ID KIN10_ARATH Reviewed; 512 AA.
AC Q38997; A6XGR0; O04728; Q38987; Q39076; Q8RWD2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 27-MAR-2024, entry version 202.
DE RecName: Full=SNF1-related protein kinase catalytic subunit alpha KIN10 {ECO:0000305};
DE Short=AKIN10 {ECO:0000312|EMBL:AAA32736.1, ECO:0000312|EMBL:CAA56146.1};
DE EC=2.7.11.1 {ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:17671505};
DE AltName: Full=AKIN alpha-2;
DE Short=AKINalpha2;
DE AltName: Full=SNF1-related kinase 1.1 {ECO:0000303|PubMed:12805596};
DE Short=SnRK1.1 {ECO:0000303|PubMed:12805596};
GN Name=KIN10 {ECO:0000305};
GN Synonyms=AK21 {ECO:0000312|EMBL:CAA60529.1},
GN AKIN10 {ECO:0000312|EMBL:AAA32736.1, ECO:0000312|EMBL:CAA56146.1},
GN SKIN10 {ECO:0000312|EMBL:CAA64384.1}, SNR2 {ECO:0000312|EMBL:ABH11527.1},
GN SNRK1.1 {ECO:0000303|PubMed:12805596};
GN OrderedLocusNames=At3g01090 {ECO:0000312|Araport:AT3G01090};
GN ORFNames=T4P13.22 {ECO:0000312|EMBL:AAF26165.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=1339373; DOI=10.1016/0378-1119(92)90100-4;
RA le Guen L., Thomas M., Bianchi M., Halford N.G., Kreis M.;
RT "Structure and expression of a gene from Arabidopsis thaliana encoding a
RT protein related to SNF1 protein kinase.";
RL Gene 120:249-254(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Lessard P., Kreis M., Thomas M.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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=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 [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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=7816049; DOI=10.1007/bf00290120;
RA le Guen L., Thomas M., Kreis M.;
RT "Gene density and organization in a small region of the Arabidopsis
RT thaliana genome.";
RL Mol. Gen. Genet. 245:390-396(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-198.
RC STRAIN=cv. Eil-0; TISSUE=Leaf;
RX PubMed=8534852; DOI=10.1007/bf00020984;
RA Thuemmler F., Kirchner M., Teuber R., Dittrich P.;
RT "Differential accumulation of the transcripts of 22 novel protein kinase
RT genes in Arabidopsis thaliana.";
RL Plant Mol. Biol. 29:551-565(1995).
RN [9]
RP FUNCTION, PHOSPHORYLATION, INDUCTION, AND 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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-20, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [17]
RP FUNCTION, MUTAGENESIS OF LYS-48 AND THR-175, DISRUPTION PHENOTYPE, AND
RP INDUCTION BY DCMU.
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 [18]
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 [19]
RP UBIQUITINATION.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [20]
RP INTERACTION WITH 5PTASE13, AND SUBCELLULAR LOCATION.
RX PubMed=18931139; DOI=10.1104/pp.108.130575;
RA Ananieva E.A., Gillaspy G.E., Ely A., Burnette R.N., Erickson F.L.;
RT "Interaction of the WD40 domain of a myoinositol polyphosphate 5-
RT phosphatase with SnRK1 links inositol, sugar, and stress signaling.";
RL Plant Physiol. 148:1868-1882(2008).
RN [21]
RP INDUCTION BY GLUCOSE, AND PHOSPHORYLATION AT THR-175.
RX PubMed=19302419; DOI=10.1111/j.1365-313x.2009.03871.x;
RA Jossier M., Bouly J.P., Meimoun P., Arjmand A., Lessard P., Hawley S.,
RA Grahame Hardie D., Thomas M.;
RT "SnRK1 (SNF1-related kinase 1) has a central role in sugar and ABA
RT signalling in Arabidopsis thaliana.";
RL Plant J. 59:316-328(2009).
RN [22]
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 [23]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [25]
RP PHOSPHORYLATION AT THR-175, MUTAGENESIS OF THR-175, AND ACTIVITY
RP 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 [26]
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 [27]
RP FUNCTION, AND MUTAGENESIS OF THR-175.
RX PubMed=20164192; DOI=10.1074/jbc.m109.079194;
RA Crozet P., Jammes F., Valot B., Ambard-Bretteville F., Nessler S.,
RA Hodges M., Vidal J., Thomas M.;
RT "Cross-phosphorylation between Arabidopsis thaliana sucrose nonfermenting
RT 1-related protein kinase 1 (AtSnRK1) and its activating kinase (AtSnAK)
RT determines their catalytic activities.";
RL J. Biol. Chem. 285:12071-12077(2010).
RN [28]
RP INTERACTION WITH SCE1 AND ESD4, AND SUMOYLATION.
