ID   GSK3H_DROME             Reviewed;         501 AA.
AC   P83101;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Putative glycogen synthase kinase-3 homolog;
DE            Short=GSK-3;
DE            EC=2.7.11.26;
DE   AltName: Full=Protein gasket;
GN   Name=gskt; ORFNames=CG31003;
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 [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   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Testis;
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26;
CC   -!- PTM: Phosphorylation on Tyr-193 is necessary for the activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR   EMBL; AE014297; AAN14270.1; -; Genomic_DNA.
DR   EMBL; BT001338; AAN71093.1; -; mRNA.
DR   RefSeq; NP_733426.1; NM_170547.3.
DR   AlphaFoldDB; P83101; -.
DR   SMR; P83101; -.
DR   BioGRID; 76872; 2.
DR   IntAct; P83101; 2.
DR   STRING; 7227.FBpp0085145; -.
DR   PaxDb; 7227-FBpp0085145; -.
DR   DNASU; 318552; -.
DR   EnsemblMetazoa; FBtr0085784; FBpp0085145; FBgn0046332.
DR   GeneID; 318552; -.
DR   KEGG; dme:Dmel_CG31003; -.
DR   UCSC; CG31003-RA; d. melanogaster.
DR   AGR; FB:FBgn0046332; -.
DR   CTD; 318552; -.
DR   FlyBase; FBgn0046332; gskt.
DR   VEuPathDB; VectorBase:FBgn0046332; -.
DR   eggNOG; KOG0658; Eukaryota.
DR   GeneTree; ENSGT00520000055635; -.
DR   HOGENOM; CLU_000288_181_20_1; -.
DR   InParanoid; P83101; -.
DR   OMA; LKPHPWS; -.
DR   OrthoDB; 2872909at2759; -.
DR   PhylomeDB; P83101; -.
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-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-DME-399956; CRMPs in Sema3A signaling.
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; P83101; -.
DR   BioGRID-ORCS; 318552; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 318552; -.
DR   PRO; PR:P83101; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0046332; Expressed in testis and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase.
DR   GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048232; P:male gamete generation; IMP:FlyBase.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
DR   CDD; cd14137; STKc_GSK3; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24057; GLYCOGEN SYNTHASE KINASE-3 ALPHA; 1.
DR   PANTHER; PTHR24057:SF0; PROTEIN KINASE SHAGGY-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; P83101; DM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..501
FT                   /note="Putative glycogen synthase kinase-3 homolog"
FT                   /id="PRO_0000085984"
FT   DOMAIN          33..317
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          355..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..470
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..501
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         39..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         193
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  56237 MW;  949DBCADBD72A2C9 CRC64;
     MASQSKNSGL TNKVTTVVAT NAFGADVMSE ISYTDAKVVG NGSFGVVFQA KMVPSNEMVA
     IKKVLQDRRF KNRELQIMRK LRHDNIITLK WFFFSSGEKR DEVYLNLVME FLPETLYKVE
     RQYARAKQTL PVNFVRLYMY QLLRSMGYLH SLGFCHRDIK PQNMLLDSET GVLKLCDFGS
     AKQLISGEPN VSYICSRYYR APELIFGSTD YTTKIDMWSA GCVMSELLLG QLIFPGDSGV
     DQIVEIVKVM GTPTSEQLHD MNPHYKQFKL PELKPHPWSK VFRIRTPAEA IDLVSKMLIY
     SPNARVSPLM GCAHPFFDEL RQDPHQQLPN GRSLPPLFNF TDYEKTIEPD TMPLLLPRAQ
     GSSTTKEPSA AHRNRNTAGE ESPRKTEDSQ KPATAALSKS PGPSGKALES PPGFLQHDLG
     NGDHVAVGTM PMEPLTLEQN HFAAESYAVG EDAEDNLEED VGDENDYDYD DGGQCNSTYI
     SDDMDEASES DDDDFEEEDE N
//