SRK2E_ARATH
ID SRK2E_ARATH Reviewed; 362 AA.
AC Q940H6; O81763;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/threonine-protein kinase SRK2E {ECO:0000303|PubMed:12514244};
DE EC=2.7.11.1 {ECO:0000269|PubMed:12468729, ECO:0000269|PubMed:12514244, ECO:0000269|PubMed:19955427, ECO:0000269|PubMed:26943172, ECO:0000269|PubMed:30361234};
DE AltName: Full=Protein OPEN STOMATA 1 {ECO:0000303|PubMed:12468729};
DE AltName: Full=SNF1-related kinase 2.6 {ECO:0000303|PubMed:12805596};
DE Short=SnRK2.6 {ECO:0000303|PubMed:12805596};
DE AltName: Full=Serine/threonine-protein kinase OST1 {ECO:0000303|PubMed:12468729};
GN Name=SRK2E {ECO:0000303|PubMed:12514244};
GN Synonyms=OST1 {ECO:0000303|PubMed:12468729},
GN SNRK2.6 {ECO:0000303|PubMed:12805596};
GN OrderedLocusNames=At4g33950 {ECO:0000312|Araport:AT4G33950};
GN ORFNames=F17I5.140 {ECO:0000312|EMBL:CAA19877.1};
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] (ISOFORM 1), FUNCTION, MUTAGENESIS OF
RP GLY-33, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12468729; DOI=10.1105/tpc.007906;
RA Mustilli A.-C., Merlot S., Vavasseur A., Fenzi F., Giraudat J.;
RT "Arabidopsis OST1 protein kinase mediates the regulation of stomatal
RT aperture by abscisic acid and acts upstream of reactive oxygen species
RT production.";
RL Plant Cell 14:3089-3099(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP FUNCTION, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=12514244; DOI=10.1093/pcp/pcf188;
RA Yoshida R., Hobo T., Ichimura K., Mizoguchi T., Takahashi F., Aronso J.,
RA Ecker J.R., Shinozaki K.;
RT "ABA-activated SnRK2 protein kinase is required for dehydration stress
RT signaling in Arabidopsis.";
RL Plant Cell Physiol. 43:1473-1483(2002).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-33.
RX PubMed=12047634; DOI=10.1046/j.1365-313x.2002.01322.x;
RA Merlot S., Mustilli A.-C., Genty B., North H., Lefebvre V., Sotta B.,
RA Vavasseur A., Giraudat J.;
RT "Use of infrared thermal imaging to isolate Arabidopsis mutants defective
RT in stomatal regulation.";
RL Plant J. 30:601-609(2002).
RN [7]
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 [8]
RP REVIEW.
RX PubMed=12711225; DOI=10.1016/s1360-1385(03)00052-9;
RA Assmann S.M.;
RT "OPEN STOMATA1 opens the door to ABA signaling in Arabidopsis guard
RT cells.";
RL Trends Plant Sci. 8:151-153(2003).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15292193; DOI=10.1074/jbc.m405259200;
RA Boudsocq M., Barbier-Brygoo H., Lauriere C.;
RT "Identification of nine sucrose nonfermenting 1-related protein kinases 2
RT activated by hyperosmotic and saline stresses in Arabidopsis thaliana.";
RL J. Biol. Chem. 279:41758-41766(2004).
RN [10]
RP FUNCTION.
RX PubMed=15064385; DOI=10.1104/pp.103.032250;
RA Suhita D., Raghavendra A.S., Kwak J.M., Vavasseur A.;
RT "Cytoplasmic alkalization precedes reactive oxygen species production
RT during methyl jasmonate- and abscisic acid-induced stomatal closure.";
RL Plant Physiol. 134:1536-1545(2004).
RN [11]
RP FUNCTION.
RX PubMed=16959575; DOI=10.1016/j.cell.2006.06.054;
RA Melotto M., Underwood W., Koczan J., Nomura K., He S.Y.;
RT "Plant stomata function in innate immunity against bacterial invasion.";
RL Cell 126:969-980(2006).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF GLY-178.
