RT "Functional significance of a family of protein kinases encoded at the
RT shaggy locus in Drosophila.";
RL EMBO J. 12:1657-1669(1993).
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 SPLICING.
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS G AND ZYGOTIC).
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-289 (ISOFORM ZYGOTIC/SGG39), NUCLEOTIDE
RP SEQUENCE [MRNA] OF 30-514 (ISOFORM SGG46), AND FUNCTION.
RC TISSUE=Embryo, and Ovary;
RX PubMed=2113617; DOI=10.1038/345825a0;
RA Siegfried E., Perkins L.A., Capaci T.M., Perrimon N.;
RT "Putative protein kinase product of the Drosophila segment-polarity gene
RT zeste-white3.";
RL Nature 345:825-829(1990).
RN [8]
RP PHOSPHORYLATION AT TYR-214.
RX PubMed=8382613; DOI=10.1002/j.1460-2075.1993.tb05715.x;
RA Hughes K., Nikolakaki E., Plyte S.E., Totty N.F., Woodgett J.R.;
RT "Modulation of the glycogen synthase kinase-3 family by tyrosine
RT phosphorylation.";
RL EMBO J. 12:803-808(1993).
RN [9]
RP FUNCTION IN PHOSPHORYLATION OF ARM.
RX PubMed=7529201; DOI=10.1006/dbio.1994.1336;
RA Peifer M., Pai L.-M., Casey M.;
RT "Phosphorylation of the Drosophila adherens junction protein Armadillo:
RT roles for wingless signal and zeste-white 3 kinase.";
RL Dev. Biol. 166:543-556(1994).
RN [10]
RP INTERACTION WITH WG AND EN.
RC TISSUE=Embryo;
RX PubMed=1335365; DOI=10.1016/s0092-8674(05)80065-0;
RA Siegfried E., Chou T.B., Perrimon N.;
RT "wingless signaling acts through zeste-white 3, the Drosophila homolog of
RT glycogen synthase kinase-3, to regulate engrailed and establish cell
RT fate.";
RL Cell 71:1167-1179(1992).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ALA-81.
RX PubMed=15269269; DOI=10.1523/jneurosci.1580-04.2004;
RA Franco B., Bogdanik L., Bobinnec Y., Debec A., Bockaert J.,
RA Parmentier M.L., Grau Y.;
RT "Shaggy, the homolog of glycogen synthase kinase 3, controls neuromuscular
RT junction growth in Drosophila.";
RL J. Neurosci. 24:6573-6577(2004).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH COS.
RX PubMed=15691767; DOI=10.1016/j.devcel.2005.01.001;
RA Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.;
RT "Hedgehog-regulated Costal2-kinase complexes control phosphorylation and
RT proteolytic processing of Cubitus interruptus.";
RL Dev. Cell 8:267-278(2005).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16570248; DOI=10.1002/cm.20128;
RA Bobinnec Y., Morin X., Debec A.;
RT "Shaggy/GSK-3beta kinase localizes to the centrosome and to specialized
RT cytoskeletal structures in Drosophila.";
RL Cell Motil. Cytoskeleton 63:313-320(2006).
RN [14]
RP FUNCTION IN PHOSPHORYLATION OF FUTSCH.
RX PubMed=16949836; DOI=10.1016/j.mcn.2006.07.004;
RA Gogel S., Wakefield S., Tear G., Klambt C., Gordon-Weeks P.R.;
RT "The Drosophila microtubule associated protein Futsch is phosphorylated by
RT Shaggy/Zeste-white 3 at an homologous GSK3beta phosphorylation site in
RT MAP1B.";
RL Mol. Cell. Neurosci. 33:188-199(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; TYR-214 AND SER-217, AND
RP IDENTIFICATION 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 [16]
RP FUNCTION IN PHOSPHORYLATION OF SRA, AND TISSUE SPECIFICITY.
RX PubMed=22421435; DOI=10.1073/pnas.1120367109;
RA Takeo S., Swanson S.K., Nandanan K., Nakai Y., Aigaki T., Washburn M.P.,
RA Florens L., Hawley R.S.;
RT "Shaggy/glycogen synthase kinase 3beta and phosphorylation of
RT Sarah/regulator of calcineurin are essential for completion of Drosophila
RT female meiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6382-6389(2012).
CC -!- FUNCTION: Required for several developmental events such as syncytial
CC blastoderm formation and embryonic segmentation. Is involved in
CC transcriptional regulation. Required for arm phosphorylation. Wg
CC signaling operates by inactivating the sgg repression of en
CC autoactivation. Negatively controls the neuromuscular junction (NMJ)
CC growth in presynaptic motoneurons. Plays a role in the regulation of
CC microtubule dynamics and actin cytoskeleton during embryogenesis.
