KIN11_ARATH
ID KIN11_ARATH Reviewed; 512 AA.
AC P92958; A6XGQ9; P92968; Q3E7R4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=SNF1-related protein kinase catalytic subunit alpha KIN11 {ECO:0000305};
DE Short=AKIN11 {ECO:0000312|EMBL:CAA67671.1};
DE EC=2.7.11.1 {ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:17671505};
DE AltName: Full=AKIN alpha-1;
DE Short=AKINalpha1;
DE AltName: Full=SNF1-related kinase 1.2 {ECO:0000303|PubMed:12805596};
DE Short=SnRK1.2 {ECO:0000303|PubMed:12805596};
GN Name=KIN11 {ECO:0000305};
GN Synonyms=AKIN11 {ECO:0000312|EMBL:CAA67671.1},
GN SNR1 {ECO:0000312|EMBL:ABH11526.1}, SNRK1.2 {ECO:0000303|PubMed:12805596};
GN OrderedLocusNames=At3g29160 {ECO:0000312|Araport:AT3G29160};
GN ORFNames=MXE2.16 {ECO:0000312|EMBL:BAB01993.1};
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], INTERACTION WITH AKINB1; AKINB2 AND AKING1, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=10417704; DOI=10.1046/j.1365-313x.1999.00476.x;
RA Bouly J.-P., Gissot L., Lessard P., Kreis M., Thomas M.;
RT "Arabidopsis thaliana proteins related to the yeast SIP and SNF4 interact
RT with AKINalpha1, an SNF1-like protein kinase.";
RL Plant J. 18:541-550(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AUTOPHOSPHORYLATION, AND
RP INTERACTION WITH PRL1.
RX PubMed=10220464; DOI=10.1073/pnas.96.9.5322;
RA Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L., Muranaka T.,
RA Machida Y., Schell J., Koncz C.;
RT "Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like
RT protein kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Fu H.;
RT "Functional differentiation of ubiquitin-interacting factors from
RT Arabidopsis.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH SNF4.
RX PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
RA Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
RT "Functional identification of an Arabidopsis Snf4 ortholog by screening for
RT heterologous multicopy suppressors of snf4 deficiency in yeast.";
RL Plant J. 23:115-122(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH SKP1 AND PAD1.
RX PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
RA Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
RA Salchert K., del Pozo C., Schell J., Koncz C.;
RT "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a
RT plant SCF ubiquitin ligase.";
RL EMBO J. 20:2742-2756(2001).
RN [9]
RP INTERACTION WITH KINB2.
RX PubMed=11522840; DOI=10.1093/nar/29.17.3685;
RA Ferrando A., Koncz-Kalman Z., Farras R., Tiburcio A., Schell J., Koncz C.;
RT "Detection of in vivo protein interactions between Snf1-related kinase
RT subunits with intron-tagged epitope-labelling in plants cells.";
RL Nucleic Acids Res. 29:3685-3693(2001).
RN [10]
RP INTERACTION WITH DSP4.
RX PubMed=12148529; DOI=10.1046/j.1365-313x.2002.01250.x;
RA Fordham-Skelton A.P., Chilley P., Lumbreras V., Reignoux S., Fenton T.R.,
RA Dahm C.C., Pages M., Gatehouse J.A.;
RT "A novel higher plant protein tyrosine phosphatase interacts with SNF1-
RT related protein kinases via a KIS (kinase interaction sequence) domain.";
RL Plant J. 29:705-715(2002).
RN [11]
RP FUNCTION, INTERACTION WITH TOMATO GOLDEN MOSAIC VIRUS AL2 AND BEET CURLY
RP TOP VIRUS L2, AND ACTIVITY REGULATION.
RX PubMed=12671096; DOI=10.1105/tpc.009530;
RA Hao L., Wang H., Sunter G., Bisaro D.M.;
RT "Geminivirus AL2 and L2 proteins interact with and inactivate SNF1
RT kinase.";
RL Plant Cell 15:1034-1048(2003).
RN [12]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12805596; DOI=10.1104/pp.102.011999;
RA Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H., Halford N.,
RA Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M., Walker-Simmons K.,
RA Zhu J.-K., Harmon A.C.;
RT "The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
RL Plant Physiol. 132:666-680(2003).
RN [13]
RP INTERACTION WITH KINB3.
