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SNF1-related protein kinase catalytic subunit alpha KIN10 (AKIN10) (EC 2.7.11.1) (AKIN alpha-2) (AKINalpha2)

 KIN10_ARATH             Reviewed;         512 AA.
Q38997; A6XGR0; O04728; Q38987; Q39076; Q8RWD2;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
10-OCT-2018, sequence version 3.
10-OCT-2018, entry version 175.
RecName: Full=SNF1-related protein kinase catalytic subunit alpha KIN10 {ECO:0000305};
Short=AKIN10 {ECO:0000312|EMBL:AAA32736.1, ECO:0000312|EMBL:CAA56146.1};
EC=2.7.11.1 {ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:17671505};
AltName: Full=AKIN alpha-2;
Short=AKINalpha2;
AltName: Full=SNF1-related kinase 1.1 {ECO:0000303|PubMed:12805596};
Short=SnRK1.1 {ECO:0000303|PubMed:12805596};
Name=KIN10 {ECO:0000305};
Synonyms=AK21 {ECO:0000312|EMBL:CAA60529.1},
AKIN10 {ECO:0000312|EMBL:AAA32736.1, ECO:0000312|EMBL:CAA56146.1},
SKIN10 {ECO:0000312|EMBL:CAA64384.1},
SNR2 {ECO:0000312|EMBL:ABH11527.1},
SNRK1.1 {ECO:0000303|PubMed:12805596};
OrderedLocusNames=At3g01090 {ECO:0000312|Araport:AT3G01090};
ORFNames=T4P13.22 {ECO:0000312|EMBL:AAF26165.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=1339373; DOI=10.1016/0378-1119(92)90100-4;
le Guen L., Thomas M., Bianchi M., Halford N.G., Kreis M.;
"Structure and expression of a gene from Arabidopsis thaliana encoding
a protein related to SNF1 protein kinase.";
Gene 120:249-254(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Columbia; TISSUE=Seedling;
Lessard P., Kreis M., Thomas M.;
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Fu H.;
"Functional differentiation of ubiquitin-interacting factors from
Arabidopsis.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19 (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=7816049; DOI=10.1007/BF00290120;
le Guen L., Thomas M., Kreis M.;
"Gene density and organization in a small region of the Arabidopsis
thaliana genome.";
Mol. Gen. Genet. 245:390-396(1994).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-198.
STRAIN=cv. Eil-0; TISSUE=Leaf;
PubMed=8534852; DOI=10.1007/BF00020984;
Thuemmler F., Kirchner M., Teuber R., Dittrich P.;
"Differential accumulation of the transcripts of 22 novel protein
kinase genes in Arabidopsis thaliana.";
Plant Mol. Biol. 29:551-565(1995).
[9]
FUNCTION, PHOSPHORYLATION, INDUCTION, AND INTERACTION WITH PRL1.
PubMed=10220464; DOI=10.1073/pnas.96.9.5322;
Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L.,
Muranaka T., Machida Y., Schell J., Koncz C.;
"Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like
protein kinases.";
Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999).
[10]
INTERACTION WITH SNF4.
PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
"Functional identification of an Arabidopsis Snf4 ortholog by
screening for heterologous multicopy suppressors of snf4 deficiency in
yeast.";
Plant J. 23:115-122(2000).
[11]
FUNCTION, AND INTERACTION WITH SKP1 AND PAD1.
PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
Salchert K., del Pozo C., Schell J., Koncz C.;
"SKP1-SnRK protein kinase interactions mediate proteasomal binding of
a plant SCF ubiquitin ligase.";
EMBO J. 20:2742-2756(2001).
[12]
INTERACTION WITH KINB2.
PubMed=11522840; DOI=10.1093/nar/29.17.3685;
Ferrando A., Koncz-Kalman Z., Farras R., Tiburcio A., Schell J.,
Koncz C.;
"Detection of in vivo protein interactions between Snf1-related kinase
subunits with intron-tagged epitope-labelling in plants cells.";
Nucleic Acids Res. 29:3685-3693(2001).
[13]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12805596; DOI=10.1104/pp.102.011999;
Hrabak E.M., Chan C.W.M., Gribskov M., Harper J.F., Choi J.H.,
Halford N., Kudla J., Luan S., Nimmo H.G., Sussman M.R., Thomas M.,
Walker-Simmons K., Zhu J.-K., Harmon A.C.;
"The Arabidopsis CDPK-SnRK superfamily of protein kinases.";
Plant Physiol. 132:666-680(2003).
[14]
INTERACTION WITH KINB3.
PubMed=15803412; DOI=10.1007/s11103-004-5111-1;
Gissot L., Polge C., Bouly J.P., Lemaitre T., Kreis M., Thomas M.;
"AKINbeta3, a plant specific SnRK1 protein, is lacking domains present
in yeast and mammals non-catalytic beta-subunits.";
Plant Mol. Biol. 56:747-759(2004).
[15]
INTERACTION WITH SNF4, COMPONENT OF A HETEROTRIMERIC COMPLEX, AND
SUBUNIT.
PubMed=17028154; DOI=10.1104/pp.106.087718;
Gissot L., Polge C., Jossier M., Girin T., Bouly J.-P., Kreis M.,
Thomas M.;
"AKINbetagamma contributes to SnRK1 heterotrimeric complexes and
interacts with two proteins implicated in plant pathogen resistance
through its KIS/GBD sequence.";
Plant Physiol. 142:931-944(2006).
[16]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-20, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[17]
FUNCTION, MUTAGENESIS OF LYS-48 AND THR-175, DISRUPTION PHENOTYPE, AND
INDUCTION BY DCMU.
PubMed=17671505; DOI=10.1038/nature06069;
Baena-Gonzalez E., Rolland F., Thevelein J.M., Sheen J.;
"A central integrator of transcription networks in plant stress and
energy signalling.";
Nature 448:938-942(2007).
[18]
REVIEW.
PubMed=17166759; DOI=10.1016/j.tplants.2006.11.005;
Polge C., Thomas M.;
"SNF1/AMPK/SnRK1 kinases, global regulators at the heart of energy
control?";
Trends Plant Sci. 12:20-28(2007).
[19]
UBIQUITINATION.
