GSK3B_MOUSE
ID GSK3B_MOUSE Reviewed; 420 AA.
AC Q9WV60;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Glycogen synthase kinase-3 beta;
DE Short=GSK-3 beta;
DE EC=2.7.11.26 {ECO:0000250|UniProtKB:P49841};
DE AltName: Full=Serine/threonine-protein kinase GSK3B;
DE EC=2.7.11.1 {ECO:0000269|PubMed:22539723};
GN Name=Gsk3b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Salameh W.A., Guo T.B., Chan K.C., Mitchell A.P.;
RT "Testicular expression and hormonal control of glycogen synthase kinase 3,
RT a homologue of yeast RIM11.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10894547; DOI=10.1038/35017574;
RA Hoeflich K.P., Luo J., Rubie E.A., Tsao M.S., Jin O., Woodgett J.R.;
RT "Requirement for glycogen synthase kinase-3beta in cell survival and NF-
RT kappaB activation.";
RL Nature 406:86-90(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP INTERACTION WITH ARRB2.
RX PubMed=16051150; DOI=10.1016/j.cell.2005.05.012;
RA Beaulieu J.-M., Sotnikova T.D., Marion S., Lefkowitz R.J.,
RA Gainetdinov R.R., Caron M.G.;
RT "An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic
RT neurotransmission and behavior.";
RL Cell 122:261-273(2005).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF SER-9.
RX PubMed=15791206; DOI=10.1038/sj.emboj.7600633;
RA McManus E.J., Sakamoto K., Armit L.J., Ronaldson L., Shpiro N., Marquez R.,
RA Alessi D.R.;
RT "Role that phosphorylation of GSK3 plays in insulin and Wnt signalling
RT defined by knockin analysis.";
RL EMBO J. 24:1571-1583(2005).
RN [7]
RP FUNCTION IN MCL1 PHOSPHORYLATION.
RX PubMed=16543145; DOI=10.1016/j.molcel.2006.02.009;
RA Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R.;
RT "Glycogen synthase kinase-3 regulates mitochondrial outer membrane
RT permeabilization and apoptosis by destabilization of MCL-1.";
RL Mol. Cell 21:749-760(2006).
RN [8]
RP FUNCTION IN AXON FORMATION.
RX PubMed=17391670; DOI=10.1016/j.febslet.2007.03.018;
RA Garrido J.J., Simon D., Varea O., Wandosell F.;
RT "GSK3 alpha and GSK3 beta are necessary for axon formation.";
RL FEBS Lett. 581:1579-1586(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP FUNCTION IN REGULATION OF PANCREATIC BETA-CELLS.
RX PubMed=18288891; DOI=10.1371/journal.pbio.0060037;
RA Tanabe K., Liu Z., Patel S., Doble B.W., Li L., Cras-Meneur C.,
RA Martinez S.C., Welling C.M., White M.F., Bernal-Mizrachi E., Woodgett J.R.,
RA Permutt M.A.;
RT "Genetic deficiency of glycogen synthase kinase-3beta corrects diabetes in
RT mouse models of insulin resistance.";
RL PLoS Biol. 6:E37-E37(2008).
RN [11]
RP INTERACTION WITH DISC1.
RX PubMed=19303846; DOI=10.1016/j.cell.2008.12.044;
RA Mao Y., Ge X., Frank C.L., Madison J.M., Koehler A.N., Doud M.K., Tassa C.,
RA Berry E.M., Soda T., Singh K.K., Biechele T., Petryshen T.L., Moon R.T.,
RA Haggarty S.J., Tsai L.H.;
RT "Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation
RT via modulation of GSK3beta/beta-catenin signaling.";
RL Cell 136:1017-1031(2009).
RN [12]
RP INTERACTION WITH AXIN1 AND ZBED3, AND MUTAGENESIS OF LYS-85.
RX PubMed=19141611; DOI=10.1074/jbc.m807753200;
RA Chen T., Li M., Ding Y., Zhang L.S., Xi Y., Pan W.J., Tao D.L., Wang J.Y.,
RA Li L.;
RT "Identification of zinc-finger BED domain-containing 3 (Zbed3) as a novel
RT Axin-interacting protein that activates Wnt/beta-catenin signaling.";
RL J. Biol. Chem. 284:6683-6689(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION.