RX PubMed=15803412; DOI=10.1007/s11103-004-5111-1;
RA Gissot L., Polge C., Bouly J.P., Lemaitre T., Kreis M., Thomas M.;
RT "AKINbeta3, a plant specific SnRK1 protein, is lacking domains present in
RT yeast and mammals non-catalytic beta-subunits.";
RL Plant Mol. Biol. 56:747-759(2004).
RN [14]
RP INTERACTION WITH SNF4, COMPONENT OF A HETEROTRIMERIC COMPLEX, AND SUBUNIT.
RX PubMed=17028154; DOI=10.1104/pp.106.087718;
RA Gissot L., Polge C., Jossier M., Girin T., Bouly J.-P., Kreis M.,
RA Thomas M.;
RT "AKINbetagamma contributes to SnRK1 heterotrimeric complexes and interacts
RT with two proteins implicated in plant pathogen resistance through its
RT KIS/GBD sequence.";
RL Plant Physiol. 142:931-944(2006).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF LYS-49.
RX PubMed=17671505; DOI=10.1038/nature06069;
RA Baena-Gonzalez E., Rolland F., Thevelein J.M., Sheen J.;
RT "A central integrator of transcription networks in plant stress and energy
RT signalling.";
RL Nature 448:938-942(2007).
RN [16]
RP REVIEW.
RX PubMed=17166759; DOI=10.1016/j.tplants.2006.11.005;
RA Polge C., Thomas M.;
RT "SNF1/AMPK/SnRK1 kinases, global regulators at the heart of energy
RT control?";
RL Trends Plant Sci. 12:20-28(2007).
RN [17]
RP ACTIVITY REGULATION.
RX PubMed=19193861; DOI=10.1104/pp.108.133934;
RA Zhang Y., Primavesi L.F., Jhurreea D., Andralojc P.J., Mitchell R.A.,
RA Powers S.J., Schluepmann H., Delatte T., Wingler A., Paul M.J.;
RT "Inhibition of SNF1-related protein kinase1 activity and regulation of
RT metabolic pathways by trehalose-6-phosphate.";
RL Plant Physiol. 149:1860-1871(2009).
RN [18]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=19211700; DOI=10.1104/pp.108.133298;
RA Fragoso S., Espindola L., Paez-Valencia J., Gamboa A., Camacho Y.,
RA Martinez-Barajas E., Coello P.;
RT "SnRK1 isoforms AKIN10 and AKIN11 are differentially regulated in
RT Arabidopsis plants under phosphate starvation.";
RL Plant Physiol. 149:1906-1916(2009).
RN [19]
RP PHOSPHORYLATION AT THR-176, AND ACTIVITY REGULATION.
RX PubMed=19339507; DOI=10.1104/pp.108.132787;
RA Shen W., Reyes M.I., Hanley-Bowdoin L.;
RT "Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate SnRK1 by
RT phosphorylating its activation loop.";
RL Plant Physiol. 150:996-1005(2009).
RN [20]
RP INTERACTION WITH ATAF1.
RX DOI=10.1016/j.plantsci.2009.06.011;
RA Kleinow T., Himbert S., Krenz B., Jeske H., Koncz C.;
RT "NAC domain transcription factor ATAF1 interacts with SNF1-related kinases
RT and silencing of its subfamily causes severe developmental defects in
RT Arabidopsis.";
RL Plant Sci. 177:360-370(2009).
RN [21]
RP INDUCTION BY BABA.
RX PubMed=20484986; DOI=10.4161/psb.5.7.11903;
RA Singh P., Wu C.C., Zimmerli L.;
RT "beta-aminobutyric acid priming by stress imprinting.";
RL Plant Signal. Behav. 5:878-880(2010).
RN [22]
RP INTERACTION WITH CIPK14.
RX PubMed=25058458; DOI=10.1016/j.bbrc.2014.07.064;
RA Yan J., Niu F., Liu W.Z., Zhang H., Wang B., Lan W., Che Y., Yang B.,
RA Luan S., Jiang Y.Q.;
RT "Arabidopsis CIPK14 positively regulates glucose response.";
RL Biochem. Biophys. Res. Commun. 450:1679-1683(2014).
RN [23]
RP REVIEW.
RX PubMed=25530701; DOI=10.1007/s12374-014-0902-7;
RA Sheen J.;
RT "Master regulators in plant glucose signaling networks.";
RL J. Plant Biol. 57:67-79(2014).
RN [24]
RP INTERACTION WITH FLZ PROTEINS, AND INTERACTION WITH GEBP.