RX PubMed=20855607; DOI=10.1073/pnas.1005452107;
RA Elrouby N., Coupland G.;
RT "Proteome-wide screens for small ubiquitin-like modifier (SUMO) substrates
RT identify Arabidopsis proteins implicated in diverse biological processes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17415-17420(2010).
RN [29]
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 [30]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SNF4.
RX PubMed=21235649; DOI=10.1111/j.1365-313x.2010.04462.x;
RA Bitrian M., Roodbarkelari F., Horvath M., Koncz C.;
RT "BAC-recombineering for studying plant gene regulation: developmental
RT control and cellular localization of SnRK1 kinase subunits.";
RL Plant J. 65:829-842(2011).
RN [31]
RP INTERACTION WITH PP2C74.
RX PubMed=22449965; DOI=10.1016/j.febslet.2012.02.019;
RA Tsugama D., Liu S., Takano T.;
RT "A putative myristoylated 2C-type protein phosphatase, PP2C74, interacts
RT with SnRK1 in Arabidopsis.";
RL FEBS Lett. 586:693-698(2012).
RN [32]
RP INTERACTION WITH FUS3, AND FUNCTION.
RX PubMed=22026387; DOI=10.1111/j.1365-313x.2011.04832.x;
RA Tsai A.Y., Gazzarrini S.;
RT "AKIN10 and FUSCA3 interact to control lateral organ development and phase
RT transitions in Arabidopsis.";
RL Plant J. 69:809-821(2012).
RN [33]
RP INDUCTION BY HYPOXIA.
RX PubMed=22232383; DOI=10.1104/pp.111.189829;
RA Cho Y.H., Hong J.W., Kim E.C., Yoo S.D.;
RT "Regulatory functions of SnRK1 in stress-responsive gene expression and in
RT plant growth and development.";
RL Plant Physiol. 158:1955-1964(2012).
RN [34]
RP FUNCTION.
RX PubMed=22902692; DOI=10.4161/psb.21549;
RA Tsai A.Y., Gazzarrini S.;
RT "Overlapping and distinct roles of AKIN10 and FUSCA3 in ABA and sugar
RT signaling during seed germination.";
RL Plant Signal. Behav. 7:1238-1242(2012).
RN [35]
RP INTERACTION WITH CDKE1, AND SUBCELLULAR LOCATION.
RX PubMed=23229550; DOI=10.1074/jbc.m112.416727;
RA Ng S., Giraud E., Duncan O., Law S.R., Wang Y., Xu L., Narsai R.,
RA Carrie C., Walker H., Day D.A., Blanco N.E., Strand A., Whelan J.,
RA Ivanova A.;
RT "Cyclin-dependent kinase E1 (CDKE1) provides a cellular switch in plants
RT between growth and stress responses.";
RL J. Biol. Chem. 288:3449-3459(2013).
RN [36]
RP INTERACTION WITH ABI1 AND PP2CA, DOMAIN, PHOSPHORYLATION AT THR-175, AND
RP ACTIVITY REGULATION.
RX PubMed=24179127; DOI=10.1105/tpc.113.114066;
RA Rodrigues A., Adamo M., Crozet P., Margalha L., Confraria A., Martinho C.,
RA Elias A., Rabissi A., Lumbreras V., Gonzalez-Guzman M., Antoni R.,
RA Rodriguez P.L., Baena-Gonzalez E.;
RT "ABI1 and PP2CA phosphatases are negative regulators of Snf1-related
RT protein kinase1 signaling in Arabidopsis.";
RL Plant Cell 25:3871-3884(2013).
RN [37]
RP FUNCTION, AND INTERACTION WITH KRP6.
RX PubMed=23617622; DOI=10.1111/tpj.12218;
RA Guerinier T., Millan L., Crozet P., Oury C., Rey F., Valot B., Mathieu C.,
RA Vidal J., Hodges M., Thomas M., Glab N.;
RT "Phosphorylation of p27(KIP1) homologs KRP6 and 7 by SNF1-related protein
RT kinase-1 links plant energy homeostasis and cell proliferation.";
RL Plant J. 75:515-525(2013).
RN [38]
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 [39]
RP INTERACTION WITH FLZ PROTEINS, INTERACTION WITH GEBP, AND SUBCELLULAR
RP LOCATION.
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 [40]
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 [41]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
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 [42]
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 [43]
RP FUNCTION.
RX PubMed=24990996; DOI=10.1128/jvi.00761-14;
RA Shen W., Dallas M.B., Goshe M.B., Hanley-Bowdoin L.;
RT "SnRK1 phosphorylation of AL2 delays Cabbage leaf curl virus infection in
RT Arabidopsis.";
RL J. Virol. 88:10598-10612(2014).
RN [44]
RP INTERACTION WITH MYC2, AND FUNCTION.