CC Required for phosphorylation of sra in activated eggs. Essential for
CC completion of meiosis, possibly by triggering calcineurin activation
CC via sra phosphorylation. Phosphorylates microtubule-associated protein
CC futsch in axons. {ECO:0000269|PubMed:15269269,
CC ECO:0000269|PubMed:16570248, ECO:0000269|PubMed:16949836,
CC ECO:0000269|PubMed:2113617, ECO:0000269|PubMed:2118107,
CC ECO:0000269|PubMed:22421435, ECO:0000269|PubMed:7529201,
CC ECO:0000269|PubMed:8467811}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with cos. {ECO:0000269|PubMed:1335365,
CC ECO:0000269|PubMed:15691767}.
CC -!- INTERACTION:
CC P18431; O77059: cry; NbExp=2; IntAct=EBI-242141, EBI-94117;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Cytoplasm, cell cortex.
CC Synapse. Cell projection, axon. Note=In syncytial embryos, detected at
CC the centrosomes throughout the cell cycle, and in the mitotic spindle
CC and pseudocleavage furrows invaginating from the cell cortex during
CC mitosis. Concentrated at the growing end of membranes during the
CC cellularization process. After cellularization, localized to the
CC centrosomes during mitosis and to the nucleus at the end of telophase.
CC Enriched in the presynaptic side of the neuromuscular junction, with
CC some signal detected also in axonal branches.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=Zygotic; Synonyms=B, C;
CC IsoId=P18431-2; Sequence=Displayed;
CC Name=SGG46; Synonyms=Maternal, D;
CC IsoId=P18431-1; Sequence=VSP_044105;
CC Name=SGG39; Synonyms=A, J;
CC IsoId=P18431-3; Sequence=VSP_044106;
CC Name=G;
CC IsoId=P18431-4; Sequence=VSP_044104;
CC -!- TISSUE SPECIFICITY: Expressed in ovaries and activated eggs (at protein
CC level). Expression is over all the embryo at all stages, no local
CC accumulation is observed. {ECO:0000269|PubMed:2118107,
CC ECO:0000269|PubMed:22421435, ECO:0000269|PubMed:8467811}.
CC -!- DEVELOPMENTAL STAGE: Isoform SGG46 is expressed at low levels in 12-24
CC hours embryos. Isoform Zygotic and isoform SGG39 are expressed in 12-24
CC hours embryos and present throughout the larval, pupal and adult stages
CC (at protein level). Isoform Zygotic is expressed maternally and
CC zygotically but reduced throughout later embryonic development.
CC Expression persists throughout larval stages.
CC {ECO:0000269|PubMed:2118107, ECO:0000269|PubMed:8467811}.
CC -!- DISRUPTION PHENOTYPE: Mutants display an overdeveloped neuromuscular
CC junction (NMJ), with the number of boutons greatly increased.
CC {ECO:0000269|PubMed:15269269}.
CC -!- MISCELLANEOUS: [Isoform Zygotic]: Major isoform.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37952.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA50216.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; X70862; CAA50212.1; -; mRNA.
DR EMBL; X70863; CAA50213.1; -; mRNA.
DR EMBL; X70864; CAA50214.1; -; mRNA.
DR EMBL; X70865; CAA50215.1; -; mRNA.
DR EMBL; X70866; CAA50216.1; ALT_SEQ; mRNA.
DR EMBL; X53332; CAA37419.1; -; mRNA.
DR EMBL; AE014298; AAF45801.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09082.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09083.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65255.1; -; Genomic_DNA.
DR EMBL; AL024485; CAA19676.1; -; Genomic_DNA.
DR EMBL; AL034544; CAA19676.1; JOINED; Genomic_DNA.
DR EMBL; AL121804; CAB65860.1; -; Genomic_DNA.
DR EMBL; AL024485; CAB65860.1; JOINED; Genomic_DNA.
DR EMBL; AL121804; CAB72296.1; -; Genomic_DNA.
DR EMBL; AL024485; CAB72296.1; JOINED; Genomic_DNA.
DR EMBL; AY122193; AAM52705.1; -; mRNA.
DR EMBL; AY119664; AAM50318.1; -; mRNA.
DR EMBL; X54005; CAA37951.1; -; mRNA.
DR EMBL; X54006; CAA37952.1; ALT_FRAME; mRNA.
DR PIR; S35325; S35325.
DR PIR; S35327; S35327.
DR PIR; S35328; S35423.
DR RefSeq; NP_476714.1; NM_057366.5. [P18431-3]
DR RefSeq; NP_476715.1; NM_057367.5. [P18431-2]
DR RefSeq; NP_476716.2; NM_057368.5.