RX PubMed=24600465; DOI=10.3389/fpls.2014.00054;
RA Nietzsche M., Schiessl I., Boernke F.;
RT "The complex becomes more complex: protein-protein interactions of SnRK1
RT with DUF581 family proteins provide a framework for cell- and stimulus
RT type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:54-54(2014).
RN [25]
RP ERRATUM OF PUBMED:24600465.
RX PubMed=25544057; DOI=10.3389/fpls.2014.00693;
RA Boernke F.;
RT "Corrigendum: The complex becomes more complex: protein-protein
RT interactions of SnRK1 with DUF581 family proteins provide a framework for
RT cell- and stimulus type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:693-693(2014).
RN [26]
RP TISSUE SPECIFICITY, INDUCTION BY TREHALOSE, AND SUBCELLULAR LOCATION.
RX PubMed=25071807; DOI=10.3389/fpls.2014.00324;
RA Williams S.P., Rangarajan P., Donahue J.L., Hess J.E., Gillaspy G.E.;
RT "Regulation of sucrose non-fermenting related kinase 1 genes in Arabidopsis
RT thaliana.";
RL Front. Plant Sci. 5:324-324(2014).
RN [27]
RP INTERACTION WITH REM4.1 AND REM4.2, AND FUNCTION.
RX PubMed=25289013; DOI=10.5423/ppj.oa.06.2014.0061;
RA Son S., Oh C.J., An C.S.;
RT "Arabidopsis thaliana remorins interact with SnRK1 and play a role in
RT susceptibility to Beet Curly Top Virus and Beet Severe Curly Top Virus.";
RL Plant Pathol. J. 30:269-278(2014).
RN [28]
RP INTERACTION WITH ADK2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24498147; DOI=10.1371/journal.pone.0087592;
RA Mohannath G., Jackel J.N., Lee Y.H., Buchmann R.C., Wang H., Patil V.,
RA Adams A.K., Bisaro D.M.;
RT "A complex containing SNF1-related kinase (SnRK1) and adenosine kinase in
RT Arabidopsis.";
RL PLoS ONE 9:E87592-E87592(2014).
RN [29]
RP INTERACTION WITH IDD8.
RX PubMed=25929516; DOI=10.1186/s12870-015-0503-8;
RA Jeong E.-Y., Seo P.J., Woo J.C., Park C.-M.;
RT "AKIN10 delays flowering by inactivating IDD8 transcription factor through
RT protein phosphorylation in Arabidopsis.";
RL BMC Plant Biol. 15:110-110(2015).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26263501; DOI=10.7554/elife.05828;
RA Mair A., Pedrotti L., Wurzinger B., Anrather D., Simeunovic A., Weiste C.,
RA Valerio C., Dietrich K., Kirchler T., Naegele T., Vicente Carbajosa J.,
RA Hanson J., Baena-Gonzalez E., Chaban C., Weckwerth W., Droege-Laser W.,
RA Teige M.;
RT "SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy
RT response in plants.";
RL Elife 4:0-0(2015).
RN [31]
RP COMPONENT OF A HETEROTRIMERIC COMPLEX, AND SUBUNIT.
RX PubMed=25736509; DOI=10.1111/tpj.12813;
RA Emanuelle S., Hossain M.I., Moller I.E., Pedersen H.L., van de Meene A.M.,
RA Doblin M.S., Koay A., Oakhill J.S., Scott J.W., Willats W.G., Kemp B.E.,
RA Bacic A., Gooley P.R., Stapleton D.I.;
RT "SnRK1 from Arabidopsis thaliana is an atypical AMPK.";
RL Plant J. 82:183-192(2015).
RN [32]
RP INTERACTION WITH FLZ3; FLZ9; TCP3; TCP13; HB21 AND HB23.
RX DOI=10.1016/j.cpb.2015.10.004;
RA Nietzsche M., Landgraf R., Tohge T., Boernke F.;
RT "A protein-protein interaction network linking the energy-sensor kinase
RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
RL Curr. Plant Biol. 5:36-44(2016).
RN [33]
RP REVIEW.
RX PubMed=27812990; DOI=10.1007/978-3-319-43589-3_17;
RA Margalha L., Valerio C., Baena-Gonzalez E.;
RT "Plant SnRK1 kinases: structure, regulation, and function.";
RL EXS 107:403-438(2016).
RN [34]
RP PHOSPHORYLATION AT THR-176.