RX PubMed=24890857; DOI=10.1111/pce.12375;
RA Im J.H., Cho Y.H., Kim G.D., Kang G.H., Hong J.W., Yoo S.D.;
RT "Inverse modulation of the energy sensor Snf1-related protein kinase 1 on
RT hypoxia adaptation and salt stress tolerance in Arabidopsis thaliana.";
RL Plant Cell Environ. 37:2303-2312(2014).
RN [45]
RP FUNCTION, INTERACTION WITH IDD8, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
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 [46]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BZIP63, AND FUNCTION.
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 [47]
RP INTERACTION WITH PTL, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=25697797; DOI=10.1093/jxb/erv032;
RA O'Brien M., Kaplan-Levy R.N., Quon T., Sappl P.G., Smyth D.R.;
RT "PETAL LOSS, a trihelix transcription factor that represses growth in
RT Arabidopsis thaliana, binds the energy-sensing SnRK1 kinase AKIN10.";
RL J. Exp. Bot. 66:2475-2485(2015).
RN [48]
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 [49]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-364, AND
RP INDUCTION BY SALT AND OXIDATIVE STRESSES.
RX PubMed=26471895; DOI=10.1104/pp.15.01486;
RA Chen Y., Hoehenwarter W.;
RT "Changes in the phosphoproteome and metabolome link early signaling events
RT to rearrangement of photosynthesis and central metabolism in salinity and
RT oxidative stress response in Arabidopsis.";
RL Plant Physiol. 169:3021-3033(2015).
RN [50]
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 [51]
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 [52]
RP PHOSPHORYLATION AT THR-175, MUTAGENESIS OF LYS-48 AND THR-175, FUNCTION,
RP AND INTERACTION WITH PTP1.
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 [53]
RP ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27436712; DOI=10.1105/tpc.16.00301;
RA Carvalho R.F., Szakonyi D., Simpson C.G., Barbosa I.C., Brown J.W.,
RA Baena-Gonzalez E., Duque P.;
RT "The Arabidopsis SR45 splicing factor, a negative regulator of sugar
RT signaling, modulates SNF1-related protein kinase 1 stability.";
RL Plant Cell 28:1910-1925(2016).
RN [54]
RP SUMOYLATION AT LYS-34; LYS-63 AND LYS-390, INTERACTION WITH SCE1,
RP MUTAGENESIS OF LYS-34; LYS-63 AND LYS-390, UBIQUITINATION, AND FUNCTION.
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 [55]
RP INTERACTION WITH RAPTOR1B, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION AT THR-175, AND SUBCELLULAR LOCATION.
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 [56]
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 [57]
RP FUNCTION.
RX PubMed=28263378; DOI=10.1002/1873-3468.12618;
RA Robertlee J., Kobayashi K., Suzuki M., Muranaka T.;
RT "AKIN10, a representative Arabidopsis SNF1-related protein kinase 1
RT (SnRK1), phosphorylates and downregulates plant HMG-CoA reductase.";
RL FEBS Lett. 591:1159-1166(2017).
RN [58]
RP FUNCTION, MUTAGENESIS OF CYS-133 AND CYS-177, SUBUNIT, AND ACTIVITY
RP REGULATION.
RX PubMed=28940407; DOI=10.1002/1873-3468.12852;
RA Wurzinger B., Mair A., Fischer-Schrader K., Nukarinen E., Roustan V.,
RA Weckwerth W., Teige M.;
RT "Redox state-dependent modulation of plant SnRK1 kinase activity differs
RT from AMPK regulation in animals.";
RL FEBS Lett. 591:3625-3636(2017).
RN [59]
RP FUNCTION.
RX PubMed=28740502; DOI=10.3389/fpls.2017.01201;
RA Chen L., Su Z.Z., Huang L., Xia F.N., Qi H., Xie L.J., Xiao S., Chen Q.F.;
RT "The AMP-activated protein kinase KIN10 is involved in the regulation of
RT autophagy in Arabidopsis.";
RL Front. Plant Sci. 8:1201-1201(2017).
RN [60]
RP DEVELOPMENTAL STAGE, FUNCTION, AND 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 [61]
RP ERRATUM OF PUBMED:28922765.
RX PubMed=29140438; DOI=10.1093/jxb/erx379;
RA Chan A., Carianopol C., Tsai A.Y., Varatharajah K., Chiu R.S.,
RA Gazzarrini S.;
RT "Corrigendum: SnRK1 phosphorylation of FUSCA3 positively regulates
RT embryogenesis, seed yield, and plant growth at high temperature in
RT Arabidopsis.";
RL J. Exp. Bot. 68:5981-5981(2017).