PubMed=18223036; DOI=10.1105/tpc.107.055418;
Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
He Y.J., Xiong Y., Deng X.W.;
"Characterization of Arabidopsis and rice DWD proteins and their roles
as substrate receptors for CUL4-RING E3 ubiquitin ligases.";
Plant Cell 20:152-167(2008).
[20]
INTERACTION WITH 5PTASE13, AND SUBCELLULAR LOCATION.
PubMed=18931139; DOI=10.1104/pp.108.130575;
Ananieva E.A., Gillaspy G.E., Ely A., Burnette R.N., Erickson F.L.;
"Interaction of the WD40 domain of a myoinositol polyphosphate 5-
phosphatase with SnRK1 links inositol, sugar, and stress signaling.";
Plant Physiol. 148:1868-1882(2008).
[21]
INDUCTION BY GLUCOSE, AND PHOSPHORYLATION AT THR-175.
PubMed=19302419; DOI=10.1111/j.1365-313X.2009.03871.x;
Jossier M., Bouly J.P., Meimoun P., Arjmand A., Lessard P., Hawley S.,
Grahame Hardie D., Thomas M.;
"SnRK1 (SNF1-related kinase 1) has a central role in sugar and ABA
signalling in Arabidopsis thaliana.";
Plant J. 59:316-328(2009).
[22]
ACTIVITY REGULATION.
PubMed=19193861; DOI=10.1104/pp.108.133934;
Zhang Y., Primavesi L.F., Jhurreea D., Andralojc P.J., Mitchell R.A.,
Powers S.J., Schluepmann H., Delatte T., Wingler A., Paul M.J.;
"Inhibition of SNF1-related protein kinase1 activity and regulation of
metabolic pathways by trehalose-6-phosphate.";
Plant Physiol. 149:1860-1871(2009).
[23]
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=19211700; DOI=10.1104/pp.108.133298;
Fragoso S., Espindola L., Paez-Valencia J., Gamboa A., Camacho Y.,
Martinez-Barajas E., Coello P.;
"SnRK1 isoforms AKIN10 and AKIN11 are differentially regulated in
Arabidopsis plants under phosphate starvation.";
Plant Physiol. 149:1906-1916(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[25]
PHOSPHORYLATION AT THR-175, MUTAGENESIS OF THR-175, AND ACTIVITY
REGULATION.
PubMed=19339507; DOI=10.1104/pp.108.132787;
Shen W., Reyes M.I., Hanley-Bowdoin L.;
"Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate
SnRK1 by phosphorylating its activation loop.";
Plant Physiol. 150:996-1005(2009).
[26]
INTERACTION WITH ATAF1.
DOI=10.1016/j.plantsci.2009.06.011;
Kleinow T., Himbert S., Krenz B., Jeske H., Koncz C.;
"NAC domain transcription factor ATAF1 interacts with SNF1-related
kinases and silencing of its subfamily causes severe developmental
defects in Arabidopsis.";
Plant Sci. 177:360-370(2009).
[27]
FUNCTION, AND MUTAGENESIS OF THR-175.
PubMed=20164192; DOI=10.1074/jbc.M109.079194;
Crozet P., Jammes F., Valot B., Ambard-Bretteville F., Nessler S.,
Hodges M., Vidal J., Thomas M.;
"Cross-phosphorylation between Arabidopsis thaliana sucrose
nonfermenting 1-related protein kinase 1 (AtSnRK1) and its activating
kinase (AtSnAK) determines their catalytic activities.";
J. Biol. Chem. 285:12071-12077(2010).
[28]
INTERACTION WITH SCE1 AND ESD4, AND SUMOYLATION.
PubMed=20855607; DOI=10.1073/pnas.1005452107;
Elrouby N., Coupland G.;
"Proteome-wide screens for small ubiquitin-like modifier (SUMO)
substrates identify Arabidopsis proteins implicated in diverse
biological processes.";
Proc. Natl. Acad. Sci. U.S.A. 107:17415-17420(2010).
[29]
INDUCTION BY BABA.
PubMed=20484986;
Singh P., Wu C.C., Zimmerli L.;
"beta-aminobutyric acid priming by stress imprinting.";
Plant Signal. Behav. 5:878-880(2010).
[30]
SUBCELLULAR LOCATION, AND INTERACTION WITH SNF4.
PubMed=21235649; DOI=10.1111/j.1365-313X.2010.04462.x;
Bitrian M., Roodbarkelari F., Horvath M., Koncz C.;
"BAC-recombineering for studying plant gene regulation: developmental
control and cellular localization of SnRK1 kinase subunits.";
Plant J. 65:829-842(2011).
[31]
INTERACTION WITH PP2C74.
PubMed=22449965; DOI=10.1016/j.febslet.2012.02.019;
Tsugama D., Liu S., Takano T.;
"A putative myristoylated 2C-type protein phosphatase, PP2C74,
interacts with SnRK1 in Arabidopsis.";
FEBS Lett. 586:693-698(2012).
[32]
INTERACTION WITH FUS3, AND FUNCTION.
PubMed=22026387; DOI=10.1111/j.1365-313X.2011.04832.x;
Tsai A.Y., Gazzarrini S.;
"AKIN10 and FUSCA3 interact to control lateral organ development and
phase transitions in Arabidopsis.";
Plant J. 69:809-821(2012).
[33]
INDUCTION BY HYPOXIA.
PubMed=22232383; DOI=10.1104/pp.111.189829;
Cho Y.H., Hong J.W., Kim E.C., Yoo S.D.;
"Regulatory functions of SnRK1 in stress-responsive gene expression
and in plant growth and development.";
Plant Physiol. 158:1955-1964(2012).
[34]
FUNCTION.
PubMed=22902692; DOI=10.4161/psb.21549;
Tsai A.Y., Gazzarrini S.;
"Overlapping and distinct roles of AKIN10 and FUSCA3 in ABA and sugar
signaling during seed germination.";
Plant Signal. Behav. 7:1238-1242(2012).
[35]
INTERACTION WITH CDKE1, AND SUBCELLULAR LOCATION.
PubMed=23229550; DOI=10.1074/jbc.M112.416727;
Ng S., Giraud E., Duncan O., Law S.R., Wang Y., Xu L., Narsai R.,
Carrie C., Walker H., Day D.A., Blanco N.E., Strand A., Whelan J.,
Ivanova A.;
"Cyclin-dependent kinase E1 (CDKE1) provides a cellular switch in
plants between growth and stress responses.";
J. Biol. Chem. 288:3449-3459(2013).
[36]
INTERACTION WITH ABI1 AND PP2CA, DOMAIN, PHOSPHORYLATION AT THR-175,
AND ACTIVITY REGULATION.