RX PubMed=27029354; DOI=10.1093/jxb/erw107;
RA Cho H.Y., Wen T.N., Wang Y.T., Shih M.C.;
RT "Quantitative phosphoproteomics of protein kinase SnRK1 regulated protein
RT phosphorylation in Arabidopsis under submergence.";
RL J. Exp. Bot. 67:2745-2760(2016).
RN [35]
RP SUMOYLATION.
RX PubMed=26662259; DOI=10.1111/tpj.13096;
RA Crozet P., Margalha L., Butowt R., Fernandes N., Elias C.A., Orosa B.,
RA Tomanov K., Teige M., Bachmair A., Sadanandom A., Baena-Gonzalez E.;
RT "SUMOylation represses SnRK1 signaling in Arabidopsis.";
RL Plant J. 85:120-133(2016).
RN [36]
RP INDUCTION BY BACTERIAL PATHOGEN.
RX PubMed=27337039; DOI=10.1016/j.plaphy.2016.06.016;
RA Wang X.Y., Li D.Z., Li Q., Ma Y.Q., Yao J.W., Huang X., Xu Z.Q.;
RT "Metabolomic analysis reveals the relationship between AZI1 and sugar
RT signaling in systemic acquired resistance of Arabidopsis.";
RL Plant Physiol. Biochem. 107:273-287(2016).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT THR-176.
RX PubMed=27545962; DOI=10.1038/srep31697;
RA Nukarinen E., Naegele T., Pedrotti L., Wurzinger B., Mair A., Landgraf R.,
RA Boernke F., Hanson J., Teige M., Baena-Gonzalez E., Droege-Laser W.,
RA Weckwerth W.;
RT "Quantitative phosphoproteomics reveals the role of the AMPK plant ortholog
RT SnRK1 as a metabolic master regulator under energy deprivation.";
RL Sci. Rep. 6:31697-31697(2016).
RN [38]
RP REVIEW.
RX PubMed=27156455; DOI=10.1016/j.tplants.2016.04.008;
RA Hulsmans S., Rodriguez M., De Coninck B., Rolland F.;
RT "The SnRK1 energy sensor in plant biotic interactions.";
RL Trends Plant Sci. 21:648-661(2016).
RN [39]
RP DISRUPTION PHENOTYPE.
RX PubMed=28922765; DOI=10.1093/jxb/erx233;
RA Chan A., Carianopol C., Tsai A.Y., Varathanajah K., Chiu R.S.,
RA Gazzarrini S.;
RT "SnRK1 phosphorylation of FUSCA3 positively regulates embryogenesis, seed
RT yield, and plant growth at high temperature in Arabidopsis.";
RL J. Exp. Bot. 68:4219-4231(2017).
RN [40]
RP INTERACTION WITH WRI1.
RX PubMed=28314829; DOI=10.1105/tpc.17.00019;
RA Zhai Z., Liu H., Shanklin J.;
RT "Phosphorylation of WRINKLED1 by KIN10 results in its proteasomal
RT degradation, providing a link between energy homeostasis and lipid
RT biosynthesis.";
RL Plant Cell 29:871-889(2017).
RN [41]
RP INTERACTION WITH FLZ PROTEINS.
RX PubMed=29945970; DOI=10.1074/jbc.ra118.002073;
RA Jamsheer K M., Shukla B.N., Jindal S., Gopan N., Mannully C.T., Laxmi A.;
RT "The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by the
RT coordinated actions of the FLZ domain and intrinsically disordered
RT regions.";
RL J. Biol. Chem. 293:13134-13150(2018).
RN [42]
RP INTERACTION WITH IPK2B.
RX PubMed=29216370; DOI=10.1093/pcp/pcx186;
RA Yang Q., Sang S., Chen Y., Wei Z., Wang P.;
RT "The role of Arabidopsis inositol polyphosphate kinase AtIPK2beta in
RT glucose suppression of seed germination and seedling development.";
RL Plant Cell Physiol. 59:343-354(2018).
RN [43]
RP INTERACTION WITH FLZ6 AND FLZ10, AND SUBCELLULAR LOCATION.
RX PubMed=29406622; DOI=10.1111/tpj.13854;
RA Jamsheer K M., Sharma M., Singh D., Mannully C.T., Jindal S., Shukla B.N.,
RA Laxmi A.;
RT "FCS-like zinc finger 6 and 10 repress SnRK1 signalling in Arabidopsis.";
RL Plant J. 94:232-245(2018).