RX PubMed=20123978; DOI=10.1128/mcb.01047-09;
RA Kurabayashi N., Hirota T., Sakai M., Sanada K., Fukada Y.;
RT "DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism
RT directing proteasomal degradation of CRY2 for circadian timekeeping.";
RL Mol. Cell. Biol. 30:1757-1768(2010).
RN [15]
RP FUNCTION, AND INTERACTION WITH ARNTL/BMAL1.
RX PubMed=20049328; DOI=10.1371/journal.pone.0008561;
RA Sahar S., Zocchi L., Kinoshita C., Borrelli E., Sassone-Corsi P.;
RT "Regulation of BMAL1 protein stability and circadian function by GSK3beta-
RT mediated phosphorylation.";
RL PLoS ONE 5:E8561-E8561(2010).
RN [16]
RP FUNCTION.
RX PubMed=21295697; DOI=10.1016/j.cell.2010.12.033;
RA Wu X., Shen Q.T., Oristian D.S., Lu C.P., Zheng Q., Wang H.W., Fuchs E.;
RT "Skin stem cells orchestrate directional migration by regulating
RT microtubule-ACF7 connections through GSK3beta.";
RL Cell 144:341-352(2011).
RN [17]
RP FUNCTION IN PHOSPHORYLATION OF DPYSL2, PHOSPHORYLATION AT SER-9, AND
RP MUTAGENESIS OF SER-9.
RX PubMed=22057101; DOI=10.1038/ncb2373;
RA Wakatsuki S., Saitoh F., Araki T.;
RT "ZNRF1 promotes Wallerian degeneration by degrading AKT to induce GSK3B-
RT dependent CRMP2 phosphorylation.";
RL Nat. Cell Biol. 13:1415-1423(2011).
RN [18]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22539723; DOI=10.1126/science.1217032;
RA Lin S.Y., Li T.Y., Liu Q., Zhang C., Li X., Chen Y., Zhang S.M., Lian G.,
RA Liu Q., Ruan K., Wang Z., Zhang C.S., Chien K.Y., Wu J., Li Q., Han J.,
RA Lin S.C.;
RT "GSK3-TIP60-ULK1 signaling pathway links growth factor deprivation to
RT autophagy.";
RL Science 336:477-481(2012).
RN [19]
RP FUNCTION, AND PHOSPHORYLATION AT SER-9.
RX PubMed=23395175; DOI=10.1016/j.cmet.2012.12.017;
RA Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K.,
RA Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.;
RT "Glucose sensor O-GlcNAcylation coordinates with phosphorylation to
RT regulate circadian clock.";
RL Cell Metab. 17:291-302(2013).
RN [20]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=28556462; DOI=10.1002/hipo.22739;
RA Besing R.C., Rogers C.O., Paul J.R., Hablitz L.M., Johnson R.L.,
RA McMahon L.L., Gamble K.L.;
RT "GSK3 activity regulates rhythms in hippocampal clock gene expression and
RT synaptic plasticity.";
RL Hippocampus 27:890-898(2017).
RN [21]
RP FUNCTION, AND INTERACTION WITH ARNTL AND PIWIL2.
RX PubMed=28903391; DOI=10.18632/oncotarget.18973;
RA Lu Y., Zheng X., Hu W., Bian S., Zhang Z., Tao D., Liu Y., Ma Y.;
RT "Cancer/testis antigen PIWIL2 suppresses circadian rhythms by regulating
RT the stability and activity of BMAL1 and CLOCK.";
RL Oncotarget 8:54913-54924(2017).