PubMed=24179127; DOI=10.1105/tpc.113.114066;
Rodrigues A., Adamo M., Crozet P., Margalha L., Confraria A.,
Martinho C., Elias A., Rabissi A., Lumbreras V., Gonzalez-Guzman M.,
Antoni R., Rodriguez P.L., Baena-Gonzalez E.;
"ABI1 and PP2CA phosphatases are negative regulators of Snf1-related
protein kinase1 signaling in Arabidopsis.";
Plant Cell 25:3871-3884(2013).
[37]
FUNCTION, AND INTERACTION WITH KRP6.
PubMed=23617622; DOI=10.1111/tpj.12218;
Guerinier T., Millan L., Crozet P., Oury C., Rey F., Valot B.,
Mathieu C., Vidal J., Hodges M., Thomas M., Glab N.;
"Phosphorylation of p27(KIP1) homologs KRP6 and 7 by SNF1-related
protein kinase-1 links plant energy homeostasis and cell
proliferation.";
Plant J. 75:515-525(2013).
[38]
INTERACTION WITH CIPK14.
PubMed=25058458; DOI=10.1016/j.bbrc.2014.07.064;
Yan J., Niu F., Liu W.Z., Zhang H., Wang B., Lan W., Che Y., Yang B.,
Luan S., Jiang Y.Q.;
"Arabidopsis CIPK14 positively regulates glucose response.";
Biochem. Biophys. Res. Commun. 450:1679-1683(2014).
[39]
INTERACTION WITH FLZ PROTEINS, INTERACTION WITH GEBP, AND SUBCELLULAR
LOCATION.
PubMed=24600465; DOI=10.3389/fpls.2014.00054;
Nietzsche M., Schiessl I., Boernke F.;
"The complex becomes more complex: protein-protein interactions of
SnRK1 with DUF581 family proteins provide a framework for cell- and
stimulus type-specific SnRK1 signaling in plants.";
Front. Plant Sci. 5:54-54(2014).
[40]
ERRATUM.
PubMed=25544057; DOI=10.3389/fpls.2014.00693;
Boernke F.;
"Corrigendum: The complex becomes more complex: protein-protein
interactions of SnRK1 with DUF581 family proteins provide a framework
for cell- and stimulus type-specific SnRK1 signaling in plants.";
Front. Plant Sci. 5:693-693(2014).
[41]
TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
PubMed=25071807; DOI=10.3389/fpls.2014.00324;
Williams S.P., Rangarajan P., Donahue J.L., Hess J.E., Gillaspy G.E.;
"Regulation of sucrose non-fermenting related kinase 1 genes in
Arabidopsis thaliana.";
Front. Plant Sci. 5:324-324(2014).
[42]
REVIEW.
PubMed=25530701; DOI=10.1007/s12374-014-0902-7;
Sheen J.;
"Master regulators in plant glucose signaling networks.";
J. Plant Biol. 57:67-79(2014).
[43]
FUNCTION.
PubMed=24990996; DOI=10.1128/JVI.00761-14;
Shen W., Dallas M.B., Goshe M.B., Hanley-Bowdoin L.;
"SnRK1 phosphorylation of AL2 delays Cabbage leaf curl virus infection
in Arabidopsis.";
J. Virol. 88:10598-10612(2014).
[44]
INTERACTION WITH MYC2, AND FUNCTION.
PubMed=24890857; DOI=10.1111/pce.12375;
Im J.H., Cho Y.H., Kim G.D., Kang G.H., Hong J.W., Yoo S.D.;
"Inverse modulation of the energy sensor Snf1-related protein kinase 1
on hypoxia adaptation and salt stress tolerance in Arabidopsis
thaliana.";
Plant Cell Environ. 37:2303-2312(2014).
[45]
FUNCTION, INTERACTION WITH IDD8, PHOSPHORYLATION, AND SUBCELLULAR
LOCATION.
STRAIN=cv. Columbia;
PubMed=25929516; DOI=10.1186/s12870-015-0503-8;
Jeong E.-Y., Seo P.J., Woo J.C., Park C.-M.;
"AKIN10 delays flowering by inactivating IDD8 transcription factor
through protein phosphorylation in Arabidopsis.";
BMC Plant Biol. 15:110-110(2015).
[46]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH BZIP63, AND
FUNCTION.
PubMed=26263501; DOI=10.7554/eLife.05828;
Mair A., Pedrotti L., Wurzinger B., Anrather D., Simeunovic A.,
Weiste C., Valerio C., Dietrich K., Kirchler T., Naegele T.,
Vicente Carbajosa J., Hanson J., Baena-Gonzalez E., Chaban C.,
Weckwerth W., Droege-Laser W., Teige M.;
"SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy
response in plants.";
Elife 4:0-0(2015).
[47]
INTERACTION WITH PTL, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=25697797; DOI=10.1093/jxb/erv032;
O'Brien M., Kaplan-Levy R.N., Quon T., Sappl P.G., Smyth D.R.;
"PETAL LOSS, a trihelix transcription factor that represses growth in
Arabidopsis thaliana, binds the energy-sensing SnRK1 kinase AKIN10.";
J. Exp. Bot. 66:2475-2485(2015).
[48]
COMPONENT OF A HETEROTRIMERIC COMPLEX, AND SUBUNIT.
PubMed=25736509; DOI=10.1111/tpj.12813;
Emanuelle S., Hossain M.I., Moller I.E., Pedersen H.L.,
van de Meene A.M., Doblin M.S., Koay A., Oakhill J.S., Scott J.W.,
Willats W.G., Kemp B.E., Bacic A., Gooley P.R., Stapleton D.I.;
"SnRK1 from Arabidopsis thaliana is an atypical AMPK.";
Plant J. 82:183-192(2015).
[49]
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-364, AND
INDUCTION BY SALT AND OXIDATIVE STRESSES.
PubMed=26471895; DOI=10.1104/pp.15.01486;
Chen Y., Hoehenwarter W.;
"Changes in the phosphoproteome and metabolome link early signaling
events to rearrangement of photosynthesis and central metabolism in
salinity and oxidative stress response in Arabidopsis.";
Plant Physiol. 169:3021-3033(2015).