RN [44]
RP INTERACTION WITH GEBP.
RX PubMed=29192025; DOI=10.1104/pp.17.01461;
RA Nietzsche M., Guerra T., Alseekh S., Wiermer M., Sonnewald S., Fernie A.R.,
RA Boernke F.;
RT "STOREKEEPER RELATED1/G-element binding protein (STKR1) interacts with
RT protein kinase SnRK1.";
RL Plant Physiol. 176:1773-1792(2018).
CC -!- FUNCTION: Catalytic subunit of the probable trimeric SNF1-related
CC protein kinase (SnRK) complex, a central regulator of cellular energy
CC homeostasis, which, in response to seemingly unrelated darkness, sugar
CC and stress conditions, activates energy-producing pathways and inhibits
CC energy-consuming processes. May play a role in a signal transduction
CC cascade regulating gene expression and carbohydrate metabolism in
CC higher plants. The SnRK complex may also be involved in the regulation
CC of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase
CC and in assimilation of nitrogen by phosphorylating nitrate reductase
CC (PubMed:17671505). In vitro, KIN11 exhibits kinase activity on sucrose
CC phosphate synthase and the kinase activity is inhibited by PRL1
CC (PubMed:10220464). May be a subunit of a SCF ubiquitin ligase complex
CC and thus be involved in proteasomal ubiquitination (PubMed:11387208).
CC Involved in innate antiviral defenses (PubMed:12671096). Phosphorylates
CC REM4.1 in vitro (PubMed:25289013). Phosphorylates ADK2 in vitro
CC (PubMed:24498147). {ECO:0000269|PubMed:10220464,
CC ECO:0000269|PubMed:11387208, ECO:0000269|PubMed:12671096,
CC ECO:0000269|PubMed:17671505, ECO:0000269|PubMed:24498147,
CC ECO:0000269|PubMed:25289013}.
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:10220464, ECO:0000269|PubMed:17671505};
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:0000269|PubMed:10220464,
CC ECO:0000269|PubMed:17671505};
CC -!- ACTIVITY REGULATION: Inactivated by the begomovirus AL2 protein or the
CC curtovirus L2 protein (PubMed:12671096). Activated by phosphorylation
CC at Thr-176 by GRIK1/SNAK2 and GRIK2/SNAK1 (PubMed:19339507). Inhibited
CC by trehalose-6-phosphate (PubMed:19193861).
CC {ECO:0000269|PubMed:12671096, ECO:0000269|PubMed:19193861,
CC ECO:0000269|PubMed:19339507}.
CC -!- SUBUNIT: Subunit of a probable heterotrimeric complex consisting of an
CC alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB) and a gamma
CC (KING or SNF4) non-catalytic regulatory subunits (PubMed:17028154,
CC PubMed:25736509). Interacts with KINB2, KINB3, SNF4 and probably with
CC KINB1 and KING1 (PubMed:10417704, PubMed:10929106, PubMed:11522840,
CC PubMed:15803412, PubMed:17028154). Interacts with SKP1/ASK1, PAD1 and
CC the N-terminus of PRL1 (PubMed:10220464, PubMed:11387208). Potential
CC subunit of a SCF ubiquitin ligase complex consisting of a SNF1-related
CC protein kinase, SKP1 and CUL1. The association of the SCF complex with
CC the proteasome may be mediated by PAD1 and seems to be inhibited by the
CC interaction with PRL1 (PubMed:11387208). Interacts with DSP4
CC (PubMed:12148529). Interacts with the begomovirus AL2 protein and the
CC curtovirus L2 protein (PubMed:12671096). Interacts with ATAF1 (Ref.20).
CC Interacts with CIPK14 (PubMed:25058458). Interacts with FLZ proteins
CC through their FLZ-type zinc finger domains (PubMed:24600465,
CC PubMed:29945970). Interacts with GEBP/STKR1 (PubMed:24600465,
CC PubMed:29192025). Interacts with REM4.1 and REM4.2 (PubMed:25289013).
CC Interacts with ADK2 (PubMed:24498147). Interacts with IDD8
CC (PubMed:25929516). Interacts with FLZ3, FLZ9, TCP3, TCP13, HB21/ZHD3
CC and HB23/ZHD10 (Ref.32). Interacts with WRI1 (PubMed:28314829).
