AHK4_ARATH
ID AHK4_ARATH Reviewed; 1080 AA.
AC Q9C5U0; A5YY60; A5YY75; Q9C5T8; Q9C5T9; Q9FDZ3; Q9SIT0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Histidine kinase 4;
DE EC=2.7.13.3;
DE AltName: Full=Arabidopsis histidine kinase 4;
DE Short=AtHK4;
DE AltName: Full=Cytokinin receptor CYTOKININ RESPONSE 1;
DE Short=AtCRE1;
DE Short=Cytokinin receptor CRE1;
DE AltName: Full=Phosphoprotein phosphatase AHK4;
DE EC=3.1.3.16;
DE AltName: Full=Protein AUTHENTIC HIS-KINASE 4;
DE AltName: Full=Protein ROOT AS IN WOL 1;
DE AltName: Full=Protein WOODEN LEG;
GN Name=AHK4; Synonyms=CRE1, RAW1, WOL; OrderedLocusNames=At2g01830;
GN ORFNames=T23K3.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, FUNCTION, AND MUTAGENESIS OF THR-301.
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=11114883; DOI=10.1101/gad.189200;
RA Maehoenen A.P., Bonke M., Kauppinen L., Riikonen M., Benfey P.N.,
RA Helariutta Y.;
RT "A novel two-component hybrid molecule regulates vascular morphogenesis of
RT the Arabidopsis root.";
RL Genes Dev. 14:2938-2943(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF HIS-482; GLY-490 AND ASP-996.
RC STRAIN=cv. Wassilewskija; TISSUE=Seedling;
RX PubMed=11234017; DOI=10.1038/35059117;
RA Inoue T., Higuchi M., Hashimoto Y., Seki M., Kobayashi M., Kato T.,
RA Tabata S., Shinozaki K., Kakimoto T.;
RT "Identification of CRE1 as a cytokinin receptor from Arabidopsis.";
RL Nature 409:1060-1063(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=11230578; DOI=10.1093/pcp/pce015;
RA Ueguchi C., Koizumi H., Suzuki T., Mizuno T.;
RT "Novel family of sensor histidine kinase genes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 42:231-235(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 [GENOMIC DNA] OF 722-983, AND VARIANT ASN-765.
RC STRAIN=cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1,
RC cv. Edi-0, cv. Ga-0, cv. Kas-2, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0,
RC cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Se-0,
RC cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1, and cv. Wassilewskija;
RX PubMed=17435248; DOI=10.1534/genetics.107.071928;
RA Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
RT "The genetic architecture of shoot branching in Arabidopsis thaliana: a
RT comparative assessment of candidate gene associations vs. quantitative
RT trait locus mapping.";
RL Genetics 176:1223-1236(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH AHP1; AHP2; AHP3 AND AHP5.
RX PubMed=11230563; DOI=10.1093/pcp/pce037;
RA Suzuki T., Miwa K., Ishikawa K., Yamada H., Aiba H., Mizuno T.;
RT "The Arabidopsis sensor His-kinase, AHk4, can respond to cytokinins.";
RL Plant Cell Physiol. 42:107-113(2001).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11479382; DOI=10.1093/pcp/pce094;
RA Ueguchi C., Sato S., Kato T., Tabata S.;
RT "The AHK4 gene involved in the cytokinin-signaling pathway as a direct
RT receptor molecule in Arabidopsis thaliana.";
RL Plant Cell Physiol. 42:751-755(2001).
RN [9]
RP FUNCTION, ACTIVATION BY CYTOKININS, AND MUTAGENESIS OF THR-301.
RX PubMed=11577198; DOI=10.1093/pcp/pce127;
RA Yamada H., Suzuki T., Terada K., Takei K., Ishikawa K., Miwa K.,
RA Yamashino T., Mizuno T.;
RT "The Arabidopsis AHK4 histidine kinase is a cytokinin-binding receptor that
RT transduces cytokinin signals across the membrane.";
RL Plant Cell Physiol. 42:1017-1023(2001).
RN [10]
RP REVIEW.
RX PubMed=11435149; DOI=10.1016/s1360-1385(01)02011-8;
RA Schmuelling T.;
RT "CREam of cytokinin signalling: receptor identified.";
RL Trends Plant Sci. 6:281-284(2001).
RN [11]
RP REVIEW.
RX PubMed=12589073; DOI=10.1266/ggs.77.383;
RA Oka A., Sakai H., Iwakoshi S.;
RT "His-Asp phosphorelay signal transduction in higher plants: receptors and
RT response regulators for cytokinin signaling in Arabidopsis thaliana.";
RL Genes Genet. Syst. 77:383-391(2002).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF GLY-490.
RX PubMed=12354925; DOI=10.1093/pcp/pcf121;
RA Kiba T., Yamada H., Mizuno T.;
RT "Characterization of the ARR15 and ARR16 response regulators with special
RT reference to the cytokinin signaling pathway mediated by the AHK4 histidine
RT kinase in roots of Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:1059-1066(2002).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND MUTAGENESIS OF GLY-493;
RP THR-1008 AND ALA-1032.