RN [62]
RP FUNCTION, AND 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 [63]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28783755; DOI=10.1371/journal.pone.0182591;
RA Soto-Burgos J., Bassham D.C.;
RT "SnRK1 activates autophagy via the TOR signaling pathway in Arabidopsis
RT thaliana.";
RL PLoS ONE 12:E0182591-E0182591(2017).
RN [64]
RP INTERACTION WITH EIN3, AND FUNCTION.
RX PubMed=28600557; DOI=10.1038/s41598-017-03506-1;
RA Kim G.D., Cho Y.H., Yoo S.D.;
RT "Regulatory functions of cellular energy sensor SNF1-related kinase1 for
RT leaf senescence delay through ETHYLENE- INSENSITIVE3 repression.";
RL Sci. Rep. 7:3193-3193(2017).
RN [65]
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 [66]
RP FUNCTION, AND INTERACTION WITH BZIP2 AND BZIP63.
RX PubMed=29348240; DOI=10.1105/tpc.17.00414;
RA Pedrotti L., Weiste C., Naegele T., Wolf E., Lorenzin F., Dietrich K.,
RA Mair A., Weckwerth W., Teige M., Baena-Gonzalez E., Droege-Laser W.;
RT "Snf1-RELATED KINASE1-controlled C/S1-bZIP signaling activates alternative
RT mitochondrial metabolic pathways to ensure plant survival in extended
RT darkness.";
RL Plant Cell 30:495-509(2018).
RN [67]
RP INTERACTION WITH IPK2B, AND FUNCTION.
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 [68]
RP INTERACTION WITH FLZ6 AND FLZ10, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
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 [69]
RP FUNCTION.
RX PubMed=29114081; DOI=10.1104/pp.17.01395;
RA Simon N.M.L., Kusakina J., Fernandez-Lopez A., Chembath A., Belbin F.E.,
RA Dodd A.N.;
RT "The energy-signaling hub SnRK1 is important for sucrose-induced hypocotyl
RT elongation.";
RL Plant Physiol. 176:1299-1310(2018).
RN [70]
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).
RN [71]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29584583; DOI=10.1080/15592324.2018.1457913;
RA Simon N.M.L., Sawkins E., Dodd A.N.;
RT "Involvement of the SnRK1 subunit KIN10 in sucrose-induced hypocotyl
RT elongation.";
RL Plant Signal. Behav. 2018:E1457913-E1457913(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, KIN10 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 Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in vitro (PubMed:20164192).
CC Cooperates with FUS3 to regulate developmental phase transitions and
CC lateral organ development and act both as positive regulators of
CC abscisic acid (ABA) signaling during germination (PubMed:22026387,
CC PubMed:22902692). Phosphorylates FUS3 in embryo (PubMed:28922765).
CC Negatively modulates MYC2 accumulation through its protein
CC phosphorylation (PubMed:24890857). Phosphorylates geminivirus (CaLCuV,
CC TGMV, ToMoV) AL2 protein resulting in a delay in the viral DNA
CC accumulation and symptom appearance during infection (PubMed:24990996).
CC Regulates bZIP63 activity to alter metabolism in response to starvation
CC through its protein phosphorylation (PubMed:26263501). Under sugar
CC deprivation conditions, antagonizes the IDD8 function in flowering time
CC control by its protein phosphorylation (PubMed:25929516). Plays a
CC cardinal role in the control of cell proliferation through inhibition
CC of KRP6 activity by its protein phosphorylation (PubMed:23617622).
CC Under submergence, phosphorylates PTP1, leading to the release of the
CC MPK6 signaling pathway inhibition (PubMed:27029354). Triggers its own
CC SUMO-mediated proteasomal degradation, establishing a negative feedback
CC loop that attenuates SnRK1 signaling and prevents detrimental
CC hyperactivation of stress responses (PubMed:26662259). Phosphorylates
CC RAPTOR1B in vitro (PubMed:27545962). Phosphorylates and down-regulates
CC HMGR1S in vitro (PubMed:28263378). Kinase activity is redox-sensitive
CC (PubMed:28940407). Acts upstream of TOR in the regulation of autophagy.
