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Glycogen synthase kinase-3 (GSK-3) (EC 2.7.11.26)

 GSK3_DICDI              Reviewed;         467 AA.
P51136; Q55A28; Q86KY0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
07-JUN-2017, entry version 124.
RecName: Full=Glycogen synthase kinase-3;
Short=GSK-3;
EC=2.7.11.26;
Name=gskA; Synonyms=gsk3; ORFNames=DDB_G0272110;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=AX2;
PubMed=7813009; DOI=10.1016/0092-8674(95)90458-1;
Harwood A.J., Plyte S.E., Woodgett J., Strutt H., Kay R.R.;
"Glycogen synthase kinase 3 regulates cell fate in Dictyostelium.";
Cell 80:139-148(1995).
[2]
SEQUENCE REVISION.
Harwood A.J., Plyte S.E., Woodgett J., Strutt H., Kay R.R.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=12097910; DOI=10.1038/nature00847;
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
Platzer M., Rosenthal A., Noegel A.A.;
"Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
Nature 418:79-85(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[5]
CATALYTIC ACTIVITY, AND INHIBITION BY LITHIUM.
PubMed=9169052; DOI=10.1006/dbio.1997.8552;
Hedgepeth C.M., Conrad L.J., Zhang J., Huang H.-C., Lee V.M.Y.,
Klein P.S.;
"Activation of the Wnt signaling pathway: a molecular mechanism for
lithium action.";
Dev. Biol. 185:82-91(1997).
[6]
FUNCTION.
PubMed=9284050; DOI=10.1101/gad.11.16.2112;
Ginsburg G.T., Kimmel A.R.;
"Autonomous and nonautonomous regulation of axis formation by
antagonistic signaling via 7-span cAMP receptors and GSK3 in
Dictyostelium.";
Genes Dev. 11:2112-2123(1997).
[7]
CATALYTIC ACTIVITY, AND INHIBITION BY LITHIUM.
PubMed=9784196; DOI=10.1006/abio.1998.2832;
Ryves W.J., Fryer L., Dale T., Harwood A.J.;
"An assay for glycogen synthase kinase 3 (GSK-3) for use in crude cell
extracts.";
Anal. Biochem. 264:124-127(1998).
[8]
FUNCTION.
PubMed=10571182; DOI=10.1016/S0092-8674(00)81526-3;
Kim L., Liu J., Kimmel A.R.;
"The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate
specification.";
Cell 99:399-408(1999).
[9]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=9847246;
Plyte S.E., O'Donovan E., Woodgett J.R., Harwood A.J.;
"Glycogen synthase kinase-3 (GSK-3) is regulated during Dictyostelium
development via the serpentine receptor cAR3.";
Development 126:325-333(1999).
[10]
CATALYTIC ACTIVITY, COFACTOR REQUIREMENT, AND INHIBITION BY LITHIUM.
PubMed=11162580; DOI=10.1006/bbrc.2000.4169;
Ryves W.J., Harwood A.J.;
"Lithium inhibits glycogen synthase kinase-3 by competition for
magnesium.";
Biochem. Biophys. Res. Commun. 280:720-725(2001).
[11]
FUNCTION, MUTAGENESIS OF LYS-85; LYS-86; TYR-214 AND TYR-220, AND
PHOSPHORYLATION AT TYR-214 AND TYR-220.
PubMed=12408804; DOI=10.1016/S1534-5807(02)00269-1;
Kim L., Harwood A.J., Kimmel A.R.;
"Receptor-dependent and tyrosine phosphatase-mediated inhibition of
GSK3 regulates cell fate choice.";
Dev. Cell 3:523-532(2002).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15342480; DOI=10.1242/dev.01330;
Schilde C., Araki T., Williams H., Harwood A.J., Williams J.G.;
"GSK3 is a multifunctional regulator of Dictyostelium development.";
Development 131:4555-4565(2004).
[13]
FUNCTION.
PubMed=21205787; DOI=10.1242/dev.055335;
Kim L., Brzostowski J., Majithia A., Lee N.S., McMains V.,
Kimmel A.R.;
"Combinatorial cell-specific regulation of GSK3 directs cell
differentiation and polarity in Dictyostelium.";
Development 138:421-430(2011).
-!- FUNCTION: During cellular differentiation, may mediate an
extracellular cyclic AMP stimulated signal transduction pathway
that regulates prespore and prestalk B-cell proportions through
inhibition of stalk cell formation and induction of prespore cell
differentiation. The cAMP receptor carC appears to activate gskA
via the tyrosine kinases zakA and zak2, to stimulate prespore
differentiation, while carD appears to negatively regulate gskA,
to promote prestalk formation. {ECO:0000269|PubMed:10571182,
ECO:0000269|PubMed:12408804, ECO:0000269|PubMed:15342480,
ECO:0000269|PubMed:21205787, ECO:0000269|PubMed:7813009,
ECO:0000269|PubMed:9284050, ECO:0000269|PubMed:9847246}.
-!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
phosphate. {ECO:0000269|PubMed:11162580,
ECO:0000269|PubMed:9169052, ECO:0000269|PubMed:9784196}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11162580};
-!- ENZYME REGULATION: Inhibited by lithium. Lithium inhibition is
competitive with respect to magnesium but non-competitive with
respect to the peptide substrate.