CC Interacts with IPK2b (PubMed:29216370). Interacts with FLZ6 and FLZ10
CC (PubMed:29406622). {ECO:0000269|PubMed:10220464,
CC ECO:0000269|PubMed:10417704, ECO:0000269|PubMed:10929106,
CC ECO:0000269|PubMed:11387208, ECO:0000269|PubMed:11522840,
CC ECO:0000269|PubMed:12148529, ECO:0000269|PubMed:12671096,
CC ECO:0000269|PubMed:15803412, ECO:0000269|PubMed:17028154,
CC ECO:0000269|PubMed:24498147, ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:25058458, ECO:0000269|PubMed:25289013,
CC ECO:0000269|PubMed:25736509, ECO:0000269|PubMed:25929516,
CC ECO:0000269|PubMed:28314829, ECO:0000269|PubMed:29192025,
CC ECO:0000269|PubMed:29216370, ECO:0000269|PubMed:29406622,
CC ECO:0000269|PubMed:29945970, ECO:0000269|Ref.20, ECO:0000269|Ref.32}.
CC -!- INTERACTION:
CC P92958; Q9FEB5: DSP4; NbExp=2; IntAct=EBI-307202, EBI-307215;
CC P92958; Q9SCY5: KINB2; NbExp=4; IntAct=EBI-307202, EBI-2042436;
CC P92958; Q42384: PRL1; NbExp=2; IntAct=EBI-307202, EBI-1382964;
CC P92958; Q9LVG2: TOE2; NbExp=2; IntAct=EBI-307202, EBI-4424568;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19211700, ECO:0000269|PubMed:25071807}. Cytoplasm
CC {ECO:0000269|PubMed:19211700, ECO:0000269|PubMed:24498147,
CC ECO:0000269|PubMed:25071807}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:29406622}. Note=Co-localized with ER marker when
CC associated with FLZ6 or FLZ10. {ECO:0000269|PubMed:29406622}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P92958-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P92958-2; Sequence=VSP_034567, VSP_034568;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, flower buds, flowers,
CC siliques and leaves (PubMed:10417704). Restrictly expressed to the base
CC of the leaf, the vascular tissue, and the hydathodes (PubMed:25071807).
CC {ECO:0000269|PubMed:10417704, ECO:0000269|PubMed:25071807}.
CC -!- INDUCTION: Induced by sucrose (PubMed:10220464). Down-regulated under
CC phosphate starvation (at the protein level) (PubMed:19211700). Up-
CC regulated by beta-aminobutyric acid (BABA) (PubMed:20484986). Induced
CC after infection by the effector avirulence protein AvrRpm1 from
CC P.syringae (PubMed:27337039). Induced by trehalose (PubMed:25071807).
CC {ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:19211700,
CC ECO:0000269|PubMed:20484986, ECO:0000269|PubMed:25071807,
CC ECO:0000269|PubMed:27337039}.
CC -!- DOMAIN: The regulatory domain (RD) contains the auto-inhibitory domain
CC (AID) that inhibits kinase activity of the protein kinase domain (KD).
CC {ECO:0000250|UniProtKB:Q38997}.
CC -!- DOMAIN: The PPI motif mediates the interaction with the ABI (abscisic
CC acid-insensitive) phosphatases. {ECO:0000250|UniProtKB:Q38997}.
CC -!- PTM: Sumoylated by SIZ1. {ECO:0000269|PubMed:26662259}.
CC -!- PTM: Phosphorylated at Thr-176 under submergence (PubMed:27029354).
CC Autophosphorylated (PubMed:10220464). Phosphorylated at Thr-176 by
CC GRIK1/SNAK2 and GRIK2/SNAK1 (PubMed:19339507).
CC {ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:19339507,
CC ECO:0000269|PubMed:27029354}.
CC -!- DISRUPTION PHENOTYPE: Increased seed abortion.
CC {ECO:0000269|PubMed:28922765}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; X94755; CAA64382.1; -; mRNA.
DR EMBL; X99279; CAA67671.1; -; mRNA.
DR EMBL; DQ778956; ABH11526.1; -; mRNA.
DR EMBL; AB018121; BAB01993.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77542.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77543.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77544.1; -; Genomic_DNA.
DR EMBL; AY070468; AAL49934.1; -; mRNA.
DR EMBL; AY149927; AAN31081.1; -; mRNA.
DR PIR; T52633; T52633.