RX PubMed=16682349; DOI=10.1016/j.cub.2006.03.028;
RA Xie X., Wang Y., Williamson L., Holroyd G.H., Tagliavia C., Murchie E.,
RA Theobald J., Knight M.R., Davies W.J., Leyser H.M.O., Hetherington A.M.;
RT "The identification of genes involved in the stomatal response to reduced
RT atmospheric relative humidity.";
RL Curr. Biol. 16:882-887(2006).
RN [13]
RP FUNCTION, MUTAGENESIS OF 1-MET--LEU-12; 283-ALA--MET-362 AND
RP 319-PRO--MET-362, GENE FAMILY, INTERACTION WITH ABI1, AND INDUCTION.
RX PubMed=16365038; DOI=10.1074/jbc.m509820200;
RA Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F.,
RA Shinozaki K.;
RT "The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and
RT integrates abscisic acid (ABA) and osmotic stress signals controlling
RT stomatal closure in Arabidopsis.";
RL J. Biol. Chem. 281:5310-5318(2006).
RN [14]
RP FUNCTION, MUTAGENESIS OF SER-7; SER-18; SER-29; GLY-33; SER-43; SER-175;
RP THR-176; 280-ASN--MET-362; 302-GLY--MET-362; 320-ALA--MET-362;
RP 331-GLY--MET-362 AND 348-ASP--MET-362, PHOSPHORYLATION AT SER-7; SER-18;
RP SER-29; SER-43 AND SER-175, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16766677; DOI=10.1104/pp.106.079327;
RA Belin C., de Franco P.-O., Bourbousse C., Chaignepain S., Schmitter J.-M.,
RA Vavasseur A., Giraudat J., Barbier-Brygoo H., Thomine S.;
RT "Identification of features regulating OST1 kinase activity and OST1
RT function in guard cells.";
RL Plant Physiol. 141:1316-1327(2006).
RN [15]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17307925; DOI=10.1105/tpc.106.048538;
RA Fujii H., Verslues P.E., Zhu J.-K.;
RT "Identification of two protein kinases required for abscisic acid
RT regulation of seed germination, root growth, and gene expression in
RT Arabidopsis.";
RL Plant Cell 19:485-494(2007).
RN [16]
RP INTERACTION WITH ABI1.
RX PubMed=19874541; DOI=10.1111/j.1365-313x.2009.04054.x;
RA Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C.,
RA Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.;
RT "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-
RT interacting proteins in Arabidopsis.";
RL Plant J. 61:290-299(2010).
RN [17]
RP FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH SLAC1 AND PP2CA, ACTIVITY
RP REGULATION, MUTAGENESIS OF LYS-50, AND CATALYTIC ACTIVITY.
RX PubMed=19955427; DOI=10.1073/pnas.0910601106;
RA Lee S.C., Lan W., Buchanan B.B., Luan S.;
RT "A protein kinase-phosphatase pair interacts with an ion channel to
RT regulate ABA signaling in plant guard cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21419-21424(2009).
RN [18]
RP FUNCTION, INTERACTION WITH ABI1, AND MUTAGENESIS OF ASP-140.
RX PubMed=19955405; DOI=10.1073/pnas.0912021106;
RA Geiger D., Scherzer S., Mumm P., Stange A., Marten I., Bauer H., Ache P.,
RA Matschi S., Liese A., Al-Rasheid K.A.S., Romeis T., Hedrich R.;
RT "Activity of guard cell anion channel SLAC1 is controlled by drought-stress
RT signaling kinase-phosphatase pair.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21425-21430(2009).
RN [19]
RP FUNCTION, DISRUPTION PHENOTYPE, AND AUTOPHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=20128877; DOI=10.1111/j.1365-313x.2010.04159.x;
RA Vahisalu T., Puzorjova I., Brosche M., Valk E., Lepiku M., Moldau H.,
RA Pechter P., Wang Y.-S., Lindgren O., Salojaervi J., Loog M.,
RA Kangasjaervi J., Kollist H.;
RT "Ozone-triggered rapid stomatal response involves the production of
RT reactive oxygen species, and is controlled by SLAC1 and OST1.";
RL Plant J. 62:442-453(2010).