-!- DEVELOPMENTAL STAGE: Expressed in growing cells and throughout
development. Levels increase during mound formation (12 hours) and
peak at approximately twice the level seen in growing cells before
decreasing again at the start of culmination (16 hours).
{ECO:0000269|PubMed:9847246}.
-!- DISRUPTION PHENOTYPE: Cells grow normally in both axenic medium
and with bacteria. Under starvation conditions, mutants lacking
gskA aggregate more quickly and form smaller mounds than wild
type, fail to form slugs and take longer than wild type to reach
culmination. At culmination, mutants lacking gskA form abnormal
fruiting bodies characterized by an unusually large mound-like
basal disk. Prestalk B (pstB) cells are formed at the expense of
prespore cells, and the proportion of gskA null cells that
differentiate into spores is greatly reduced when compared to
wild-type cells. {ECO:0000269|PubMed:15342480,
ECO:0000269|PubMed:7813009}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L34674; AAA65968.2; -; mRNA.
EMBL; AAFI02000008; EAL71207.1; -; Genomic_DNA.
PIR; A55476; A55476.
RefSeq; XP_645156.1; XM_640064.1.
ProteinModelPortal; P51136; -.
SMR; P51136; -.
STRING; 44689.DDB0185150; -.
BindingDB; P51136; -.
ChEMBL; CHEMBL2311226; -.
iPTMnet; P51136; -.
PaxDb; P51136; -.
EnsemblProtists; EAL71207; EAL71207; DDB_G0272110.
GeneID; 8618327; -.
KEGG; ddi:DDB_G0272110; -.
dictyBase; DDB_G0272110; gskA.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
InParanoid; P51136; -.
KO; K03083; -.
OMA; FDELRCP; -.
PhylomeDB; P51136; -.
BRENDA; 2.7.11.26; 1939.
Reactome; R-DDI-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:P51136; -.
Proteomes; UP000002195; Chromosome 2.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0072686; C:mitotic spindle; IDA:dictyBase.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:dictyBase.
GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:dictyBase.
GO; GO:0030154; P:cell differentiation; IMP:dictyBase.
GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
GO; GO:0031154; P:culmination involved in sorocarp development; IMP:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
GO; GO:0007275; P:multicellular organism development; IMP:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:dictyBase.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:dictyBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IMP:dictyBase.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:dictyBase.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0060176; P:regulation of aggregation involved in sorocarp development; IMP:dictyBase.
GO; GO:0030155; P:regulation of cell adhesion; TAS:dictyBase.
GO; GO:0043087; P:regulation of GTPase activity; IMP:dictyBase.
GO; GO:0043520; P:regulation of myosin II filament assembly; IMP:dictyBase.
GO; GO:0061118; P:regulation of positive chemotaxis to cAMP; IMP:dictyBase.
GO; GO:0045859; P:regulation of protein kinase activity; IMP:dictyBase.
GO; GO:1904776; P:regulation of protein localization to cell cortex; IMP:dictyBase.
GO; GO:0007165; P:signal transduction; IMP:dictyBase.
GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:UniProtKB.
GO; GO:0031929; P:TOR signaling; IMP:dictyBase.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 467 Glycogen synthase kinase-3.
/FTId=PRO_0000085983.
DOMAIN 56 339 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 62 70 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 28 41 Ser-rich.
COMPBIAS 399 450 Ser-rich.
COMPBIAS 444 464 Thr-rich.
ACT_SITE 179 179 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 85 85 ATP.
MOD_RES 214 214 Phosphotyrosine; by zakA.
{ECO:0000269|PubMed:12408804}.
MOD_RES 220 220 Phosphotyrosine; by zakA.
{ECO:0000269|PubMed:12408804}.
MUTAGEN 85 85 K->M: Inactive kinase.
{ECO:0000269|PubMed:12408804}.
MUTAGEN 86 86 K->M: Inactive kinase.
{ECO:0000269|PubMed:12408804}.
MUTAGEN 214 214 Y->F: Not phosphorylated or activated by
zakA. {ECO:0000269|PubMed:12408804}.
MUTAGEN 220 220 Y->F: Not phosphorylated or activated by
zakA. {ECO:0000269|PubMed:12408804}.
SEQUENCE 467 AA; 51483 MW; EF6C00122B90C61D CRC64;
MSSKDQILEK DKKETDDNGN KKTTTTTSSS SSSSSSSKPR SNKFDKVIIK SNGVCYITEG
VIGNGSFGVV TQAIVADTKE VVAIKKVLQD QRYKNRELQI MKMLNHINIV SLKNSFYTSD
NDEVYLNLVL EYVPDTVYRV SRHYSMSKQP VPNIFVKLYI YQLCRSINYI HSLGICHRDI
KPQNLLLDTS TSTLKLCDFG SAKILIKGET NVSYICSRHY RAPELIFGST NYTTTIDVWS
LGCVLAELLL GQPLFPGENG IDQLVEIIKV LGTPTKEQIH AMNPYYTSFK FPEIKANPWP
RVFKAKDVPA ESIDLISKIL LYDPSSRLKP VEICAHPFFD ELRDPKTCLP DGKPLPPLFN
FTIAEQTSIG PKLAKTLIPS HAMNQIELPS PLFPNLAISS SNQSSSSNSN ANVSSNLNSH
SASPSTTSSS SSTPNSIPVQ SPSTTNTTSS TTNNTTTTTT TTTTSNH


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