[50]
INTERACTION WITH FLZ3; FLZ9; TCP3; TCP13; HB21 AND HB23.
DOI=10.1016/j.cpb.2015.10.004;
Nietzsche M., Landgraf R., Tohge T., Boernke F.;
"A protein-protein interaction network linking the energy-sensor
kinase SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
Curr. Plant Biol. 5:36-44(2016).
[51]
REVIEW.
PubMed=27812990; DOI=10.1007/978-3-319-43589-3_17;
Margalha L., Valerio C., Baena-Gonzalez E.;
"Plant SnRK1 kinases: structure, regulation, and function.";
EXS 107:403-438(2016).
[52]
PHOSPHORYLATION AT THR-175, MUTAGENESIS OF LYS-48 AND THR-175,
FUNCTION, AND INTERACTION WITH PTP1.
PubMed=27029354; DOI=10.1093/jxb/erw107;
Cho H.Y., Wen T.N., Wang Y.T., Shih M.C.;
"Quantitative phosphoproteomics of protein kinase SnRK1 regulated
protein phosphorylation in Arabidopsis under submergence.";
J. Exp. Bot. 67:2745-2760(2016).
[53]
ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
PubMed=27436712; DOI=10.1105/tpc.16.00301;
Carvalho R.F., Szakonyi D., Simpson C.G., Barbosa I.C., Brown J.W.,
Baena-Gonzalez E., Duque P.;
"The Arabidopsis SR45 splicing factor, a negative regulator of sugar
signaling, modulates SNF1-related protein kinase 1 stability.";
Plant Cell 28:1910-1925(2016).
[54]
SUMOYLATION AT LYS-34; LYS-63 AND LYS-390, INTERACTION WITH SCE1,
MUTAGENESIS OF LYS-34; LYS-63 AND LYS-390, UBIQUITINATION, AND
FUNCTION.
PubMed=26662259; DOI=10.1111/tpj.13096;
Crozet P., Margalha L., Butowt R., Fernandes N., Elias C.A., Orosa B.,
Tomanov K., Teige M., Bachmair A., Sadanandom A., Baena-Gonzalez E.;
"SUMOylation represses SnRK1 signaling in Arabidopsis.";
Plant J. 85:120-133(2016).
[55]
INTERACTION WITH RAPTOR1B, FUNCTION, IDENTIFICATION BY MASS
SPECTROMETRY, PHOSPHORYLATION AT THR-175, AND SUBCELLULAR LOCATION.
PubMed=27545962; DOI=10.1038/srep31697;
Nukarinen E., Naegele T., Pedrotti L., Wurzinger B., Mair A.,
Landgraf R., Boernke F., Hanson J., Teige M., Baena-Gonzalez E.,
Droege-Laser W., Weckwerth W.;
"Quantitative phosphoproteomics reveals the role of the AMPK plant
ortholog SnRK1 as a metabolic master regulator under energy
deprivation.";
Sci. Rep. 6:31697-31697(2016).
[56]
REVIEW.
PubMed=27156455; DOI=10.1016/j.tplants.2016.04.008;
Hulsmans S., Rodriguez M., De Coninck B., Rolland F.;
"The SnRK1 energy sensor in plant biotic interactions.";
Trends Plant Sci. 21:648-661(2016).
[57]
FUNCTION.
PubMed=28263378; DOI=10.1002/1873-3468.12618;
Robertlee J., Kobayashi K., Suzuki M., Muranaka T.;
"AKIN10, a representative Arabidopsis SNF1-related protein kinase 1
(SnRK1), phosphorylates and downregulates plant HMG-CoA reductase.";
FEBS Lett. 591:1159-1166(2017).
[58]
FUNCTION, MUTAGENESIS OF CYS-133 AND CYS-177, SUBUNIT, AND ACTIVITY
REGULATION.
PubMed=28940407; DOI=10.1002/1873-3468.12852;
Wurzinger B., Mair A., Fischer-Schrader K., Nukarinen E., Roustan V.,
Weckwerth W., Teige M.;
"Redox state-dependent modulation of plant SnRK1 kinase activity
differs from AMPK regulation in animals.";
FEBS Lett. 591:3625-3636(2017).
[59]
FUNCTION.
PubMed=28740502; DOI=10.3389/fpls.2017.01201;
Chen L., Su Z.Z., Huang L., Xia F.N., Qi H., Xie L.J., Xiao S.,
Chen Q.F.;
"The AMP-activated protein kinase KIN10 is involved in the regulation
of autophagy in Arabidopsis.";
Front. Plant Sci. 8:1201-1201(2017).
[60]
DEVELOPMENTAL STAGE, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=28922765; DOI=10.1093/jxb/erx233;
Chan A., Carianopol C., Tsai A.Y., Varathanajah K., Chiu R.S.,
Gazzarrini S.;
"SnRK1 phosphorylation of FUSCA3 positively regulates embryogenesis,
seed yield, and plant growth at high temperature in Arabidopsis.";
J. Exp. Bot. 68:4219-4231(2017).
[61]
ERRATUM.
PubMed=29140438; DOI=10.1093/jxb/erx379;
Chan A., Carianopol C., Tsai A.Y., Varatharajah K., Chiu R.S.,
Gazzarrini S.;
"Corrigendum: SnRK1 phosphorylation of FUSCA3 positively regulates
embryogenesis, seed yield, and plant growth at high temperature in
Arabidopsis.";
J. Exp. Bot. 68:5981-5981(2017).
[62]
FUNCTION, AND INTERACTION WITH WRI1.
PubMed=28314829; DOI=10.1105/tpc.17.00019;
Zhai Z., Liu H., Shanklin J.;
"Phosphorylation of WRINKLED1 by KIN10 results in its proteasomal
degradation, providing a link between energy homeostasis and lipid
biosynthesis.";
Plant Cell 29:871-889(2017).
[63]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=28783755; DOI=10.1371/journal.pone.0182591;
Soto-Burgos J., Bassham D.C.;
"SnRK1 activates autophagy via the TOR signaling pathway in
Arabidopsis thaliana.";
PLoS ONE 12:E0182591-E0182591(2017).
[64]
INTERACTION WITH EIN3, AND FUNCTION.