RN [20]
RP INTERACTION WITH ABI2, AND ACTIVITY REGULATION.
RX PubMed=22730405; DOI=10.1105/tpc.112.100107;
RA Hua D., Wang C., He J., Liao H., Duan Y., Zhu Z., Guo Y., Chen Z., Gong Z.;
RT "A plasma membrane receptor kinase, GHR1, mediates abscisic acid- and
RT hydrogen peroxide-regulated stomatal movement in Arabidopsis.";
RL Plant Cell 24:2546-2561(2012).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26443375; DOI=10.1093/pcp/pcv146;
RA Mitula F., Tajdel M., Ciesla A., Kasprowicz-Maluski A., Kulik A.,
RA Babula-Skowronska D., Michalak M., Dobrowolska G., Sadowski J.,
RA Ludwikow A.;
RT "Arabidopsis ABA-activated kinase MAPKKK18 is regulated by protein
RT phosphatase 2C ABI1 and the ubiquitin-proteasome pathway.";
RL Plant Cell Physiol. 56:2351-2367(2015).
RN [22]
RP INTERACTION WITH B'ALPHA; B'BETA; B'DELTA; PP2AA2; PP2AA3; PP2A1 AND PP2A2.
RX PubMed=26175513; DOI=10.1104/pp.15.00575;
RA Waadt R., Manalansan B., Rauniyar N., Munemasa S., Booker M.A., Brandt B.,
RA Waadt C., Nusinow D.A., Kay S.A., Kunz H.H., Schumacher K., DeLong A.,
RA Yates J.R. III, Schroeder J.I.;
RT "Identification of Open Stomata1-interacting proteins reveals interactions
RT with sucrose non-fermenting1-related protein kinases2 and with type 2a
RT protein phosphatases that function in abscisic acid responses.";
RL Plant Physiol. 169:760-779(2015).
RN [23]
RP INTERACTION WITH MAPKKK18, AND SUBCELLULAR LOCATION.
RX PubMed=26852793; DOI=10.1080/15592324.2016.1139277;
RA Tajdel M., Mitula F., Ludwikow A.;
RT "Regulation of Arabidopsis MAPKKK18 by ABI1 and SnRK2, components of the
RT ABA signaling pathway.";
RL Plant Signal. Behav. 11:E1139277-E1139277(2016).
RN [24]
RP ACTIVITY REGULATION, INTERACTION WITH I-2; TOPP1 AND TOPP2, AND CATALYTIC
RP ACTIVITY.
RX PubMed=26943172; DOI=10.1371/journal.pgen.1005835;
RA Hou Y.J., Zhu Y., Wang P., Zhao Y., Xie S., Batelli G., Wang B., Duan C.G.,
RA Wang X., Xing L., Lei M., Yan J., Zhu X., Zhu J.K.;
RT "Type one protein phosphatase 1 and its regulatory protein inhibitor 2
RT negatively regulate ABA signaling.";
RL PLoS Genet. 12:E1005835-E1005835(2016).