DR RefSeq; NP_566843.1; NM_113839.4. [P92958-1]
DR RefSeq; NP_974374.1; NM_202645.3. [P92958-1]
DR RefSeq; NP_974375.1; NM_202646.1. [P92958-2]
DR AlphaFoldDB; P92958; -.
DR SMR; P92958; -.
DR BioGRID; 7895; 85.
DR IntAct; P92958; 35.
DR STRING; 3702.AT3G29160.1; -.
DR iPTMnet; P92958; -.
DR PaxDb; P92958; -.
DR PRIDE; P92958; -.
DR ProteomicsDB; 237086; -. [P92958-1]
DR EnsemblPlants; AT3G29160.1; AT3G29160.1; AT3G29160. [P92958-1]
DR EnsemblPlants; AT3G29160.2; AT3G29160.2; AT3G29160. [P92958-1]
DR EnsemblPlants; AT3G29160.3; AT3G29160.3; AT3G29160. [P92958-2]
DR GeneID; 822566; -.
DR Gramene; AT3G29160.1; AT3G29160.1; AT3G29160. [P92958-1]
DR Gramene; AT3G29160.2; AT3G29160.2; AT3G29160. [P92958-1]
DR Gramene; AT3G29160.3; AT3G29160.3; AT3G29160. [P92958-2]
DR KEGG; ath:AT3G29160; -.
DR Araport; AT3G29160; -.
DR TAIR; locus:2094672; AT3G29160.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; P92958; -.
DR OMA; HWVPSPM; -.
DR PhylomeDB; P92958; -.
DR PRO; PR:P92958; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P92958; baseline and differential.
DR Genevisible; P92958; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0010353; P:response to trehalose; IEP:UniProtKB.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
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; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral protein; ATP-binding;
KW Carbohydrate metabolism; Chloroplast; Cytoplasm; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Host-virus interaction;
KW Kinase; Lipid biosynthesis; Lipid metabolism; Nitrate assimilation;
KW Nucleotide-binding; Phosphoprotein; Plastid; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..512
FT /note="SNF1-related protein kinase catalytic subunit alpha
FT KIN11"
FT /id="PRO_0000086129"
FT DOMAIN 20..272
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 293..333
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 463..511
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 291..391
FT /note="Auto-inhibitory domain (AID)"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT REGION 295..512
FT /note="Regulatory domain (RD)"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT REGION 392..512
FT /note="PPI"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
FT REGION 399..512
FT /note="Interaction with PAD1 and SKP1"
FT /evidence="ECO:0000269|PubMed:11387208"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:17671505"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 176
FT /note="Phosphothreonine; by GRIK1 or GRIK2"
FT /evidence="ECO:0000269|PubMed:19339507,
FT ECO:0000269|PubMed:27029354, ECO:0000269|PubMed:27545962"
FT VAR_SEQ 352..359
FT /note="DSGSNPMR -> WFQSYAHT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034567"
FT VAR_SEQ 360..512
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034568"
FT MUTAGEN 49
FT /note="K->M: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:17671505"
FT CONFLICT 291
FT /note="A -> T (in Ref. 1; CAA64382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 58690 MW; 4FBEF55D3EC60F87 CRC64;
MDHSSNRFGN NGVESILPNY KLGKTLGIGS FGKVKIAEHV VTGHKVAIKI LNRRKIKNME
MEEKVRREIK ILRLFMHPHI IRQYEVIETT SDIYVVMEYV KSGELFDYIV EKGRLQEDEA
RNFFQQIISG VEYCHRNMVV HRDLKPENLL LDSRCNIKIA DFGLSNVMRD GHFLKTSCGS
PNYAAPEVIS GKLYAGPEVD VWSCGVILYA LLCGTLPFDD ENIPNLFKKI KGGIYTLPSH
LSSEARDLIP RMLIVDPVKR ITIPEIRQHR WFQTHLPRYL AVSPPDTVEQ AKKINEEIVQ
EVVNMGFDRN QVLESLRNRT QNDATVTYYL LLDNRFRVPS GYLESEFQET TDSGSNPMRT
PEAGASPVGH WIPAHVDHYG LGARSQVPVD RKWALGLQSH AHPREIMNEV LKALQELNVC
WKKIGHYNMK CRWVPGLADG QNTMVNNQLH FRDESSIIED DCAMTSPTVI KFELQLYKAR
EEKYLLDIQR VNGPQFLFLD LCAAFLTELR VI
