GSK2_ORYSJ
ID GSK2_ORYSJ Reviewed; 402 AA.
AC Q60EZ2;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Shaggy-related protein kinase GSK2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Glycogen synthase kinase3-like protein 2 {ECO:0000305};
DE Short=OsGSK2 {ECO:0000303|PubMed:27332964};
DE AltName: Full=Shaggy/GSK3-like kinase 22 {ECO:0000303|PubMed:30920691};
DE Short=OsSK22 {ECO:0000303|PubMed:30920691};
GN Name=GSK2 {ECO:0000303|PubMed:22685166};
GN Synonyms=SK22 {ECO:0000303|PubMed:30920691};
GN OrderedLocusNames=Os05g0207500 {ECO:0000312|EMBL:BAF16815.1},
GN LOC_Os05g11730 {ECO:0000305};
GN ORFNames=OJ1430_B02.4 {ECO:0000312|EMBL:AAU90187.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, INTERACTION WITH DLT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF THR-284 AND GLU-286.
RX PubMed=22685166; DOI=10.1105/tpc.112.097394;
RA Tong H., Liu L., Jin Y., Du L., Yin Y., Qian Q., Zhu L., Chu C.;
RT "DWARF AND LOW-TILLERING acts as a direct downstream target of a
RT GSK3/SHAGGY-like kinase to mediate brassinosteroid responses in rice.";
RL Plant Cell 24:2562-2577(2012).
RN [6]
RP INTERACTION WITH GRF4.
RX PubMed=27250747; DOI=10.1038/nplants.2015.195;
RA Che R., Tong H., Shi B., Liu Y., Fang S., Liu D., Xiao Y., Hu B., Liu L.,
RA Wang H., Zhao M., Chu C.;
RT "Control of grain size and rice yield by GL2-mediated brassinosteroid
RT responses.";
RL Nat. Plants 2:15195-15195(2015).
RN [7]
RP FUNCTION, AND INTERACTION WITH OFP8.
RX PubMed=27332964; DOI=10.1371/journal.pgen.1006118;
RA Yang C., Shen W., He Y., Tian Z., Li J.;
RT "OVATE family protein 8 positively mediates brassinosteroid signaling
RT through interacting with the GSK3-like kinase in rice.";
RL PLoS Genet. 12:E1006118-E1006118(2016).
RN [8]
RP FUNCTION, AND INTERACTION WITH SMOS1.
RX PubMed=28100707; DOI=10.1105/tpc.16.00611;
RA Qiao S., Sun S., Wang L., Wu Z., Li C., Li X., Wang T., Leng L., Tian W.,
RA Lu T., Wang X.;
RT "The RLA1/SMOS1 transcription factor functions with OsBZR1 to regulate
RT brassinosteroid signaling and rice architecture.";
RL Plant Cell 29:292-309(2017).
RN [9]
RP FUNCTION, INTERACTION WITH PUB24, AND AUTOPHOSPHORYLATION.
RX PubMed=30920691; DOI=10.1111/tpj.14332;
RA Min H.J., Cui L.H., Oh T.R., Kim J.H., Kim T.W., Kim W.T.;
RT "OsBZR1 turnover mediated by OsSK22-regulated U-box E3 ligase OsPUB24 in
RT rice BR response.";
RL Plant J. 99:426-438(2019).
CC -!- FUNCTION: Serine-threonine kinase that acts as a negative regulator of
CC brassinosteroid (BR) signaling (PubMed:22685166, PubMed:27332964,
CC PubMed:30920691). Phosphorylates DLT and BZR1, two positive regulators
CC that mediates several BR responses. Phosphorylation of DLT and BZR1
CC inhibits their activities in BR signaling (PubMed:22685166).
CC Phosphorylates OFP8, a positive regulator of BR responses.