RN [25]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=cv. Columbia, and cv. Columbia GL1;
RX PubMed=30361234; DOI=10.1105/tpc.18.00441;
RA Sierla M., Horak H., Overmyer K., Waszczak C., Yarmolinsky D.,
RA Maierhofer T., Vainonen J.P., Denessiouk K., Salojaervi J., Laanemets K.,
RA Toldsepp K., Vahisalu T., Gauthier A., Puukko T., Paulin L., Auvinen P.,
RA Geiger D., Hedrich R., Kollist H., Kangasjaervi J.;
RT "The receptor-like pseudokinase GHR1 is required for stomatal closure.";
RL Plant Cell 30:2813-2837(2018).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RX PubMed=21983340; DOI=10.1016/j.jmb.2011.09.041;
RA Yunta C., Martinez-Ripoll M., Zhu J.K., Albert A.;
RT "The structure of Arabidopsis thaliana OST1 provides insights into the
RT kinase regulation mechanism in response to osmotic stress.";
RL J. Mol. Biol. 414:135-144(2011).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
RX PubMed=22160701; DOI=10.1073/pnas.1118651109;
RA Ng L.M., Soon F.F., Zhou X.E., West G.M., Kovach A., Suino-Powell K.M.,
RA Chalmers M.J., Li J., Yong E.L., Zhu J.K., Griffin P.R., Melcher K.,
RA Xu H.E.;
RT "Structural basis for basal activity and autoactivation of abscisic acid
RT (ABA) signaling SnRK2 kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:21259-21264(2011).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 11-362.
RX PubMed=22116026; DOI=10.1126/science.1215106;
RA Soon F.F., Ng L.M., Zhou X.E., West G.M., Kovach A., Tan M.H.,
RA Suino-Powell K.M., He Y., Xu Y., Chalmers M.J., Brunzelle J.S., Zhang H.,
RA Yang H., Jiang H., Li J., Yong E.L., Cutler S., Zhu J.K., Griffin P.R.,
RA Melcher K., Xu H.E.;
RT "Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C
RT phosphatases.";
RL Science 335:85-88(2012).
CC -!- FUNCTION: Activator of the abscisic acid (ABA) signaling pathway that
CC regulates numerous ABA responses, such as stomata closure in response
CC to drought, darkness, high CO(2), plant pathogens, or decreases in
CC atmospheric relative humidity (RH) (PubMed:30361234). Involved in the
CC resistance to drought by avoiding water loss. Required for the stomata
CC closure mediated by pathogen-associated molecular pattern (PAMPs) (e.g.
CC flg22 and LPS) of pathogenic bacteria such as P.syringae pv. tomato
CC (Pst) and E.coli O157:H7. As a plant defense process, stomata are
CC closed transiently in order to limit invaders, but actively reopened by
CC bacteria after a few hours; virulent strains (e.g. Pst DC3000) are more
CC efficient than avirulent strains (e.g. Pst DC3000 AvrRpt2) in reopening
CC stomata. Mediates the phosphorylation and activation of the S-type
CC anion efflux channel SLAC1, and thus promotes stomata closure.
CC Essential for stomatal closure in response to reactive oxygen species
CC (ROS). Promotes MAPKKK18 activity upon abscisic acid (ABA) treatment
CC (PubMed:26443375). {ECO:0000269|PubMed:12047634,
CC ECO:0000269|PubMed:12468729, ECO:0000269|PubMed:12514244,
CC ECO:0000269|PubMed:15064385, ECO:0000269|PubMed:16365038,
CC ECO:0000269|PubMed:16682349, ECO:0000269|PubMed:16766677,
CC ECO:0000269|PubMed:16959575, ECO:0000269|PubMed:17307925,
CC ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:19955427,
CC ECO:0000269|PubMed:20128877, ECO:0000269|PubMed:26443375,
CC ECO:0000269|PubMed:30361234}.
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:12468729, ECO:0000269|PubMed:12514244,
CC ECO:0000269|PubMed:19955427, ECO:0000269|PubMed:26943172,
CC ECO:0000269|PubMed:30361234};
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:12468729,
CC ECO:0000269|PubMed:12514244, ECO:0000269|PubMed:19955427,
CC ECO:0000269|PubMed:26943172, ECO:0000269|PubMed:30361234};
CC -!- ACTIVITY REGULATION: Kinase activity enhanced by ABA and low humidity.
CC Repressed by PP2CA independently of its phosphatase activity. Probably
CC inactivated by ABI1 (PubMed:12468729, PubMed:12514244,
CC PubMed:19955427). Repressed by TOPP1 (PubMed:26943172). Negatively
CC regulated by ABI2 (PubMed:22730405). {ECO:0000269|PubMed:12468729,
CC ECO:0000269|PubMed:12514244, ECO:0000269|PubMed:19955427,
CC ECO:0000269|PubMed:22730405, ECO:0000269|PubMed:26943172}.