RN [22]
RP INTERACTION WITH LMBR1L.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: Constitutively active protein kinase that acts as a negative
CC regulator in the hormonal control of glucose homeostasis, Wnt signaling
CC and regulation of transcription factors and microtubules, by
CC phosphorylating and inactivating glycogen synthase (GYS1 or GYS2),
CC EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN,
CC NFATC1/NFATC, MAPT/TAU and MACF1 (PubMed:15791206, PubMed:22057101,
CC PubMed:23395175). Requires primed phosphorylation of the majority of
CC its substrates (PubMed:15791206, PubMed:22057101, PubMed:23395175). In
CC skeletal muscle, contributes to insulin regulation of glycogen
CC synthesis by phosphorylating and inhibiting GYS1 activity and hence
CC glycogen synthesis (By similarity). May also mediate the development of
CC insulin resistance by regulating activation of transcription factors
CC (By similarity). Regulates protein synthesis by controlling the
CC activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as
CC glycogen synthase (By similarity). In Wnt signaling, GSK3B forms a
CC multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and
CC phosphorylates the N-terminus of CTNNB1 leading to its degradation
CC mediated by ubiquitin/proteasomes (By similarity). Phosphorylates JUN
CC at sites proximal to its DNA-binding domain, thereby reducing its
CC affinity for DNA (By similarity). Phosphorylates NFATC1/NFATC on
CC conserved serine residues promoting NFATC1/NFATC nuclear export,
CC shutting off NFATC1/NFATC gene regulation, and thereby opposing the
CC action of calcineurin (By similarity). Phosphorylates MAPT/TAU on 'Thr-
CC 548', decreasing significantly MAPT/TAU ability to bind and stabilize
CC microtubules (By similarity). MAPT/TAU is the principal component of
CC neurofibrillary tangles in Alzheimer disease (By similarity). Plays an
CC important role in ERBB2-dependent stabilization of microtubules at the
CC cell cortex (By similarity). Phosphorylates MACF1, inhibiting its
CC binding to microtubules which is critical for its role in bulge stem
CC cell migration and skin wound repair (PubMed:21295697). Probably
CC regulates NF-kappa-B (NFKB1) at the transcriptional level and is
CC required for the NF-kappa-B-mediated anti-apoptotic response to TNF-
CC alpha (TNF/TNFA) (PubMed:10894547). Negatively regulates replication in
CC pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and
CC diabetes (PubMed:18288891). Through phosphorylation of the anti-
CC apoptotic protein MCL1, may control cell apoptosis in response to
CC growth factors deprivation (PubMed:16543145). Phosphorylates MUC1 in
CC breast cancer cells, decreasing the interaction of MUC1 with
CC CTNNB1/beta-catenin (By similarity). Is necessary for the establishment
CC of neuronal polarity and axon outgrowth (PubMed:17391670).
CC Phosphorylates MARK2, leading to inhibition of its activity (By
CC similarity). Phosphorylates SIK1 at 'Thr-182', leading to sustainment
CC of its activity (By similarity). Phosphorylates ZC3HAV1 which enhances
CC its antiviral activity (By similarity). Phosphorylates SNAI1, leading
CC to its BTRC-triggered ubiquitination and proteasomal degradation (By
CC similarity). Phosphorylates SFPQ at 'Thr-687' upon T-cell activation
CC (By similarity). Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and
CC stabilizes it by protecting it from proteasomal degradation (By
CC similarity). Regulates the circadian clock via phosphorylation of the
CC major clock components including ARNTL/BMAL1, CLOCK and PER2
CC (PubMed:20049328, PubMed:28556462, PubMed:28903391, PubMed:20123978).
CC Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal
CC degradation (By similarity). Phosphorylates ARNTL/BMAL1 at 'Ser-17' and
CC 'Ser-21' and primes it for ubiquitination and proteasomal degradation
CC (PubMed:20049328, PubMed:28903391). Phosphorylates OGT at 'Ser-3' or
CC 'Ser-4' which positively regulates its activity (By similarity).
CC Phosphorylates MYCN in neuroblastoma cells which may promote its
CC degradation (By similarity). Regulates the circadian rhythmicity of
CC hippocampal long-term potentiation and ARNTL/BMLA1 and PER2 expression
CC (PubMed:28556462). Acts as a regulator of autophagy by mediating
CC phosphorylation of KAT5/TIP60 under starvation conditions, activating
CC KAT5/TIP60 acetyltransferase activity and promoting acetylation of key
CC autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:22539723).
CC Negatively regulates extrinsic apoptotic signaling pathway via death
CC domain receptors (By similarity). Promotes the formation of an anti-
CC apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors,
CC including TNFRSF10B (By similarity). The anti-apoptotic function is
CC most effective with weak apoptotic signals and can be overcome by
CC stronger stimulation (By similarity). Phosphorylates E2F1, promoting
CC the interaction between E2F1 and USP11, stabilizing E2F1 and promoting
CC its activity (By similarity). {ECO:0000250|UniProtKB:P18266,
CC ECO:0000250|UniProtKB:P49841, ECO:0000269|PubMed:10894547,
CC ECO:0000269|PubMed:15791206, ECO:0000269|PubMed:16543145,
CC ECO:0000269|PubMed:17391670, ECO:0000269|PubMed:18288891,
CC ECO:0000269|PubMed:20049328, ECO:0000269|PubMed:20123978,
CC ECO:0000269|PubMed:21295697, ECO:0000269|PubMed:22057101,
CC ECO:0000269|PubMed:22539723, ECO:0000269|PubMed:23395175,
CC ECO:0000269|PubMed:28556462, ECO:0000269|PubMed:28903391}.