CC Phosphorylated OFP8 shuttles from the nucleus to the cytoplasm where it
CC is degraded by the proteasome (PubMed:27332964). Phosphorylates the E3
CC ubiquitin-protein ligase PUB24, a negative regulator of BR signaling,
CC which targets BZR1 and promotes its degradation via the 26S proteasome
CC (PubMed:30920691). Phosphorylation of PUB24 increases its stability
CC (PubMed:30920691). Phosphorylates the AP2-ERF transcription factor
CC SMOS1, a positive regulator of BR signaling, which cooperatively
CC functions in a transactivating complex with BZR1 to enhance the
CC transcription of BR biosynthetic genes (PubMed:30920691).
CC Phosphorylation of SMOS1 leads to its degradation by an unknown
CC mechanism (PubMed:30920691). {ECO:0000269|PubMed:22685166,
CC ECO:0000269|PubMed:27332964, ECO:0000269|PubMed:30920691}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Interacts with DLT (PubMed:22685166). Interacts with OFP8
CC (PubMed:27332964). Interacts with GRF4 (PubMed:27250747). Interacts
CC with PUB24 (PubMed:30920691). Interacts with SMOS1 (PubMed:28100707).
CC {ECO:0000269|PubMed:22685166, ECO:0000269|PubMed:27250747,
CC ECO:0000269|PubMed:27332964, ECO:0000269|PubMed:28100707,
CC ECO:0000269|PubMed:30920691}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22685166}. Nucleus
CC {ECO:0000269|PubMed:22685166}.
CC -!- TISSUE SPECIFICITY: Expressed in lamina joints, vascular tissue and
CC nodes. {ECO:0000269|PubMed:22685166}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:30920691}.
CC -!- MISCELLANEOUS: Plants over-expressing GSK2 display typical
CC brassinosteroid (BR) loss-of-function phenotypes, and plants silencing
CC GSK2 have enhanced BR signaling phenotypes.
CC {ECO:0000269|PubMed:22685166}.
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; AC104280; AAU90187.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16815.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92763.1; -; Genomic_DNA.
DR RefSeq; XP_015637571.1; XM_015782085.1.
DR AlphaFoldDB; Q60EZ2; -.
DR SMR; Q60EZ2; -.
DR STRING; 4530.OS05T0207500-01; -.
DR iPTMnet; Q60EZ2; -.
DR PaxDb; Q60EZ2; -.
DR PRIDE; Q60EZ2; -.
DR EnsemblPlants; Os05t0207500-01; Os05t0207500-01; Os05g0207500.
DR GeneID; 4338079; -.
DR Gramene; Os05t0207500-01; Os05t0207500-01; Os05g0207500.
DR KEGG; osa:4338079; -.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q60EZ2; -.
DR OMA; QAAHNFF; -.
DR OrthoDB; 990896at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; 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; IBA:GO_Central.
DR GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..402
FT /note="Shaggy-related protein kinase GSK2"
FT /id="PRO_0000439008"
FT DOMAIN 63..347
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 284
FT /note="T->I: Gain-of-function mutant."
FT /evidence="ECO:0000269|PubMed:22685166"
FT MUTAGEN 286
FT /note="E->K: Gain-of-function mutant."
FT /evidence="ECO:0000269|PubMed:22685166"
SQ SEQUENCE 402 AA; 45509 MW; F92767F790691DAB CRC64;
MDQPAPAPEP MLLDAQPPAA VACDKKQQEG EAPYAEGNDA VTGHIISTTI GGKNGEPKRT
ISYMAERVVG TGSFGIVFQA KCLETGETVA IKKVLQDRRY KNRELQLMRA MDHPNVISLK
HCFFSTTSRD ELFLNLVMEY VPETLYRVLK HYSNANHRMP LIYVKLYMYQ LFRGLAYIHT
VPGVCHRDVK PQNVLVDPLT HQVKLCDFGS AKTLVPGEPN ISYICSRYYR APELIFGATE
YTTSIDIWSA GCVLAELLLG QPLFPGESAV DQLVEIIKVL GTPTREEIRC MNPNYTEFRF
PQIKAHPWHK VFHKRMPPEA IDLASRLLQY SPSLRCTALD ACAHPFFDEL REPNARLPNG
RPFPPLFNFK HELANSSQEL ISRLIPEHVR RQATHNFFNT GS