CC -!- SUBUNIT: Interacts with ABI1, PP2CA and SLAC1 (PubMed:16365038,
CC PubMed:19874541, PubMed:19955405, PubMed:19955427). Interacts with
CC B'ALPHA, B'BETA, B'DELTA, PP2AA2, PP2AA3, PP2A1 and PP2A2
CC (PubMed:26175513). Associates with MAPKKK18 within the nucleus
CC (PubMed:26852793). Interacts with I-2, TOPP1 and TOPP2
CC (PubMed:26943172). Interacts with ABI2 (PubMed:22730405).
CC {ECO:0000269|PubMed:16365038, ECO:0000269|PubMed:19874541,
CC ECO:0000269|PubMed:19955405, ECO:0000269|PubMed:19955427,
CC ECO:0000269|PubMed:22730405, ECO:0000269|PubMed:26175513,
CC ECO:0000269|PubMed:26852793, ECO:0000269|PubMed:26943172}.
CC -!- INTERACTION:
CC Q940H6; Q9M7Q4: ABF2; NbExp=2; IntAct=EBI-782514, EBI-1538369;
CC Q940H6; P49597: ABI1; NbExp=15; IntAct=EBI-782514, EBI-782526;
CC Q940H6; O04719-1: ABI2; NbExp=5; IntAct=EBI-782514, EBI-15803514;
CC Q940H6; Q9FLZ8: EDL2; NbExp=3; IntAct=EBI-782514, EBI-25521013;
CC Q940H6; Q9CAJ0: HAB1; NbExp=5; IntAct=EBI-782514, EBI-2309302;
CC Q940H6; Q2MHE4: HT1; NbExp=2; IntAct=EBI-782514, EBI-11174828;
CC Q940H6; P49598: PP2CA; NbExp=2; IntAct=EBI-782514, EBI-1764934;
CC Q940H6; O48538: RBOHF; NbExp=4; IntAct=EBI-782514, EBI-7197253;
CC Q940H6; Q9FIF5: SAG113; NbExp=2; IntAct=EBI-782514, EBI-2363373;
CC Q940H6; Q9LD83: SLAC1; NbExp=8; IntAct=EBI-782514, EBI-11174918;
CC Q940H6; Q940H6: SRK2E; NbExp=2; IntAct=EBI-782514, EBI-782514;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26852793}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q940H6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q940H6-2; Sequence=VSP_034923;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, flowers, stems, and
CC roots, but restricted to guard cells and vascular tissue.
CC {ECO:0000269|PubMed:12468729, ECO:0000269|PubMed:15292193,
CC ECO:0000269|PubMed:16766677, ECO:0000269|PubMed:17307925}.
CC -!- INDUCTION: In roots by ABA in an ABI1-dependent manner and by osmotic
CC stress (e.g. sorbitol) in an ABI1-independent manner, but in leaves by
CC low humidity (at protein level). Also induced by salt stress.
CC {ECO:0000269|PubMed:15292193, ECO:0000269|PubMed:16365038}.
CC -!- PTM: Autophosphorylation on residues Ser-7, Ser-18, Ser-29, Ser-43,
CC Ser-175 and/or Thr-176 (PubMed:30361234). Only the phosphorylation of
CC Ser-175 is crucial for the kinase activity. The phosphorylation of Ser-
CC 43 may repress the ABA signaling pathway in absence of ABA.
CC {ECO:0000269|PubMed:16766677, ECO:0000269|PubMed:30361234}.