PubMed=28600557; DOI=10.1038/s41598-017-03506-1;
Kim G.D., Cho Y.H., Yoo S.D.;
"Regulatory functions of cellular energy sensor SNF1-related kinase1
for leaf senescence delay through ETHYLENE- INSENSITIVE3 repression.";
Sci. Rep. 7:3193-3193(2017).
[65]
INTERACTION WITH FLZ PROTEINS.
PubMed=29945970; DOI=10.1074/jbc.RA118.002073;
Jamsheer K M., Shukla B.N., Jindal S., Gopan N., Mannully C.T.,
Laxmi A.;
"The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by
the coordinated actions of the FLZ domain and intrinsically disordered
regions.";
J. Biol. Chem. 0:0-0(2018).
[66]
FUNCTION, AND INTERACTION WITH BZIP2 AND BZIP63.
PubMed=29348240; DOI=10.1105/tpc.17.00414;
Pedrotti L., Weiste C., Naegele T., Wolf E., Lorenzin F., Dietrich K.,
Mair A., Weckwerth W., Teige M., Baena-Gonzalez E., Droege-Laser W.;
"Snf1-RELATED KINASE1-controlled C/S1-bZIP signaling activates
alternative mitochondrial metabolic pathways to ensure plant survival
in extended darkness.";
Plant Cell 30:495-509(2018).
[67]
INTERACTION WITH IPK2B, AND FUNCTION.
PubMed=29216370; DOI=10.1093/pcp/pcx186;
Yang Q., Sang S., Chen Y., Wei Z., Wang P.;
"The role of Arabidopsis inositol polyphosphate kinase AtIPK2beta in
glucose suppression of seed germination and seedling development.";
Plant Cell Physiol. 59:343-354(2018).
[68]
INTERACTION WITH FLZ6 AND FLZ10, SUBCELLULAR LOCATION, AND ACTIVITY
REGULATION.
PubMed=29406622; DOI=10.1111/tpj.13854;
Jamsheer K M., Sharma M., Singh D., Mannully C.T., Jindal S.,
Shukla B.N., Laxmi A.;
"FCS-like zinc finger 6 and 10 repress SnRK1 signalling in
Arabidopsis.";
Plant J. 94:232-245(2018).
[69]
FUNCTION.
PubMed=29114081; DOI=10.1104/pp.17.01395;
Simon N.M.L., Kusakina J., Fernandez-Lopez A., Chembath A.,
Belbin F.E., Dodd A.N.;
"The energy-signaling hub SnRK1 is important for sucrose-induced
hypocotyl elongation.";
Plant Physiol. 176:1299-1310(2018).
[70]
INTERACTION WITH GEBP.
PubMed=29192025; DOI=10.1104/pp.17.01461;
Nietzsche M., Guerra T., Alseekh S., Wiermer M., Sonnewald S.,
Fernie A.R., Boernke F.;
"STOREKEEPER RELATED1/G-element binding protein (STKR1) interacts with
protein kinase SnRK1.";
Plant Physiol. 176:1773-1792(2018).
[71]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=29584583; DOI=10.1080/15592324.2018.1457913;
Simon N.M.L., Sawkins E., Dodd A.N.;
"Involvement of the SnRK1 subunit KIN10 in sucrose-induced hypocotyl
elongation.";
Plant Signal. Behav. 2018:E1457913-E1457913(2018).
-!- FUNCTION: Catalytic subunit of the probable trimeric SNF1-related
protein kinase (SnRK) complex, a central regulator of cellular
energy homeostasis, which, in response to seemingly unrelated
darkness, sugar and stress conditions, activates energy-producing
pathways and inhibits energy-consuming processes. May play a role
in a signal transduction cascade regulating gene expression and
carbohydrate metabolism in higher plants. The SnRK complex may
also be involved in the regulation of fatty acid synthesis by
phosphorylation of acetyl-CoA carboxylase and in assimilation of
nitrogen by phosphorylating nitrate reductase (PubMed:17671505).
In vitro, KIN10 exhibits kinase activity on sucrose phosphate
synthase and the kinase activity is inhibited by PRL1
(PubMed:10220464). May be a subunit of a SCF ubiquitin ligase
complex and thus be involved in proteasomal ubiquitination
(PubMed:11387208). Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in
vitro (PubMed:20164192). Cooperates with FUS3 to regulate
developmental phase transitions and lateral organ development and
act both as positive regulators of abscisic acid (ABA) signaling
during germination (PubMed:22026387, PubMed:22902692).
Phosphorylates FUS3 in embryo (PubMed:28922765). Negatively
modulates MYC2 accumulation through its protein phosphorylation
(PubMed:24890857). Phosphorylates geminivirus (CaLCuV, TGMV,
ToMoV) AL2 protein resulting in a delay in the viral DNA
accumulation and symptom appearance during infection
(PubMed:24990996). Regulates bZIP63 activity to alter metabolism
in response to starvation through its protein phosphorylation
(PubMed:26263501). Under sugar deprivation conditions, antagonizes
the IDD8 function in flowering time control by its protein
phosphorylation (PubMed:25929516). Plays a cardinal role in the
control of cell proliferation through inhibition of KRP6 activity
by its protein phosphorylation (PubMed:23617622). Under
submergence, phosphorylates PTP1, leading to the release of the
MPK6 signaling pathway inhibition (PubMed:27029354). Triggers its
own SUMO-mediated proteasomal degradation, establishing a negative
feedback loop that attenuates SnRK1 signaling and prevents
detrimental hyperactivation of stress responses (PubMed:26662259).
Phosphorylates RAPTOR1B in vitro (PubMed:27545962). Phosphorylates
and down-regulates HMGR1S in vitro (PubMed:28263378). Kinase
activity is redox-sensitive (PubMed:28940407). Acts upstream of
TOR in the regulation of autophagy. Required for the activation of
autophagy by many abiotic stresses (PubMed:28783755). Involved in
positive regulation of autophagy, possibly by affecting the
phosphorylation of ATG1 proteins (PubMed:28740502). Negatively
modulates WRI1 accumulation through its protein phosphorylation
(PubMed:28314829). Modulates leaf senescence progression by the
negative regulation of EIN3 accumulation through its protein
phosphorylation (PubMed:28600557). Under extended darkness, C/S1-
bZIP-SnRK1 complex interacts with the histone acetylation
machinery to remodel chromatin and facilitate transcription.
BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-
regulate its transcription (PubMed:29348240). Phosphorylates and
down-regulates IPK2b in vitro (PubMed:29216370). Involved in the
regulation of sucrose-induced hypocotyl elongation under
light/dark cycles (PubMed:29114081, PubMed:29584583).
{ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:11387208,
ECO:0000269|PubMed:17671505, ECO:0000269|PubMed:20164192,
ECO:0000269|PubMed:22026387, ECO:0000269|PubMed:22902692,
ECO:0000269|PubMed:23617622, ECO:0000269|PubMed:24890857,
ECO:0000269|PubMed:24990996, ECO:0000269|PubMed:25929516,
ECO:0000269|PubMed:26263501, ECO:0000269|PubMed:26662259,
ECO:0000269|PubMed:27029354, ECO:0000269|PubMed:27545962,
ECO:0000269|PubMed:28263378, ECO:0000269|PubMed:28314829,
ECO:0000269|PubMed:28600557, ECO:0000269|PubMed:28740502,
ECO:0000269|PubMed:28783755, ECO:0000269|PubMed:28922765,
ECO:0000269|PubMed:28940407, ECO:0000269|PubMed:29114081,
ECO:0000269|PubMed:29216370, ECO:0000269|PubMed:29348240,
ECO:0000269|PubMed:29584583}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:17671505}.
-!- ACTIVITY REGULATION: Activated by phosphorylation at Thr-175 by
GRIK1/SNAK2 and GRIK2/SNAK1 (PubMed:19339507). Inactivated by
dephosphorylation at Thr-175 (PubMed:24179127). Inhibited by
trehalose-6-phosphate (PubMed:19193861). Down-regulated by SR45 by
affecting its stability (PubMed:27436712). Reduced kinase activity
in response to H(2)O(2) treatment. The redox-state of Cys-177
seems to directly influence its kinase activity (PubMed:28940407).
Down-regulated by FLZ6 and FLZ10 (PubMed:29406622).
{ECO:0000269|PubMed:19193861, ECO:0000269|PubMed:19339507,
ECO:0000269|PubMed:24179127, ECO:0000269|PubMed:27436712,
ECO:0000269|PubMed:28940407, ECO:0000269|PubMed:29406622}.
-!- SUBUNIT: Subunit of a probable heterotrimeric complex consisting
of an alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB)
and a gamma (KING or SNF4) non-catalytic regulatory subunits
(PubMed:17028154, PubMed:25736509). Interacts with KINB2, KINB3,
SNF4 and probably with KINB1 and KING1 (PubMed:10929106,
PubMed:11522840, PubMed:15803412, PubMed:17028154,
PubMed:21235649). Interacts with SKP1/ASK1, PAD1, the N-terminus
of PRL1 and the WD40 domain of 5PTase13 (PubMed:10220464,
PubMed:11387208, PubMed:18931139). Potential subunit of a SCF
ubiquitin ligase complex consisting of a SNF1-related protein
kinase, SKP1 and CUL1. The association of the SCF complex with the
proteasome may be mediated by PAD1 and seems to be inhibited by
the interaction with PRL1 (PubMed:11387208). Interacts with ATAF1
(Ref.26). Interacts with ESD4 (PubMed:20855607). Interacts with
SCE1 (PubMed:20855607, PubMed:26662259). Interacts with FUS3
(PubMed:22026387). Interacts with PP2C74 (PubMed:22449965).
Interacts with CDKE1 (PubMed:23229550). Interacts with ABI1 and
PP2CA (PubMed:24179127). Interacts with KRP6 (PubMed:23617622).
Interacts with CIPK14 (PubMed:25058458). Interacts with FLZ
proteins through their FLZ-type zinc finger domains
(PubMed:24600465, PubMed:29945970). Interacts with GEBP/STKR1
(PubMed:24600465, PubMed:29192025). Interacts with MYC2
(PubMed:24890857). Interacts with IDD8 (PubMed:25929516).
Interacts with BZIP63 (PubMed:26263501). Interacts with PTL
(PubMed:25697797). Interacts with FLZ3, FLZ9, TCP3, TCP13,
HB21/ZHD3 and HB23/ZHD10 (Ref.50). Interacts with PTP1
(PubMed:27029354). Interacts with RAPTOR1B (PubMed:27545962).
Forms oligomers in vitro under strongly reducing conditions
(PubMed:28940407). Interacts with WRI1 (PubMed:28314829).
Interacts with EIN3 (PubMed:28600557). Component of a ternary
complex composed of BZIP2-BZIP63 heterodimer and KIN10
(PubMed:29348240). Interacts with IPK2b (PubMed:29216370).
Interacts with FLZ6 and FLZ10 (PubMed:29406622).
{ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:10929106,
ECO:0000269|PubMed:11387208, ECO:0000269|PubMed:11522840,
ECO:0000269|PubMed:15803412, ECO:0000269|PubMed:17028154,
ECO:0000269|PubMed:18931139, ECO:0000269|PubMed:20855607,
ECO:0000269|PubMed:21235649, ECO:0000269|PubMed:22026387,
ECO:0000269|PubMed:22449965, ECO:0000269|PubMed:23229550,
ECO:0000269|PubMed:23617622, ECO:0000269|PubMed:24179127,
ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:24890857,
ECO:0000269|PubMed:25058458, ECO:0000269|PubMed:25697797,
ECO:0000269|PubMed:25736509, ECO:0000269|PubMed:25929516,
ECO:0000269|PubMed:26263501, ECO:0000269|PubMed:26662259,
ECO:0000269|PubMed:27029354, ECO:0000269|PubMed:27545962,
ECO:0000269|PubMed:28314829, ECO:0000269|PubMed:28600557,
ECO:0000269|PubMed:28940407, ECO:0000269|PubMed:29192025,
ECO:0000269|PubMed:29216370, ECO:0000269|PubMed:29348240,
ECO:0000269|PubMed:29406622, ECO:0000269|PubMed:29945970,
ECO:0000269|Ref.26, ECO:0000269|Ref.50}.