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 Evidence={ECO:0000250|UniProtKB:P49841};
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; Evidence={ECO:0000250|UniProtKB:P49841};
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:22539723};
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:0000250|UniProtKB:P49841};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation at Tyr-216. In
CC response to insulin, inhibited by phosphorylation at Ser-9 by PKB/AKT1
CC and RPS6KA3; phosphorylation at this site causes a conformational
CC change, preventing access of substrates to the active site. Inhibited
CC by lithium.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with DAB2IP (via C2
CC domain); the interaction stimulates GSK3B kinase activation (By
CC similarity). Interacts (via C2 domain) with PPP2CA (By similarity).
CC Interacts with CABYR, MMP2, MUC1, NIN and PRUNE1 (By similarity).
CC Interacts with AXIN1; the interaction mediates hyperphosphorylation of
CC CTNNB1 leading to its ubiquitination and destruction (PubMed:19141611).
CC Interacts with and phosphorylates SNAI1 (By similarity). Interacts with
CC DNM1L (via a C-terminal domain) (By similarity). Interacts with ARRB2
CC (PubMed:16051150). Interacts with DISC1 (PubMed:19303846). Found in a
CC complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (By
CC similarity). Interacts with SGK3 (By similarity). Interacts with the
CC CLOCK-ARNTL/BMAL1 heterodimer (By similarity). Interacts with ZBED3
CC (PubMed:19141611). Interacts with the ARNTL/BMAL1 (PubMed:20049328,
CC PubMed:28903391). The complex composed, at least, of APC, CTNNB1 and
CC GSK3B interacts with JPT1; the interaction requires the inactive form
CC of GSK3B (phosphorylated at 'Ser-9') (By similarity). Forms a complex
CC composed of PRKAR2A or PRKAR2B, GSK3B and GSKIP through GSKIP
CC interaction; facilitates PKA-induced phosphorylation and regulates
CC GSK3B activity (By similarity). Interacts with GSKIP (By similarity).
CC Interacts with GID8 (By similarity). Interacts with PIWIL2
CC (PubMed:28903391). Interacts with LMBR1L (PubMed:31073040). Interacts
CC with DDX3X (By similarity). Interacts with BIRC2 (By similarity).
CC Interacts with TNFRSF10B; TNFRSF10B stimulation inhibits GSK3B kinase
CC activity (By similarity). {ECO:0000250|UniProtKB:P49841,
CC ECO:0000269|PubMed:16051150, ECO:0000269|PubMed:19141611,
CC ECO:0000269|PubMed:19303846, ECO:0000269|PubMed:20049328,
CC ECO:0000269|PubMed:28903391, ECO:0000269|PubMed:31073040}.
CC -!- INTERACTION:
CC Q9WV60; Q02248: Ctnnb1; NbExp=2; IntAct=EBI-400793, EBI-397872;
CC Q9WV60; Q9WUA5: Epm2a; NbExp=2; IntAct=EBI-400793, EBI-1040928;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49841}. Nucleus
CC {ECO:0000250|UniProtKB:P49841}. Cell membrane
CC {ECO:0000250|UniProtKB:P49841}. Note=The phosphorylated form shows
CC localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1
CC signaling pathway controls localization of the phosphorylated form to
CC the cell membrane (By similarity). {ECO:0000250|UniProtKB:P49841}.
CC -!- PTM: Phosphorylated by AKT1 and ILK1. Upon insulin-mediated signaling,
CC the activated PKB/AKT1 protein kinase phosphorylates and deactivates
CC GSK3B, resulting in the dephosphorylation and activation of GYS1.
CC Activated by phosphorylation at Tyr-216. Phosphorylation of Ser-9 in
CC the hippocampus peaks at CT0, whereas in the liver it peaks at CT12.
CC Inactivated by phosphorylation at Ser-9 (By similarity). Phosphorylated
CC in a circadian manner in the hippocampus (PubMed:28556462).