RX PubMed=12410813; DOI=10.1046/j.1365-313x.2002.01431.x;
RA Franco-Zorrilla J.M., Martin A.C., Solano R., Rubio V., Leyva A.,
RA Paz-Ares J.;
RT "Mutations at CRE1 impair cytokinin-induced repression of phosphate
RT starvation responses in Arabidopsis.";
RL Plant J. 32:353-360(2002).
RN [14]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12068096; DOI=10.1104/pp.005504;
RA Hwang I., Chen H.-C., Sheen J.;
RT "Two-component signal transduction pathways in Arabidopsis.";
RL Plant Physiol. 129:500-515(2002).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15155880; DOI=10.1105/tpc.021477;
RA Nishimura C., Ohashi Y., Sato S., Kato T., Tabata S., Ueguchi C.;
RT "Histidine kinase homologs that act as cytokinin receptors possess
RT overlapping functions in the regulation of shoot and root growth in
RT Arabidopsis.";
RL Plant Cell 16:1365-1377(2004).
RN [16]
RP FUNCTION.
RX PubMed=15509853; DOI=10.1093/pcp/pch132;
RA Spichal L., Rakova N.Y., Riefler M., Mizuno T., Romanov G.A., Strnad M.,
RA Schmuelling T.;
RT "Two cytokinin receptors of Arabidopsis thaliana, CRE1/AHK4 and AHK3,
RT differ in their ligand specificity in a bacterial assay.";
RL Plant Cell Physiol. 45:1299-1305(2004).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF THR-301 AND LEU-529.
RX PubMed=15053761; DOI=10.1111/j.1365-313x.2004.02023.x;
RA de Leon B.G.-P., Zorrilla J.M.F., Rubio V., Dahiya P., Paz-Ares J.,
RA Leyva A.;
RT "Interallelic complementation at the Arabidopsis CRE1 locus uncovers
RT independent pathways for the proliferation of vascular initials and
RT canonical cytokinin signalling.";
RL Plant J. 38:70-79(2004).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF GLY-490.
RX PubMed=15144379; DOI=10.1111/j.1365-313x.2004.02079.x;
RA Maruyama-Nakashita A., Nakamura Y., Yamaya T., Takahashi H.;
RT "A novel regulatory pathway of sulfate uptake in Arabidopsis roots:
RT implication of CRE1/WOL/AHK4-mediated cytokinin-dependent regulation.";
RL Plant J. 38:779-789(2004).
RN [19]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15166290; DOI=10.1073/pnas.0402887101;
RA Higuchi M., Pischke M.S., Maehoenen A.P., Miyawaki K., Hashimoto Y.,
RA Seki M., Kobayashi M., Shinozaki K., Kato T., Tabata S., Helariutta Y.,
RA Sussman M.R., Kakimoto T.;
RT "In planta functions of the Arabidopsis cytokinin receptor family.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8821-8826(2004).
RN [20]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16246292; DOI=10.1016/j.ab.2005.09.012;
RA Romanov G.A., Spichal L., Lomin S.N., Strnad M., Schmuelling T.;
RT "A live cell hormone-binding assay on transgenic bacteria expressing a
RT eukaryotic receptor protein.";
RL Anal. Biochem. 347:129-134(2005).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15923327; DOI=10.1104/pp.105.060517;
RA Franco-Zorrilla J.M., Martin A.C., Leyva A., Paz-Ares J.;
RT "Interaction between phosphate-starvation, sugar, and cytokinin signaling
RT in Arabidopsis and the roles of cytokinin receptors CRE1/AHK4 and AHK3.";
RL Plant Physiol. 138:847-857(2005).
RN [22]
RP FUNCTION.
RX PubMed=15728338; DOI=10.1104/pp.104.057174;
RA Mok M.C., Martin R.C., Dobrev P.I., Vankova R., Ho P.S.,
RA Yonekura-Sakakibara K., Sakakibara H., Mok D.W.;
RT "Topolins and hydroxylated thidiazuron derivatives are substrates of
RT cytokinin O-glucosyltransferase with position specificity related to
RT receptor recognition.";
RL Plant Physiol. 137:1057-1066(2005).
RN [23]
RP FUNCTION, PHOSPHORYLATION AT HIS-482, MUTAGENESIS OF THR-301; HIS-482;
RP PHE-708 AND ASP-996, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=16753566; DOI=10.1016/j.cub.2006.04.030;
RA Maehoenen A.P., Higuchi M., Toermaekangas K., Miyawaki K., Pischke M.S.,
RA Sussman M.R., Helariutta Y., Kakimoto T.;
RT "Cytokinins regulate a bidirectional phosphorelay network in Arabidopsis.";
RL Curr. Biol. 16:1116-1122(2006).
RN [24]
RP INTERACTION WITH AHP1; AHP2; AHP3; AHP5 AND AHK3.
RX PubMed=16965536; DOI=10.1111/j.1742-4658.2006.05467.x;
RA Dortay H., Mehnert N., Buerkle L., Schmuelling T., Heyl A.;
RT "Analysis of protein interactions within the cytokinin-signaling pathway of
RT Arabidopsis thaliana.";
RL FEBS J. 273:4631-4644(2006).
