KSG3_ARATH
ID KSG3_ARATH Reviewed; 409 AA.
AC P43289; Q8L5U7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Shaggy-related protein kinase gamma {ECO:0000303|PubMed:7509023};
DE EC=2.7.11.1;
DE AltName: Full=ASK-gamma {ECO:0000303|PubMed:7509023};
DE AltName: Full=Shaggy-related protein kinase 12 {ECO:0000303|PubMed:28575660};
DE Short=AtSK12 {ECO:0000303|PubMed:28575660};
GN Name=ASK3 {ECO:0000303|PubMed:7509023};
GN Synonyms=SK12 {ECO:0000303|PubMed:28575660};
GN OrderedLocusNames=At3g05840 {ECO:0000312|Araport:AT3G05840};
GN ORFNames=F10A16.14 {ECO:0000312|EMBL:AAF26086.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=7509023; DOI=10.1007/bf00280424;
RA Bianchi M.W., Guivarc'H D., Thomas M., Woodgett J.R., Kreis M.;
RT "Arabidopsis homologs of the shaggy and GSK-3 protein kinases: molecular
RT cloning and functional expression in Escherichia coli.";
RL Mol. Gen. Genet. 242:337-345(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9611268; DOI=10.1016/s0378-1119(98)00147-4;
RA Dornelas M.C., Lejeune B., Dron M., Kreis M.;
RT "The Arabidopsis SHAGGY-related protein kinase (ASK) gene family:
RT structure, organization and evolution.";
RL Gene 212:249-257(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH KIB1.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
RA Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S., Wang Z.-Y.;
RT "The F-box protein KIB1 mediates brassinosteroid-induced inactivation and
RT degradation of GSK3-like kinases in Arabidopsis.";
RL Mol. Cell 66:648-657(2017).
RN [8]
RP FUNCTION, INTERACTION WITH POLAR AND BASL, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=30429609; DOI=10.1038/s41586-018-0714-x;
RA Houbaert A., Zhang C., Tiwari M., Wang K., de Marcos Serrano A.,
RA Savatin D.V., Urs M.J., Zhiponova M.K., Gudesblat G.E., Vanhoutte I.,
RA Eeckhout D., Boeren S., Karimi M., Betti C., Jacobs T., Fenoll C., Mena M.,
RA de Vries S., De Jaeger G., Russinova E.;
RT "POLAR-guided signalling complex assembly and localization drive asymmetric
RT cell division.";
RL Nature 563:574-578(2018).
CC -!- FUNCTION: May mediate extracellular signals to regulate transcription
CC in differentiating cells. Probably involved first at the cortical
CC polarity site, to restrict MAPK signaling and promote asymmetric cell
CC division (ACD), and second in the nucleus of stomatal lineage ground
CC cells (SLGCs) or meristemoids, to limit cell division and to promote
CC differentiation into pavement or stomatal guard cells, respectively
CC (PubMed:30429609). Phosphorylate YDA and SPCH in vitro
CC (PubMed:30429609). {ECO:0000269|PubMed:30429609}.
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 -!- 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;
CC -!- SUBUNIT: Binds to KIB1 (PubMed:28575660). Component of a complex made
CC of POLAR, BASL, ASK7/BIN2 and ASK3/SK12 (PubMed:30429609). Binds to
CC POLAR and BASL (PubMed:30429609). {ECO:0000269|PubMed:28575660,
CC ECO:0000269|PubMed:30429609}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30429609}.
CC Cytoplasm, cell cortex {ECO:0000269|PubMed:30429609}. Note=Localized
CC throughout the plasma membrane in asymmetric cell division (ACD)
CC precursors (PubMed:30429609). Accumulates transiently in a polarized
CC pattern at the plasma membrane immediately before ACD, relocalizing to
CC well-defined foci, in a POLAR-dependent and in the presence of BASL
CC (PubMed:30429609). {ECO:0000269|PubMed:30429609}.
CC -!- TISSUE SPECIFICITY: Roots, shoots and leaves.
CC -!- DEVELOPMENTAL STAGE: Expressed in protodermal cells in young seedlings.
CC {ECO:0000269|PubMed:30429609}.
CC -!- PTM: Autophosphorylated mainly on threonine and serine residues.
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; X75431; CAA53180.1; -; mRNA.
DR EMBL; Y12710; CAA73247.1; -; Genomic_DNA.
DR EMBL; AC012393; AAF26086.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74303.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74304.1; -; Genomic_DNA.
DR EMBL; AY093347; AAM13346.1; -; mRNA.
DR EMBL; AY062713; AAL32791.1; -; mRNA.
DR EMBL; AY085752; AAM62970.1; -; mRNA.
DR PIR; S41597; S41597.
DR RefSeq; NP_187235.1; NM_111458.5.
DR RefSeq; NP_850520.1; NM_180189.4.
DR AlphaFoldDB; P43289; -.
DR SMR; P43289; -.
DR BioGRID; 5088; 5.
DR IntAct; P43289; 2.
DR STRING; 3702.AT3G05840.1; -.
DR iPTMnet; P43289; -.
DR PaxDb; P43289; -.
DR PRIDE; P43289; -.
DR ProteomicsDB; 237103; -.
DR EnsemblPlants; AT3G05840.1; AT3G05840.1; AT3G05840.
DR EnsemblPlants; AT3G05840.2; AT3G05840.2; AT3G05840.
DR GeneID; 819753; -.
DR Gramene; AT3G05840.1; AT3G05840.1; AT3G05840.
DR Gramene; AT3G05840.2; AT3G05840.2; AT3G05840.
DR KEGG; ath:AT3G05840; -.
DR Araport; AT3G05840; -.
DR TAIR; locus:2074464; AT3G05840.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; P43289; -.
DR OMA; DMKIQDD; -.
DR OrthoDB; 990896at2759; -.
DR PhylomeDB; P43289; -.
DR BRENDA; 2.7.11.26; 399.
DR PRO; PR:P43289; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P43289; baseline and differential.
DR Genevisible; P43289; AT.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; HDA:TAIR.
DR GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
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 Acetylation; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P43288"
FT CHAIN 2..409
FT /note="Shaggy-related protein kinase gamma"
FT /id="PRO_0000086218"
FT DOMAIN 73..357
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 79..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P43288"
FT MOD_RES 233
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q39011"
FT CONFLICT 22
FT /note="A -> V (in Ref. 5; AAM62970)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="I -> V (in Ref. 5; AAM62970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 46587 MW; 3A7950B183D8C33B CRC64;
MASVGIEPSA AVRESTGNVT DADRLPEEMK DMKIQDDKEM EATIVNGNVT ETGHIIVTTI
GGRNGQPKQT ISYMAERVVG HGSFGVVFQA KCLETGETVA IKKVLQDRRY KNRELQTMRL
LDHPNVVSLK HCFFSTTEKD ELYLNLVLEY VPETVHRVIK HYNKLNQRMP LVYVKLYTYQ
IFRSLSYIHR CIGVCHRDIK PQNLLVNPHT HQVKLCDFGS AKVLVKGEPN ISYICSRYYR
APELIFGATE YTTAIDVWSA GCVLAELLLG QPLFPGESGV DQLVEIIKVL GTPTREEIKC
MNPNYTEFKF PQIKAHPWHK IFHKRMPPEA VDLVSRLLQY SPNLRCAALD SLVHPFFDEL
RDPNARLPNG RFLPPLFNFK PHELKGVPVE MVAKLVPEHA RKQCPWLSL