CC -!- DISRUPTION PHENOTYPE: Impaired ozone-triggered rapid transient decrease
CC (RTD) in stomatal conductance (PubMed:20128877). Impaired induction of
CC MKKK18 activity after 90 minutes of abscisic acid (ABA) treatment
CC (PubMed:26443375). Delayed CO(2)-mediated and darkness-induced and
CC reduced abscisic acid (ABA)-triggered stomatal closure
CC (PubMed:30361234). {ECO:0000269|PubMed:20128877,
CC ECO:0000269|PubMed:26443375, ECO:0000269|PubMed:30361234}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA19877.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80112.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ316009; CAC87047.1; -; Genomic_DNA.
DR EMBL; AL031032; CAA19877.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80112.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86299.1; -; Genomic_DNA.
DR EMBL; AY054624; AAK96815.1; -; mRNA.
DR EMBL; AY081538; AAM10100.1; -; mRNA.
DR PIR; T05223; T05223.
DR RefSeq; NP_567945.1; NM_119556.3. [Q940H6-1]
DR PDB; 3UC4; X-ray; 2.30 A; A/B=1-362.
DR PDB; 3UDB; X-ray; 2.57 A; A/B/C/D/E/F=1-317.
DR PDB; 3UJG; X-ray; 2.60 A; A=11-362.
DR PDB; 3ZUT; X-ray; 2.50 A; A/B=1-362.
DR PDB; 3ZUU; X-ray; 2.70 A; A/B=1-362.
DR PDBsum; 3UC4; -.
DR PDBsum; 3UDB; -.
DR PDBsum; 3UJG; -.
DR PDBsum; 3ZUT; -.
DR PDBsum; 3ZUU; -.
DR AlphaFoldDB; Q940H6; -.
DR SMR; Q940H6; -.
DR BioGRID; 14823; 52.
DR DIP; DIP-36705N; -.
DR IntAct; Q940H6; 14.
DR MINT; Q940H6; -.
DR STRING; 3702.AT4G33950.1; -.
DR iPTMnet; Q940H6; -.
DR PaxDb; Q940H6; -.
DR PRIDE; Q940H6; -.
DR EnsemblPlants; AT4G33950.1; AT4G33950.1; AT4G33950. [Q940H6-1]
DR GeneID; 829541; -.
DR Gramene; AT4G33950.1; AT4G33950.1; AT4G33950. [Q940H6-1]
DR KEGG; ath:AT4G33950; -.
DR Araport; AT4G33950; -.
DR TAIR; locus:2118929; AT4G33950.
DR eggNOG; KOG0583; Eukaryota.
DR InParanoid; Q940H6; -.
DR PhylomeDB; Q940H6; -.
DR PRO; PR:Q940H6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q940H6; baseline and differential.
DR Genevisible; Q940H6; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0019903; F:protein 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; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; TAS:TAIR.
DR GO; GO:0071485; P:cellular response to absence of light; IMP:UniProtKB.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:CACAO.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010359; P:regulation of anion channel activity; IDA:UniProtKB.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:1902456; P:regulation of stomatal opening; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IDA:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IDA:TAIR.
DR GO; GO:0009651; P:response to salt stress; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR GO; GO:0005985; P:sucrose metabolic process; IMP:TAIR.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:TAIR.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:TAIR.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Alternative splicing;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Plant defense; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..362
FT /note="Serine/threonine-protein kinase SRK2E"
FT /id="PRO_0000345160"
FT DOMAIN 21..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 160..186
FT /note="Activation loop"
FT /evidence="ECO:0000305|PubMed:16766677"
FT REGION 283..318
FT /note="Domain I; osmotic stress response, required for the
FT kinase activity"
FT /evidence="ECO:0000305|PubMed:16365038"
FT REGION 319..362
FT /note="Domain II; ABA response and ABI1 binding"
FT /evidence="ECO:0000305|PubMed:16365038"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 7
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16766677"
FT MOD_RES 18
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16766677"
FT MOD_RES 29
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16766677"
FT MOD_RES 43
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:16766677"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16766677"
FT VAR_SEQ 26..57
FT /note="DIGSGNFGVARLMRDKQSNELVAVKYIERGEK -> MVGLFVFVQ (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034923"
FT MUTAGEN 1..12
FT /note="Missing: Reduced kinase activity in response to ABA
FT and osmotic stress."