-!- INTERACTION:
Q93V58:GRIK1; NbExp=2; IntAct=EBI-2107143, EBI-6399184;
Q5HZ38:GRIK2; NbExp=2; IntAct=EBI-2107143, EBI-6399237;
Q9SCY5:KINB2; NbExp=3; IntAct=EBI-2107143, EBI-2042436;
Q42384:PRL1; NbExp=3; IntAct=EBI-2107143, EBI-1382964;
Q944A6:SNF4; NbExp=2; IntAct=EBI-2107143, EBI-2360649;
-!- SUBCELLULAR LOCATION: Isoform 1: Plastid, chloroplast
{ECO:0000269|PubMed:19211700}. Cytoplasm
{ECO:0000269|PubMed:19211700, ECO:0000269|PubMed:21235649,
ECO:0000269|PubMed:23229550, ECO:0000269|PubMed:24600465,
ECO:0000269|PubMed:25071807, ECO:0000269|PubMed:25697797}. Nucleus
{ECO:0000269|PubMed:18931139, ECO:0000269|PubMed:21235649,
ECO:0000269|PubMed:23229550, ECO:0000269|PubMed:24600465,
ECO:0000269|PubMed:25071807, ECO:0000269|PubMed:25697797,
ECO:0000269|PubMed:25929516}. Golgi apparatus
{ECO:0000269|PubMed:25697797}. Note=Shuttles from the cytoplasm to
the nucleus when associated with a FLZ protein.
{ECO:0000269|PubMed:24600465}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:25071807, ECO:0000269|PubMed:27545962}.
Nucleus {ECO:0000269|PubMed:25071807, ECO:0000269|PubMed:25929516,
ECO:0000269|PubMed:27545962}. Endoplasmic reticulum
{ECO:0000269|PubMed:29406622}. Note=Co-localized with ER marker
when associated with FLZ6 or FLZ10. {ECO:0000269|PubMed:29406622}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=Q38997-2; Sequence=Displayed;
Name=1;
IsoId=Q38997-1; Sequence=VSP_059890;
Note=No experimental confirmation available.
{ECO:0000305|PubMed:25071807};
-!- TISSUE SPECIFICITY: Isoform 2 is widely expressed, especially in
newly developing tissues (PubMed:25697797). Isoform 2 is expressed
throughout the seedling, with highest expression in leaf primordia
and vascular tissue, and the seedling root tip. Isoform 2 is later
expressed in developing lateral root primordia and developing
embryos within siliques (PubMed:25071807). Isoform 1 is widely
expressed but at very low levels (PubMed:25071807).
{ECO:0000269|PubMed:25071807, ECO:0000269|PubMed:25697797}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryo development from
the heart to mature embryo stages. {ECO:0000269|PubMed:28922765}.
-!- INDUCTION: Induced by sucrose (PubMed:10220464). Induced by DCMU
herbicide (PubMed:17671505). Induced by glucose (PubMed:19302419).
Up-regulated by beta-aminobutyric acid (BABA) (PubMed:20484986).
Induced by hypoxia following submergence (PubMed:22232383).
Induced by salt and oxidative stresses (at the protein level)
(PubMed:26471895). {ECO:0000269|PubMed:10220464,
ECO:0000269|PubMed:17671505, ECO:0000269|PubMed:19302419,
ECO:0000269|PubMed:20484986, ECO:0000269|PubMed:22232383,
ECO:0000269|PubMed:26471895}.
-!- DOMAIN: The regulatory domain (RD) contains the auto-inhibitory
domain (AID) that inhibits kinase activity of the protein kinase
domain (KD). {ECO:0000269|PubMed:24179127}.
-!- DOMAIN: The PPI motif mediates the interaction with the ABI
(abscisic acid-insensitive) phosphatases.
{ECO:0000269|PubMed:24179127}.
-!- PTM: Phosphorylated at Thr-175 in response to glucose
(PubMed:19302419). Phosphorylated at Thr-175 under submergence
(PubMed:27029354). Autophosphorylated (PubMed:10220464,
PubMed:24179127, PubMed:25929516). Dephosphorylated at Thr-175 by
ABI1 and PP2CA (PubMed:24179127). {ECO:0000269|PubMed:10220464,
ECO:0000269|PubMed:19302419, ECO:0000269|PubMed:24179127,
ECO:0000269|PubMed:25929516, ECO:0000269|PubMed:27029354}.
-!- PTM: Ubiquitinated (PubMed:26662259). Degradation is mediated by a
CUL4-based E3 ligase that uses PRL1 as a substrate receptor
(PubMed:18223036). {ECO:0000269|PubMed:18223036,
ECO:0000269|PubMed:26662259}.
-!- PTM: Sumoylated by SIZ1 (PubMed:20855607, PubMed:26662259).
Sumoylated SnRK1 is ubiquitinated and degraded by the proteasome
(PubMed:26662259). {ECO:0000269|PubMed:20855607,
ECO:0000269|PubMed:26662259}.
-!- DISRUPTION PHENOTYPE: Anthocyanin accumulation and accelerated
senescence (PubMed:17671505). Starch accumulation during phosphate
deficiency (PubMed:19211700). Reduced sensitivity to glucose
during early development (PubMed:27436712). Increased seed
abortion (PubMed:28922765). Blocked autophagy during abiotic
stresses but not under control conditions (PubMed:28783755).
Enhanced sucrose-induced hypocotyl elongation (PubMed:29584583).
{ECO:0000269|PubMed:17671505, ECO:0000269|PubMed:19211700,
ECO:0000269|PubMed:27436712, ECO:0000269|PubMed:28783755,
ECO:0000269|PubMed:28922765, ECO:0000269|PubMed:29584583}.
-!- MISCELLANEOUS: Overexpressing plants show delayed leaf senescence,
enhanced tolerance to nutrient starvation dependent on a
functional autophagy pathway, enhanced formation of
autophagosomes, and tolerance to drought and submergence
(PubMed:28740502). Overexpression of KIN10 leads to increased
autophagy (PubMed:28783755). Overexpression inhibits sucrose-
induced hypocotyl elongation (PubMed:29114081).
{ECO:0000269|PubMed:28740502, ECO:0000269|PubMed:28783755,
ECO:0000269|PubMed:29114081}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
-----------------------------------------------------------------------
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EMBL; M93023; AAA32736.1; -; Genomic_DNA.
EMBL; X94757; CAA64384.1; -; mRNA.
EMBL; DQ778957; ABH11527.1; -; mRNA.
EMBL; AC008261; AAF26165.1; -; Genomic_DNA.