CC {ECO:0000250|UniProtKB:P49841, ECO:0000269|PubMed:22057101,
CC ECO:0000269|PubMed:23395175, ECO:0000269|PubMed:28556462}.
CC -!- PTM: Mono-ADP-ribosylation by PARP10 negatively regulates kinase
CC activity. {ECO:0000250|UniProtKB:P49841}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality at 16 dpc due to hepatocyte
CC apoptosis. {ECO:0000269|PubMed:10894547}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF156099; AAD39258.2; -; mRNA.
DR EMBL; BC006936; AAH06936.1; -; mRNA.
DR EMBL; BC060743; AAH60743.1; -; mRNA.
DR CCDS; CCDS28163.1; -.
DR RefSeq; NP_062801.1; NM_019827.6.
DR PDB; 4NU1; X-ray; 2.50 A; A=1-383.
DR PDB; 5AIR; X-ray; 2.53 A; A/B=4-420.
DR PDB; 6AE3; X-ray; 2.14 A; A/B/C/D=1-420.
DR PDBsum; 4NU1; -.
DR PDBsum; 5AIR; -.
DR PDBsum; 6AE3; -.
DR AlphaFoldDB; Q9WV60; -.
DR SMR; Q9WV60; -.
DR BioGRID; 208115; 101.
DR ComplexPortal; CPX-103; Beta-catenin destruction core complex, variant 1.
DR ComplexPortal; CPX-108; Nuclear export complex Frat1-Gsk3b.
DR ComplexPortal; CPX-110; Nuclear export complex Frat2-Gsk3b.
DR ComplexPortal; CPX-448; Beta-catenin destruction core complex, variant 2.
DR ComplexPortal; CPX-449; Beta-catenin destruction core complex, variant 3.
DR ComplexPortal; CPX-452; Beta-catenin destruction core complex, variant 4.
DR ComplexPortal; CPX-464; Nuclear export complex Frat3-Gsk3b.
DR CORUM; Q9WV60; -.
DR DIP; DIP-32446N; -.
DR ELM; Q9WV60; -.
DR IntAct; Q9WV60; 54.
DR MINT; Q9WV60; -.
DR STRING; 10090.ENSMUSP00000023507; -.
DR BindingDB; Q9WV60; -.
DR ChEMBL; CHEMBL1075321; -.
DR iPTMnet; Q9WV60; -.
DR PhosphoSitePlus; Q9WV60; -.
DR EPD; Q9WV60; -.
DR jPOST; Q9WV60; -.
DR MaxQB; Q9WV60; -.
DR PaxDb; Q9WV60; -.
DR PRIDE; Q9WV60; -.
DR ProteomicsDB; 270899; -.
DR Antibodypedia; 4266; 1408 antibodies from 53 providers.
DR DNASU; 56637; -.
DR Ensembl; ENSMUST00000023507; ENSMUSP00000023507; ENSMUSG00000022812.
DR GeneID; 56637; -.
DR KEGG; mmu:56637; -.
DR UCSC; uc007zen.1; mouse.
DR CTD; 2932; -.
DR MGI; MGI:1861437; Gsk3b.
DR VEuPathDB; HostDB:ENSMUSG00000022812; -.
DR eggNOG; KOG0658; Eukaryota.
DR GeneTree; ENSGT00520000055635; -.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q9WV60; -.
DR OMA; EMQYTQC; -.
DR PhylomeDB; Q9WV60; -.
DR TreeFam; TF101104; -.
DR BRENDA; 2.7.11.26; 3474.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR BioGRID-ORCS; 56637; 13 hits in 76 CRISPR screens.
DR ChiTaRS; Gsk3b; mouse.
DR PRO; PR:Q9WV60; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9WV60; protein.
DR Bgee; ENSMUSG00000022812; Expressed in spermatid and 248 other tissues.
DR ExpressionAtlas; Q9WV60; baseline and differential.
DR Genevisible; Q9WV60; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030877; C:beta-catenin destruction complex; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043227; C:membrane-bounded organelle; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:1990909; C:Wnt signalosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR GO; GO:0034452; F:dynactin binding; ISO:MGI.
DR GO; GO:0070840; F:dynein complex binding; IPI:CAFA.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR GO; GO:0050321; F:tau-protein kinase activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0048675; P:axon extension; IGI:MGI.
DR GO; GO:0007409; P:axonogenesis; IGI:MGI.