CC Required for the activation of autophagy by many abiotic stresses
CC (PubMed:28783755). Involved in positive regulation of autophagy,
CC possibly by affecting the phosphorylation of ATG1 proteins
CC (PubMed:28740502). Negatively modulates WRI1 accumulation through its
CC protein phosphorylation (PubMed:28314829). Modulates leaf senescence
CC progression by the negative regulation of EIN3 accumulation through its
CC protein phosphorylation (PubMed:28600557). Under extended darkness,
CC C/S1-bZIP-SnRK1 complex interacts with the histone acetylation
CC machinery to remodel chromatin and facilitate transcription. BZIP2-
CC BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its
CC transcription (PubMed:29348240). Phosphorylates and down-regulates
CC IPK2b in vitro (PubMed:29216370). Involved in the regulation of
CC sucrose-induced hypocotyl elongation under light/dark cycles
CC (PubMed:29114081, PubMed:29584583). {ECO:0000269|PubMed:10220464,
CC ECO:0000269|PubMed:11387208, ECO:0000269|PubMed:17671505,
CC ECO:0000269|PubMed:20164192, ECO:0000269|PubMed:22026387,
CC ECO:0000269|PubMed:22902692, ECO:0000269|PubMed:23617622,
CC ECO:0000269|PubMed:24890857, ECO:0000269|PubMed:24990996,
CC ECO:0000269|PubMed:25929516, ECO:0000269|PubMed:26263501,
CC ECO:0000269|PubMed:26662259, ECO:0000269|PubMed:27029354,
CC ECO:0000269|PubMed:27545962, ECO:0000269|PubMed:28263378,
CC ECO:0000269|PubMed:28314829, ECO:0000269|PubMed:28600557,
CC ECO:0000269|PubMed:28740502, ECO:0000269|PubMed:28783755,
CC ECO:0000269|PubMed:28922765, ECO:0000269|PubMed:28940407,
CC ECO:0000269|PubMed:29114081, ECO:0000269|PubMed:29216370,
CC ECO:0000269|PubMed:29348240, ECO:0000269|PubMed:29584583}.
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: Activated by phosphorylation at Thr-175 by
CC GRIK1/SNAK2 and GRIK2/SNAK1 (PubMed:19339507). Inactivated by
CC dephosphorylation at Thr-175 (PubMed:24179127). Inhibited by trehalose-
CC 6-phosphate (PubMed:19193861). Down-regulated by SR45 by affecting its
CC stability (PubMed:27436712). Reduced kinase activity in response to
CC H(2)O(2) treatment. The redox-state of Cys-177 seems to directly
CC influence its kinase activity (PubMed:28940407). Down-regulated by FLZ6
CC and FLZ10 (PubMed:29406622). {ECO:0000269|PubMed:19193861,
CC ECO:0000269|PubMed:19339507, ECO:0000269|PubMed:24179127,
CC ECO:0000269|PubMed:27436712, ECO:0000269|PubMed:28940407,
CC ECO:0000269|PubMed:29406622}.
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:10929106, PubMed:11522840, PubMed:15803412,
CC PubMed:17028154, PubMed:21235649). Interacts with SKP1/ASK1, PAD1, the
CC N-terminus of PRL1 and the WD40 domain of 5PTase13 (PubMed:10220464,
CC PubMed:11387208, PubMed:18931139). Potential subunit of a SCF ubiquitin
CC ligase complex consisting of a SNF1-related protein kinase, SKP1 and
CC CUL1. The association of the SCF complex with the proteasome may be
CC mediated by PAD1 and seems to be inhibited by the interaction with PRL1
CC (PubMed:11387208). Interacts with ATAF1 (Ref.26). Interacts with ESD4
CC (PubMed:20855607). Interacts with SCE1 (PubMed:20855607,
CC PubMed:26662259). Interacts with FUS3 (PubMed:22026387). Interacts with
CC PP2C74 (PubMed:22449965). Interacts with CDKE1 (PubMed:23229550).
CC Interacts with ABI1 and PP2CA (PubMed:24179127). Interacts with KRP6
CC (PubMed:23617622). Interacts with CIPK14 (PubMed:25058458). Interacts
CC with FLZ proteins through their FLZ-type zinc finger domains
CC (PubMed:24600465, PubMed:29945970). Interacts with GEBP/STKR1
CC (PubMed:24600465, PubMed:29192025). Interacts with MYC2
CC (PubMed:24890857). Interacts with IDD8 (PubMed:25929516). Interacts
CC with BZIP63 (PubMed:26263501). Interacts with PTL (PubMed:25697797).