EMBL; CP002686; AEE73607.1; -; Genomic_DNA.
EMBL; CP002686; AEE73608.1; -; Genomic_DNA.
EMBL; CP002686; AEE73609.1; -; Genomic_DNA.
EMBL; AY093170; AAM13169.1; -; mRNA.
EMBL; BT010386; AAQ56829.1; -; mRNA.
EMBL; X79707; CAA56146.1; -; Genomic_DNA.
EMBL; X86966; CAA60529.1; -; Genomic_DNA.
PIR; JC1446; JC1446.
RefSeq; NP_001118546.1; NM_001125074.2. [Q38997-2]
RefSeq; NP_566130.1; NM_110974.5. [Q38997-2]
RefSeq; NP_850488.1; NM_180157.1. [Q38997-1]
UniGene; At.22965; -.
ProteinModelPortal; Q38997; -.
SMR; Q38997; -.
BioGrid; 6592; 36.
IntAct; Q38997; 10.
STRING; 3702.AT3G01090.2; -.
iPTMnet; Q38997; -.
PaxDb; Q38997; -.
PRIDE; Q38997; -.
EnsemblPlants; AT3G01090.1; AT3G01090.1; AT3G01090. [Q38997-2]
EnsemblPlants; AT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
EnsemblPlants; AT3G01090.3; AT3G01090.3; AT3G01090. [Q38997-2]
GeneID; 821259; -.
Gramene; AT3G01090.1; AT3G01090.1; AT3G01090. [Q38997-2]
Gramene; AT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
Gramene; AT3G01090.3; AT3G01090.3; AT3G01090. [Q38997-2]
KEGG; ath:AT3G01090; -.
Araport; AT3G01090; -.
TAIR; locus:2102132; AT3G01090.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233016; -.
InParanoid; Q38997; -.
KO; K07198; -.
OMA; QGVRRAK; -.
OrthoDB; EOG0936066G; -.
PhylomeDB; Q38997; -.
BRENDA; 2.7.11.1; 399.
Reactome; R-ATH-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-ATH-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-ATH-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
PRO; PR:Q38997; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q38997; baseline and differential.
Genevisible; Q38997; AT.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
GO; GO:0009594; P:detection of nutrient; IDA:TAIR.
GO; GO:0003006; P:developmental process involved in reproduction; IMP:TAIR.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0010150; P:leaf senescence; IMP:TAIR.
GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
GO; GO:0080022; P:primary root development; IMP:TAIR.
GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
GO; GO:1902074; P:response to salt; IEP:UniProtKB.
GO; GO:0005982; P:starch metabolic process; IMP:UniProtKB.
GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
GO; GO:0010050; P:vegetative phase change; IMP:TAIR.
GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:UniProtKB.
InterPro; IPR028375; KA1/Ssp2_C.
InterPro; IPR001772; KA1_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like_sf.
Pfam; PF02149; KA1; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00627; UBA; 1.
SMART; SM00220; S_TKc; 1.
SMART; SM00165; UBA; 1.
SUPFAM; SSF103243; SSF103243; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50032; KA1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50030; UBA; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Carbohydrate metabolism;
Chloroplast; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Fatty acid biosynthesis; Fatty acid metabolism; Golgi apparatus;
Isopeptide bond; Kinase; Lipid biosynthesis; Lipid metabolism;
Nitrate assimilation; Nucleotide-binding; Nucleus; Phosphoprotein;
Plastid; Reference proteome; Serine/threonine-protein kinase;
Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 512 SNF1-related protein kinase catalytic
subunit alpha KIN10.
/FTId=PRO_0000086128.
DOMAIN 19 271 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 292 332 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 463 511 KA1. {ECO:0000255|PROSITE-
ProRule:PRU00565}.
NP_BIND 25 33 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 290 389 Auto-inhibitory domain (AID).
{ECO:0000269|PubMed:24179127}.
REGION 294 512 Regulatory domain (RD).
{ECO:0000269|PubMed:24179127}.
REGION 390 512 PPI. {ECO:0000269|PubMed:24179127}.
ACT_SITE 142 142 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 48 48 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:17671505,
ECO:0000269|PubMed:27029354}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000250|UniProtKB:Q93V58}.
MOD_RES 175 175 Phosphothreonine; by GRIK1 or GRIK2.
{ECO:0000269|PubMed:19302419,
ECO:0000269|PubMed:19339507,
ECO:0000269|PubMed:24179127,
ECO:0000269|PubMed:27029354,
ECO:0000269|PubMed:27545962}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000269|PubMed:26471895}.
CROSSLNK 20 20 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:17272265}.
CROSSLNK 34 34 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:26662259}.
CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:26662259}.
CROSSLNK 390 390 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:26662259}.
VAR_SEQ 1 1 M -> MFKRVDEFNLVSSTIDHRIFKSRM (in isoform
1).
/FTId=VSP_059890.
MUTAGEN 34 34 K->R: Abolishes sumoylation. When
associated with R-63 and R-390.
{ECO:0000269|PubMed:26662259}.
MUTAGEN 48 48 K->M: Abolishes kinase activity. Enhances
sensitivity to submergence.
{ECO:0000269|PubMed:17671505,
ECO:0000269|PubMed:27029354}.
MUTAGEN 63 63 K->R: Abolishes sumoylation. When
associated with R-34 and R-390.
{ECO:0000269|PubMed:26662259}.
MUTAGEN 133 133 C->S: Reduced kinase activity and
retained redox sensitivity.
{ECO:0000269|PubMed:28940407}.
MUTAGEN 175 175 T->A: Abolishes phosphorylation by GRIK1
or GRIK2 leading to inactivation of the
protein. Enhances sensitivity to
submergence.
{ECO:0000269|PubMed:17671505,
ECO:0000269|PubMed:19339507,
ECO:0000269|PubMed:20164192,
ECO:0000269|PubMed:27029354}.
MUTAGEN 175 175 T->D: Enhances tolerance to submergence.
{ECO:0000269|PubMed:27029354}.
MUTAGEN 177 177 C->S: Retained kinase activity and
abolished redox sensitivity.
{ECO:0000269|PubMed:28940407}.
MUTAGEN 390 390 K->R: Abolishes sumoylation. When
associated with R-34 and R-63.
{ECO:0000269|PubMed:26662259}.
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


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