FT /evidence="ECO:0000269|PubMed:16365038"
FT MUTAGEN 7
FT /note="S->A,D: Normal kinase activity, but loss of ABA
FT signaling pathway positive regulation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 18
FT /note="S->A,D: Normal kinase activity, but loss of ABA
FT signaling pathway positive regulation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 29
FT /note="S->A,D: Normal kinase activity, but loss of ABA
FT signaling pathway positive regulation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 33
FT /note="G->R: In ost1-2; loss of kinase activity, and
FT insensitivity to ABA during the stomatal aperture
FT regulation."
FT /evidence="ECO:0000269|PubMed:12047634,
FT ECO:0000269|PubMed:12468729, ECO:0000269|PubMed:16766677"
FT MUTAGEN 43
FT /note="S->A,D: Normal kinase activity, but constitutive ABA
FT signaling pathway activation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 50
FT /note="K->N: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:19955427"
FT MUTAGEN 140
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:19955405"
FT MUTAGEN 175
FT /note="S->A,D: Loss of kinase activity, and loss of ABA
FT signaling pathway positive regulation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 176
FT /note="T->A: Normal kinase activity, and normal regulation
FT of the ABA signaling pathway."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 176
FT /note="T->D: Reduced kinase activity, but normal regulation
FT of the ABA signaling pathway."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 178
FT /note="G->Q: In ost1-4; no stomatal closure when RH
FT decreases, and insensitivity to ABA."
FT /evidence="ECO:0000269|PubMed:16682349"
FT MUTAGEN 280..362
FT /note="Missing: Loss of kinase activity, and loss of ABA
FT signaling pathway positive regulation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 283..362
FT /note="Missing: Loss of kinase activity in response to ABA
FT and osmotic stress."
FT /evidence="ECO:0000269|PubMed:16365038"
FT MUTAGEN 302..362
FT /note="Missing: Loss of kinase activity, and loss of ABA
FT signaling pathway positive regulation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 319..362
FT /note="Missing: Loss of kinase activity specifically in
FT response to ABA, and impaired interaction with ABI1."
FT /evidence="ECO:0000269|PubMed:16365038"
FT MUTAGEN 320..362
FT /note="Missing: Normal kinase activity, but loss of ABA
FT signaling pathway positive regulation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 331..362
FT /note="Missing: Normal kinase activity, but loss of ABA
FT signaling pathway positive regulation."
FT /evidence="ECO:0000269|PubMed:16766677"
FT MUTAGEN 348..362
FT /note="Missing: Normal kinase activity, and normal
FT regulation of the ABA signaling pathway."
FT /evidence="ECO:0000269|PubMed:16766677"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3UJG"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3UC4"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:3UC4"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 114..134
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3ZUT"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3UJG"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3UJG"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 195..212
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:3UC4"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:3UJG"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3UC4"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:3UC4"
SQ SEQUENCE 362 AA; 41048 MW; FFBCCA1474839B88 CRC64;
MDRPAVSGPM DLPIMHDSDR YELVKDIGSG NFGVARLMRD KQSNELVAVK YIERGEKIDE
NVKREIINHR SLRHPNIVRF KEVILTPTHL AIVMEYASGG ELFERICNAG RFSEDEARFF
FQQLISGVSY CHAMQVCHRD LKLENTLLDG SPAPRLKICD FGYSKSSVLH SQPKSTVGTP
AYIAPEVLLK KEYDGKVADV WSCGVTLYVM LVGAYPFEDP EEPKNFRKTI HRILNVQYAI
PDYVHISPEC RHLISRIFVA DPAKRISIPE IRNHEWFLKN LPADLMNDNT MTTQFDESDQ
PGQSIEEIMQ IIAEATVPPA GTQNLNHYLT GSLDIDDDME EDLESDLDDL DIDSSGEIVY
AM