DR RefSeq; NP_599105.1; NM_134278.3. [P18431-2]
DR RefSeq; NP_726822.1; NM_166947.3. [P18431-2]
DR RefSeq; NP_726823.1; NM_166948.4. [P18431-2]
DR RefSeq; NP_996335.1; NM_206612.3. [P18431-4]
DR RefSeq; NP_996336.1; NM_206613.3. [P18431-3]
DR RefSeq; NP_996337.1; NM_206614.3. [P18431-2]
DR RefSeq; NP_996338.1; NM_206615.2. [P18431-2]
DR AlphaFoldDB; P18431; -.
DR SMR; P18431; -.
DR BioGRID; 57779; 186.
DR DIP; DIP-39170N; -.
DR IntAct; P18431; 696.
DR STRING; 7227.FBpp0304140; -.
DR iPTMnet; P18431; -.
DR PaxDb; P18431; -.
DR DNASU; 31248; -.
DR EnsemblMetazoa; FBtr0070466; FBpp0070449; FBgn0003371. [P18431-2]
DR EnsemblMetazoa; FBtr0070467; FBpp0070450; FBgn0003371. [P18431-3]
DR EnsemblMetazoa; FBtr0070468; FBpp0070451; FBgn0003371. [P18431-2]
DR EnsemblMetazoa; FBtr0070469; FBpp0070452; FBgn0003371. [P18431-2]
DR EnsemblMetazoa; FBtr0070470; FBpp0070453; FBgn0003371. [P18431-2]
DR EnsemblMetazoa; FBtr0070472; FBpp0089162; FBgn0003371. [P18431-2]
DR EnsemblMetazoa; FBtr0070473; FBpp0089158; FBgn0003371. [P18431-2]
DR EnsemblMetazoa; FBtr0070474; FBpp0089159; FBgn0003371. [P18431-3]
DR EnsemblMetazoa; FBtr0070475; FBpp0089160; FBgn0003371. [P18431-4]
DR GeneID; 31248; -.
DR KEGG; dme:Dmel_CG2621; -.
DR CTD; 31248; -.
DR FlyBase; FBgn0003371; sgg.
DR VEuPathDB; VectorBase:FBgn0003371; -.
DR eggNOG; KOG0658; Eukaryota.
DR GeneTree; ENSGT00520000055635; -.
DR InParanoid; P18431; -.
DR OMA; EMQYTQC; -.
DR BRENDA; 2.7.11.26; 1994.
DR Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-DME-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-DME-209155; Phosphorylation of AXN and APC.
DR Reactome; R-DME-209159; Assembly of the CI containing complexes.
DR Reactome; R-DME-209190; Phosphorylation of CI.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-209387; Phosphorylation of ARR.
DR Reactome; R-DME-209396; Phosphorylation of ARM.
DR Reactome; R-DME-209413; Assembly of the 'destruction complex'.
DR Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
DR Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-399956; CRMPs in Sema3A signaling.
DR Reactome; R-DME-432553; Phosphorylation of PER and TIM.
DR Reactome; R-DME-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-DME-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR SignaLink; P18431; -.
DR BioGRID-ORCS; 31248; 1 hit in 3 CRISPR screens.
DR ChiTaRS; sgg; fly.
DR GenomeRNAi; 31248; -.
DR PRO; PR:P18431; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003371; Expressed in seminal fluid secreting gland and 13 other tissues.
DR ExpressionAtlas; P18431; baseline and differential.
DR Genevisible; P18431; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0035324; C:female germline ring canal; IDA:UniProtKB.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0008407; P:chaeta morphogenesis; NAS:FlyBase.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0009649; P:entrainment of circadian clock; IMP:FlyBase.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:FlyBase.
DR GO; GO:0090163; P:establishment of epithelial cell planar polarity; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:FlyBase.
DR GO; GO:0046959; P:habituation; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; TAS:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; NAS:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; IDA:FlyBase.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; NAS:UniProtKB.
DR GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0042306; P:regulation of protein import into nucleus; TAS:FlyBase.
DR GO; GO:0030162; P:regulation of proteolysis; IDA:FlyBase.
DR GO; GO:0072347; P:response to anesthetic; IMP:FlyBase.
DR GO; GO:0007622; P:rhythmic behavior; TAS:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0035309; P:wing and notum subfield formation; IMP:FlyBase.
DR CDD; cd14137; STKc_GSK3; 1.