CC Interacts with FLZ3, FLZ9, TCP3, TCP13, HB21/ZHD3 and HB23/ZHD10
CC (Ref.50). Interacts with PTP1 (PubMed:27029354). Interacts with
CC RAPTOR1B (PubMed:27545962). Forms oligomers in vitro under strongly
CC reducing conditions (PubMed:28940407). Interacts with WRI1
CC (PubMed:28314829). Interacts with EIN3 (PubMed:28600557). Component of
CC a ternary complex composed of BZIP2-BZIP63 heterodimer and KIN10
CC (PubMed:29348240). Interacts with IPK2b (PubMed:29216370). Interacts
CC with FLZ6 and FLZ10 (PubMed:29406622). {ECO:0000269|PubMed:10220464,
CC ECO:0000269|PubMed:10929106, ECO:0000269|PubMed:11387208,
CC ECO:0000269|PubMed:11522840, ECO:0000269|PubMed:15803412,
CC ECO:0000269|PubMed:17028154, ECO:0000269|PubMed:18931139,
CC ECO:0000269|PubMed:20855607, ECO:0000269|PubMed:21235649,
CC ECO:0000269|PubMed:22026387, ECO:0000269|PubMed:22449965,
CC ECO:0000269|PubMed:23229550, ECO:0000269|PubMed:23617622,
CC ECO:0000269|PubMed:24179127, ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:24890857, ECO:0000269|PubMed:25058458,
CC ECO:0000269|PubMed:25697797, ECO:0000269|PubMed:25736509,
CC ECO:0000269|PubMed:25929516, ECO:0000269|PubMed:26263501,
CC ECO:0000269|PubMed:26662259, ECO:0000269|PubMed:27029354,
CC ECO:0000269|PubMed:27545962, ECO:0000269|PubMed:28314829,
CC ECO:0000269|PubMed:28600557, ECO:0000269|PubMed:28940407,
CC ECO:0000269|PubMed:29192025, ECO:0000269|PubMed:29216370,
CC ECO:0000269|PubMed:29348240, ECO:0000269|PubMed:29406622,
CC ECO:0000269|PubMed:29945970, ECO:0000269|Ref.26, ECO:0000269|Ref.50}.
CC -!- INTERACTION:
CC Q38997; Q8VY80: FLZ5; NbExp=3; IntAct=EBI-2107143, EBI-4439342;
CC Q38997; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-2107143, EBI-25519488;
CC Q38997; Q9SCY5: KINB2; NbExp=12; IntAct=EBI-2107143, EBI-2042436;
CC Q38997; Q944A6: SNF4; NbExp=11; IntAct=EBI-2107143, EBI-2360649;
CC Q38997-2; Q93V58: GRIK1; NbExp=2; IntAct=EBI-20798606, EBI-6399184;
CC Q38997-2; Q5HZ38: GRIK2; NbExp=2; IntAct=EBI-20798606, EBI-6399237;
CC Q38997-2; Q42384: PRL1; NbExp=3; IntAct=EBI-20798606, EBI-1382964;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast
CC {ECO:0000269|PubMed:19211700}. Cytoplasm {ECO:0000269|PubMed:19211700,
CC ECO:0000269|PubMed:21235649, ECO:0000269|PubMed:23229550,
CC ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:25071807,
CC ECO:0000269|PubMed:25697797}. Nucleus {ECO:0000269|PubMed:18931139,
CC ECO:0000269|PubMed:21235649, ECO:0000269|PubMed:23229550,
CC ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:25071807,
CC ECO:0000269|PubMed:25697797, ECO:0000269|PubMed:25929516}. Golgi
CC apparatus {ECO:0000269|PubMed:25697797}. Note=Shuttles from the
CC cytoplasm to the nucleus when associated with a FLZ protein.
CC {ECO:0000269|PubMed:24600465}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:25071807, ECO:0000269|PubMed:27545962}. Nucleus
CC {ECO:0000269|PubMed:25071807, ECO:0000269|PubMed:25929516,
CC ECO:0000269|PubMed:27545962}. 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=2;
CC IsoId=Q38997-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q38997-1; Sequence=VSP_059890;
CC -!- TISSUE SPECIFICITY: Isoform 2 is widely expressed, especially in newly
CC developing tissues (PubMed:25697797). Isoform 2 is expressed throughout
CC the seedling, with highest expression in leaf primordia and vascular
CC tissue, and the seedling root tip. Isoform 2 is later expressed in
CC developing lateral root primordia and developing embryos within
CC siliques (PubMed:25071807). Isoform 1 is widely expressed but at very
CC low levels (PubMed:25071807). {ECO:0000269|PubMed:25071807,
CC ECO:0000269|PubMed:25697797}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryo development from the
CC heart to mature embryo stages. {ECO:0000269|PubMed:28922765}.
CC -!- INDUCTION: Induced by sucrose (PubMed:10220464). Induced by DCMU
CC herbicide (PubMed:17671505). Induced by glucose (PubMed:19302419). Up-
CC regulated by beta-aminobutyric acid (BABA) (PubMed:20484986). Induced
CC by hypoxia following submergence (PubMed:22232383). Induced by salt and
CC oxidative stresses (at the protein level) (PubMed:26471895).
CC {ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:17671505,
CC ECO:0000269|PubMed:19302419, ECO:0000269|PubMed:20484986,
CC ECO:0000269|PubMed:22232383, ECO:0000269|PubMed:26471895}.
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:0000269|PubMed:24179127}.
CC -!- DOMAIN: The PPI motif mediates the interaction with the ABI (abscisic
CC acid-insensitive) phosphatases. {ECO:0000269|PubMed:24179127}.
