GSK1_ORYSJ
ID GSK1_ORYSJ Reviewed; 407 AA.
AC Q9LWN0; Q0JPS3;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Shaggy-related protein kinase GSK1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Glycogen synthase kinase3-like protein 1 {ECO:0000305|PubMed:17690841};
DE Short=OsGSK1 {ECO:0000303|PubMed:17690841};
DE AltName: Full=Shaggy/GSK3-like kinase 21 {ECO:0000305};
DE Short=OsSK21 {ECO:0000305};
GN Name=GSK1 {ECO:0000303|PubMed:17690841}; Synonyms=SK21 {ECO:0000305};
GN OrderedLocusNames=Os01g0205700 {ECO:0000312|EMBL:BAS70941.1},
GN LOC_Os01g10840 {ECO:0000305};
GN ORFNames=P0451C06.26 {ECO:0000312|EMBL:BAA92966.1};
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
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, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17690841; DOI=10.1007/s11103-007-9213-4;
RA Koh S., Lee S.C., Kim M.K., Koh J.H., Lee S., An G., Choe S., Kim S.R.;
RT "T-DNA tagged knockout mutation of rice OsGSK1, an orthologue of
RT Arabidopsis BIN2, with enhanced tolerance to various abiotic stresses.";
RL Plant Mol. Biol. 65:453-466(2007).
RN [6]
RP FUNCTION, AND INTERACTION WITH LIC.
RX PubMed=22570626; DOI=10.1371/journal.pgen.1002686;
RA Zhang C., Xu Y., Guo S., Zhu J., Huan Q., Liu H., Wang L., Luo G., Wang X.,
RA Chong K.;
RT "Dynamics of brassinosteroid response modulated by negative regulator LIC
RT in rice.";
RL PLoS Genet. 8:E1002686-E1002686(2012).
CC -!- FUNCTION: Probable serine-threonine kinase that may act as a negative
CC regulator of brassinosteroid (BR) signaling during flower development.
CC May have physiological roles in stress signal-transduction pathways
CC (PubMed:17690841). Phosphorylates LIC in response to BR perception
CC (PubMed:22570626). {ECO:0000269|PubMed:17690841,
CC ECO:0000269|PubMed:22570626}.
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 LIC. {ECO:0000269|PubMed:22570626}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the entire young panicles,
CC spikelets, awns, vascular bundles of palea and lemma, stigma and
CC rachilla. Expressed in root tips, root hairs, lamina joint in the
CC collar region, vascular bundles of coleoptiles.
CC {ECO:0000269|PubMed:17690841}.
CC -!- INDUCTION: Induced by cold and salt stresses. Down-regulated by drought
CC stress. {ECO:0000269|PubMed:22570626}.
CC -!- DISRUPTION PHENOTYPE: Increased length of spikelet awns and weight of
CC seeds. Increased sensitivity to brassinolide. Enhanced tolerance to
CC drought, salt, cold and heat stresses. {ECO:0000269|PubMed:17690841}.
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=BAF04255.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS70941.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP001551; BAA92966.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04255.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; BAS70941.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q9LWN0; -.
DR SMR; Q9LWN0; -.
DR STRING; 39947.Q9LWN0; -.
DR PRIDE; Q9LWN0; -.
DR eggNOG; KOG0658; Eukaryota.
DR InParanoid; Q9LWN0; -.
DR PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:1902911; C:protein kinase complex; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
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; Brassinosteroid signaling pathway; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase.
FT CHAIN 1..407
FT /note="Shaggy-related protein kinase GSK1"
FT /id="PRO_0000439007"
FT DOMAIN 68..352
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 407 AA; 45580 MW; 9D530F76C3C6BA75 CRC64;
MEAPPGPEPM ELDAPPPPAA VAAAAATAGI SEKVLQKKEE GGGDAVTGHI ISTTIGGKNG
EPKRTISYMA ERVVGTGSFG IVFQAKCLET GETVAIKKVL QDRRYKNREL QLMRAMEHPN
VICLKHCFFS TTSRDELFLN LVMEYVPETL YRVLKHYSNA NQRMPLIYVK LYIYQLFRGL
AYIHTVPGVC HRDVKPQNVL VDPLTHQVKL CDFGSAKVLV PGEPNISYIC SRYYRAPELI
FGATEYTTSI DIWSAGCVLA ELLLGQPLFP GESAVDQLVE IIKVLGTPTR EEIRCMNPNY
TEFKFPQIKA HPWHKIFHKR MPPEAIDLAS RLLQYSPSLR CTALDACAHS FFDELREPNA
RLPNGRPFPP LFNFKHELAS ASPELIHRLI PDHIRRQHGL NFAHAGS