DR GO; GO:1904886; P:beta-catenin destruction complex disassembly; ISO:MGI.
DR GO; GO:0046849; P:bone remodeling; ISO:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IGI:ARUK-UCL.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
DR GO; GO:0036016; P:cellular response to interleukin-3; IDA:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0006983; P:ER overload response; IDA:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
DR GO; GO:0035733; P:hepatic stellate cell activation; ISO:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; ISO:MGI.
DR GO; GO:0021766; P:hippocampus development; ISO:MGI.
DR GO; GO:0044027; P:hypermethylation of CpG island; IMP:BHF-UCL.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:CAFA.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:CACAO.
DR GO; GO:0030011; P:maintenance of cell polarity; ISO:MGI.
DR GO; GO:0007520; P:myoblast fusion; IDA:MGI.
DR GO; GO:0014902; P:myotube differentiation; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:1905240; P:negative regulation of canonical Wnt signaling pathway involved in osteoblast differentiation; ISO:MGI.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IDA:MGI.
DR GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:1904339; P:negative regulation of dopaminergic neuron differentiation; ISO:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:2000740; P:negative regulation of mesenchymal stem cell differentiation; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISS:UniProtKB.
DR GO; GO:0014043; P:negative regulation of neuron maturation; IGI:MGI.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:MGI.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISO:MGI.
DR GO; GO:1901984; P:negative regulation of protein acetylation; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; IMP:CAFA.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; ISO:MGI.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IGI:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0106027; P:neuron projection organization; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IGI:MGI.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IMP:BHF-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0010822; P:positive regulation of mitochondrion organization; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0033690; P:positive regulation of osteoblast proliferation; ISO:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
DR GO; GO:0090290; P:positive regulation of osteoclast proliferation; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IGI:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:MGI.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; ISO:MGI.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; IMP:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:MGI.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
DR GO; GO:0035372; P:protein localization to microtubule; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0000320; P:re-entry into mitotic cell cycle; IDA:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:0030516; P:regulation of axon extension; ISO:MGI.
DR GO; GO:0050770; P:regulation of axonogenesis; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IMP:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:BHF-UCL.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0150101; P:regulation of microtubule anchoring at centrosome; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0032886; P:regulation of microtubule-based process; IDA:UniProtKB.
DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; ISO:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IGI:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0046825; P:regulation of protein export from nucleus; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0010043; P:response to zinc ion; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR GO; GO:0071109; P:superior temporal gyrus development; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
DR CDD; cd14137; STKc_GSK3; 1.
DR IDEAL; IID50236; -.
DR InterPro; IPR033573; GSK3B.
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:SF8; PTHR24057:SF8; 1.
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 3D-structure; ADP-ribosylation; ATP-binding; Biological rhythms;
KW Carbohydrate metabolism; Cell membrane; Cytoplasm; Developmental protein;
KW Differentiation; Glycogen metabolism; Kinase; Membrane; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Signal transduction inhibitor;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..420
FT /note="Glycogen synthase kinase-3 beta"
FT /id="PRO_0000085981"
FT DOMAIN 56..340
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 62..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 9
FT /note="Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3"
FT /evidence="ECO:0000269|PubMed:22057101,
FT ECO:0000269|PubMed:23395175"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49841"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MUTAGEN 9
FT /note="S->A: Loss of phosphorylation; No inhibition of
FT activity and constitutively active."
FT /evidence="ECO:0000269|PubMed:15791206,
FT ECO:0000269|PubMed:22057101"
FT MUTAGEN 85
FT /note="K->R: Inhibits interaction with AXIN1 and ZBED3."
FT /evidence="ECO:0000269|PubMed:19141611"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5AIR"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:6AE3"
FT STRAND 52..64
FT /evidence="ECO:0007829|PDB:6AE3"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:6AE3"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6AE3"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:6AE3"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:6AE3"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5AIR"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 155..173
FT /evidence="ECO:0007829|PDB:6AE3"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6AE3"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6AE3"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6AE3"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 237..252
FT /evidence="ECO:0007829|PDB:6AE3"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4NU1"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:6AE3"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6AE3"
SQ SEQUENCE 420 AA; 46710 MW; 200C3FD1B38B4883 CRC64;
MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK
VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG
EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR
DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV
WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP
WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF
NFTTQELSSN PPLATILIPP HARIQAAASP PANATAASDT NAGDRGQTNN AASASASNST