CC -!- PTM: Phosphorylated at Thr-175 in response to glucose
CC (PubMed:19302419). Phosphorylated at Thr-175 under submergence
CC (PubMed:27029354). Autophosphorylated (PubMed:10220464,
CC PubMed:24179127, PubMed:25929516). Dephosphorylated at Thr-175 by ABI1
CC and PP2CA (PubMed:24179127). {ECO:0000269|PubMed:10220464,
CC ECO:0000269|PubMed:19302419, ECO:0000269|PubMed:24179127,
CC ECO:0000269|PubMed:25929516, ECO:0000269|PubMed:27029354}.
CC -!- PTM: Ubiquitinated (PubMed:26662259). Degradation is mediated by a
CC CUL4-based E3 ligase that uses PRL1 as a substrate receptor
CC (PubMed:18223036). {ECO:0000269|PubMed:18223036,
CC ECO:0000269|PubMed:26662259}.
CC -!- PTM: Sumoylated by SIZ1 (PubMed:20855607, PubMed:26662259). Sumoylated
CC SnRK1 is ubiquitinated and degraded by the proteasome
CC (PubMed:26662259). {ECO:0000269|PubMed:20855607,
CC ECO:0000269|PubMed:26662259}.
CC -!- DISRUPTION PHENOTYPE: Anthocyanin accumulation and accelerated
CC senescence (PubMed:17671505). Starch accumulation during phosphate
CC deficiency (PubMed:19211700). Reduced sensitivity to glucose during
CC early development (PubMed:27436712). Increased seed abortion
CC (PubMed:28922765). Blocked autophagy during abiotic stresses but not
CC under control conditions (PubMed:28783755). Enhanced sucrose-induced
CC hypocotyl elongation (PubMed:29584583). {ECO:0000269|PubMed:17671505,
CC ECO:0000269|PubMed:19211700, ECO:0000269|PubMed:27436712,
CC ECO:0000269|PubMed:28783755, ECO:0000269|PubMed:28922765,
CC ECO:0000269|PubMed:29584583}.
CC -!- MISCELLANEOUS: Overexpressing plants show delayed leaf senescence,
CC enhanced tolerance to nutrient starvation dependent on a functional
CC autophagy pathway, enhanced formation of autophagosomes, and tolerance
CC to drought and submergence (PubMed:28740502). Overexpression of KIN10
CC leads to increased autophagy (PubMed:28783755). Overexpression inhibits
CC sucrose-induced hypocotyl elongation (PubMed:29114081).
CC {ECO:0000269|PubMed:28740502, ECO:0000269|PubMed:28783755,
CC ECO:0000269|PubMed:29114081}.
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; M93023; AAA32736.1; -; Genomic_DNA.
DR EMBL; X94757; CAA64384.1; -; mRNA.
DR EMBL; DQ778957; ABH11527.1; -; mRNA.
DR EMBL; AC008261; AAF26165.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73607.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73608.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73609.1; -; Genomic_DNA.
DR EMBL; AY093170; AAM13169.1; -; mRNA.
DR EMBL; BT010386; AAQ56829.1; -; mRNA.
DR EMBL; X79707; CAA56146.1; -; Genomic_DNA.
DR EMBL; X86966; CAA60529.1; -; Genomic_DNA.
DR PIR; JC1446; JC1446.
DR RefSeq; NP_001118546.1; NM_001125074.2. [Q38997-2]
DR RefSeq; NP_566130.1; NM_110974.5. [Q38997-2]
DR RefSeq; NP_850488.1; NM_180157.1. [Q38997-1]
DR AlphaFoldDB; Q38997; -.
DR SMR; Q38997; -.
DR BioGRID; 6592; 88.
DR IntAct; Q38997; 119.
DR STRING; 3702.Q38997; -.
DR iPTMnet; Q38997; -.
DR PaxDb; 3702-AT3G01090-2; -.
DR ProteomicsDB; 238213; -. [Q38997-2]
DR EnsemblPlants; AT3G01090.1; AT3G01090.1; AT3G01090. [Q38997-2]
DR EnsemblPlants; AT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
DR EnsemblPlants; AT3G01090.3; AT3G01090.3; AT3G01090. [Q38997-2]
DR GeneID; 821259; -.
DR Gramene; AT3G01090.1; AT3G01090.1; AT3G01090. [Q38997-2]
DR Gramene; AT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
DR Gramene; AT3G01090.3; AT3G01090.3; AT3G01090. [Q38997-2]
DR KEGG; ath:AT3G01090; -.
DR Araport; AT3G01090; -.
DR TAIR; AT3G01090; KIN10.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q38997; -.
DR OMA; QMEMEEK; -.
DR OrthoDB; 5388562at2759; -.
DR PhylomeDB; Q38997; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:Q38997; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38997; baseline and differential.
DR Genevisible; Q38997; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000152; C:nuclear ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
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:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0009594; P:detection of nutrient; IDA:TAIR.