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; IPR039192; STKc_GSK3.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Developmental protein; Kinase; Meiosis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Segmentation polarity protein;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..514
FT /note="Protein kinase shaggy"
FT /id="PRO_0000086641"
FT DOMAIN 54..338
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 379..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 60..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 214
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:8382613"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..29
FT /note="MSGRPRTSSFAEGNKQSPSLVLGGVKTCS -> MLINRGSLLEG (in
FT isoform G)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_044104"
FT VAR_SEQ 1..29
FT /note="MSGRPRTSSFAEGNKQSPSLVLGGVKTCS -> MATTTTTQRAGAAPALNLL
FT PASNNNINNTLINNNNNNNNTSNSNNNNNNVISQPIKIPLTERFSSQTSTGSADSGVIV
FT SSASQQQLQLPPPRSSSGSLSLPQAPPGGKWRQKQQRQQLLLSQDSGIENGVTTRPSKA
FT KDNQGAGKASHNATSSKESGAQSNSSSESLGSNCSEAQEQQRVRASSALELSSVDTPVI
FT VGGVVSGGNSILRSRIKYKSTNSTGTQGFDVEDRIDEVDICDDDDVDCDDRGSEIEEEE
FT EEEEDDGVNVDDDVEEADNQSDNQSGIIINLKSQTEQEEEVDEVDAKPKNRLLPPDQAE
FT LTVAAAMARRRDAKSLATDGHIYFPLLKISEDPHIDSKLINRKDGLQDTMYYLDEFGSP
FT KLREKFARKQKQLLAKQQKQLMKRERRSEEQRKKRNTTVASNLAASGAVVDDTKDDYKQ
FT QPHCDTSSRSKNNSVPNPPSSHLHQNHNHLVVDVQEDVDDVNVVATSDVDSGVVKMRRH
FT SHDNHYDRIPRSNAATITTRPQIDQQSSHHQNTEDVEQGAEPQIDGEADLDADADADSD
FT GSGENVKTAKLARTQSCVSWTKVVQKFKNILG (in isoform SGG46)"
FT /evidence="ECO:0000303|PubMed:2113617,
FT ECO:0000303|PubMed:8467811"
FT /id="VSP_044105"
FT VAR_SEQ 513..514
FT /note="DS -> GSQSNSALNSSGSGGSGNGEAAGSGSGSGSGSGGGNGGDNDAGDSG
FT AIASGGGAAETEAAASG (in isoform SGG39)"
FT /evidence="ECO:0000303|PubMed:8467811"
FT /id="VSP_044106"
FT MUTAGEN 81
FT /note="A->T: Increases the amount of synaptic boutons and
FT microtubule loops when expressed presynaptically."
FT /evidence="ECO:0000269|PubMed:15269269"
FT CONFLICT 244
FT /note="V -> I (in Ref. 2; CAA37419)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="A -> R (in Ref. 7; CAA37952)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="T -> A (in Ref. 2; CAA37419 and 7; AAM50318)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="A -> R (in Ref. 7; CAA37952)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="A -> R (in Ref. 7; CAA37952)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="Missing (in Ref. 7; CAA37952)"
FT /evidence="ECO:0000305"
FT CONFLICT 513..514
FT /note="DS -> GE (in Ref. 5; CAA19676/CAB65860)"
FT /evidence="ECO:0000305"
FT CONFLICT P18431-1:9
FT /note="R -> A (in Ref. 3; AAF45801 and 5; CAA19676/
FT CAB65860)"
FT /evidence="ECO:0000305"
FT CONFLICT P18431-1:256..259
FT /note="EEEE -> E (in Ref. 7; CAA37952)"
FT /evidence="ECO:0000305"
FT CONFLICT P18431-1:258..259
FT /note="EE -> E (in Ref. 5; CAA19676/CAB65860)"
FT /evidence="ECO:0000305"
FT CONFLICT P18431-1:539..540
FT /note="AD -> RI (in Ref. 7; CAA37952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 53872 MW; 193EE2A1294BE494 CRC64;
MSGRPRTSSF AEGNKQSPSL VLGGVKTCSR DGSKITTVVA TPGQGTDRVQ EVSYTDTKVI
GNGSFGVVFQ AKLCDTGELV AIKKVLQDRR FKNRELQIMR KLEHCNIVKL LYFFYSSGEK
RDEVFLNLVL EYIPETVYKV ARQYAKTKQT IPINFIRLYM YQLFRSLAYI HSLGICHRDI
KPQNLLLDPE TAVLKLCDFG SAKQLLHGEP NVSYICSRYY RAPELIFGAI NYTTKIDVWS
AGCVLAELLL GQPIFPGDSG VDQLVEVIKV LGTPTREQIR EMNPNYTEFK FPQIKSHPWQ
KVFRIRTPTE AINLVSLLLE YTPSARITPL KACAHPFFDE LRMEGNHTLP NGRDMPPLFN
FTEHELSIQP SLVPQLLPKH LQNASGPGGN RPSAGGAASI AASGSTSVSS TGSGASVEGS
AQPQSQGTAA AAGSGSGGAT AGTGGASAGG PGSGNNSSSG GASGAPSAVA AGGANAAVAG
GAGGGGGAGA ATAAATATGA IGATNAGGAN VTDS