DR GO; GO:0003006; P:developmental process involved in reproduction; IMP:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:1900055; P:regulation of leaf senescence; IDA:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
DR GO; GO:0009635; P:response to herbicide; IEP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0005982; P:starch metabolic process; IMP:UniProtKB.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010050; P:vegetative phase change; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:UniProtKB.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR CDD; cd14335; UBA_SnRK1_plant; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
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; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46934; UBA-like; 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; ATP-binding; Carbohydrate metabolism; Chloroplast;
KW Cytoplasm; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Golgi apparatus; Isopeptide bond; Kinase;
KW Lipid biosynthesis; Lipid metabolism; Nitrate assimilation;
KW Nucleotide-binding; Nucleus; 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 KIN10"
FT /id="PRO_0000086128"
FT DOMAIN 19..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 292..332
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 290..389
FT /note="Auto-inhibitory domain (AID)"
FT /evidence="ECO:0000269|PubMed:24179127"
FT REGION 294..512
FT /note="Regulatory domain (RD)"
FT /evidence="ECO:0000269|PubMed:24179127"
FT REGION 390..512
FT /note="PPI"
FT /evidence="ECO:0000269|PubMed:24179127"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 25..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:17671505, ECO:0000269|PubMed:27029354"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 175
FT /note="Phosphothreonine; by GRIK1 or GRIK2"
FT /evidence="ECO:0000269|PubMed:19302419,
FT ECO:0000269|PubMed:19339507, ECO:0000269|PubMed:24179127,
FT ECO:0000269|PubMed:27029354, ECO:0000269|PubMed:27545962"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26471895"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:26662259"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:26662259"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:26662259"
FT VAR_SEQ 1
FT /note="M -> MFKRVDEFNLVSSTIDHRIFKSRM (in isoform 1)"
FT /id="VSP_059890"
FT MUTAGEN 34
FT /note="K->R: Abolishes sumoylation. When associated with R-
FT 63 and R-390."
FT /evidence="ECO:0000269|PubMed:26662259"
FT MUTAGEN 48
FT /note="K->M: Abolishes kinase activity. Enhances
FT sensitivity to submergence."
FT /evidence="ECO:0000269|PubMed:17671505,
FT ECO:0000269|PubMed:27029354"
FT MUTAGEN 63
FT /note="K->R: Abolishes sumoylation. When associated with R-
FT 34 and R-390."
FT /evidence="ECO:0000269|PubMed:26662259"
FT MUTAGEN 133
FT /note="C->S: Reduced kinase activity and retained redox
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:28940407"
FT MUTAGEN 175
FT /note="T->A: Abolishes phosphorylation by GRIK1 or GRIK2
FT leading to inactivation of the protein. Enhances
FT sensitivity to submergence."
FT /evidence="ECO:0000269|PubMed:17671505,
FT ECO:0000269|PubMed:19339507, ECO:0000269|PubMed:20164192,
FT ECO:0000269|PubMed:27029354"
FT MUTAGEN 175
FT /note="T->D: Enhances tolerance to submergence."
FT /evidence="ECO:0000269|PubMed:27029354"
FT MUTAGEN 177
FT /note="C->S: Retained kinase activity and abolished redox
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:28940407"
FT MUTAGEN 390
FT /note="K->R: Abolishes sumoylation. When associated with R-
FT 34 and R-63."
FT /evidence="ECO:0000269|PubMed:26662259"
SQ SEQUENCE 512 AA; 58373 MW; 5A18655A0AA506DF CRC64;
MDGSGTGSRS GVESILPNYK LGRTLGIGSF GRVKIAEHAL TGHKVAIKIL NRRKIKNMEM
EEKVRREIKI LRLFMHPHII RLYEVIETPT DIYLVMEYVN SGELFDYIVE KGRLQEDEAR
NFFQQIISGV EYCHRNMVVH RDLKPENLLL DSKCNVKIAD FGLSNIMRDG HFLKTSCGSP
NYAAPEVISG KLYAGPEVDV WSCGVILYAL LCGTLPFDDE NIPNLFKKIK GGIYTLPSHL
SPGARDLIPR MLVVDPMKRV TIPEIRQHPW FQAHLPRYLA VPPPDTVQQA KKIDEEILQE
VINMGFDRNH LIESLRNRTQ NDGTVTYYLI LDNRFRASSG YLGAEFQETM EGTPRMHPAE
SVASPVSHRL PGLMEYQGVG LRSQYPVERK WALGLQSRAH PREIMTEVLK ALQDLNVCWK
KIGHYNMKCR WVPNSSADGM LSNSMHDNNY FGDESSIIEN EAAVKSPNVV KFEIQLYKTR
DDKYLLDLQR VQGPQFLFLD LCAAFLAQLR VL
//