RN [25]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17075078; DOI=10.1093/jxb/erl179;
RA Romanov G.A., Lomin S.N., Schmuelling T.;
RT "Biochemical characteristics and ligand-binding properties of Arabidopsis
RT cytokinin receptor AHK3 compared to CRE1/AHK4 as revealed by a direct
RT binding assay.";
RL J. Exp. Bot. 57:4051-4058(2006).
RN [26]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16361392; DOI=10.1105/tpc.105.037796;
RA Riefler M., Novak O., Strnad M., Schmuelling T.;
RT "Arabidopsis cytokinin receptor mutants reveal functions in shoot growth,
RT leaf senescence, seed size, germination, root development, and cytokinin
RT metabolism.";
RL Plant Cell 18:40-54(2006).
RN [27]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF MET-459 AND GLY-490.
RX PubMed=16357038; DOI=10.1093/pcp/pci240;
RA Kuroha T., Ueguchi C., Sakakibara H., Satoh S.;
RT "Cytokinin receptors are required for normal development of auxin-
RT transporting vascular tissues in the hypocotyl but not in adventitious
RT roots.";
RL Plant Cell Physiol. 47:234-243(2006).
RN [28]
RP FUNCTION.
RX PubMed=17216481; DOI=10.1007/s00425-006-0464-0;
RA Horiuchi J., Badri D.V., Kimball B.A., Negre F., Dudareva N., Paschke M.W.,
RA Vivanco J.M.;
RT "The floral volatile, methyl benzoate, from snapdragon (Antirrhinum majus)
RT triggers phytotoxic effects in Arabidopsis thaliana.";
RL Planta 226:1-10(2007).
RN [29]
RP FUNCTION, AND MUTAGENESIS OF THR-301; GLY-435; PHE-436; MET-447; VAL-471
RP AND MET-494.
RX PubMed=17956858; DOI=10.1093/pcp/pcm145;
RA Miwa K., Ishikawa K., Terada K., Yamada H., Suzuki T., Yamashino T.,
RA Mizuno T.;
RT "Identification of amino acid substitutions that render the Arabidopsis
RT cytokinin receptor histidine kinase AHK4 constitutively active.";
RL Plant Cell Physiol. 48:1809-1814(2007).
RN [30]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18077346; DOI=10.1073/pnas.0706547105;
RA Tran L.S., Urao T., Qin F., Maruyama K., Kakimoto T., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine kinases
RT in response to abscisic acid, drought, and salt stress in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20623-20628(2007).
RN [31]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17965178; DOI=10.1104/pp.107.107953;
RA Lopez-Bucio J., Millan-Godinez M., Mendez-Bravo A., Morquecho-Contreras A.,
RA Ramirez-Chavez E., Molina-Torres J., Perez-Torres A., Higuchi M.,
RA Kakimoto T., Herrera-Estrella L.;
RT "Cytokinin receptors are involved in alkamide regulation of root and shoot
RT development in Arabidopsis.";
RL Plant Physiol. 145:1703-1713(2007).
RN [32]
RP FUNCTION.
RX PubMed=18571199; DOI=10.1016/j.jmb.2008.05.044;
RA Kopecny D., Sebela M., Briozzo P., Spichal L., Houba-Herin N., Masek V.,
RA Joly N., Madzak C., Anzenbacher P., Laloue M.;
RT "Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack FAD
RT cofactor.";
RL J. Mol. Biol. 380:886-899(2008).
RN [33]
RP INTERACTION WITH AHP2; AMPD; WNK5 AND AT4G15630.
RX PubMed=18642946; DOI=10.1021/pr0703831;
RA Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT "Toward an interaction map of the two-component signaling pathway of
RT Arabidopsis thaliana.";
RL J. Proteome Res. 7:3649-3660(2008).
RN [34]
RP FUNCTION.
RX PubMed=18785832; DOI=10.1094/mpmi-21-10-1371;
RA Vadassery J., Ritter C., Venus Y., Camehl I., Varma A., Shahollari B.,
RA Novak O., Strnad M., Ludwig-Mueller J., Oelmueller R.;
RT "The role of auxins and cytokinins in the mutualistic interaction between
RT Arabidopsis and Piriformospora indica.";
RL Mol. Plant Microbe Interact. 21:1371-1383(2008).
RN [35]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18397377; DOI=10.1111/j.1365-313x.2008.03502.x;
RA Seguela M., Briat J.-F., Vert G., Curie C.;
RT "Cytokinins negatively regulate the root iron uptake machinery in
RT Arabidopsis through a growth-dependent pathway.";
RL Plant J. 55:289-300(2008).
RN [36]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=19032596; DOI=10.1111/j.1742-4658.2008.06777.x;
RA Spichal L., Werner T., Popa I., Riefler M., Schmuelling T., Strnad M.;
RT "The purine derivative PI-55 blocks cytokinin action via receptor
RT inhibition.";
RL FEBS J. 276:244-253(2009).
RN [37]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20110319; DOI=10.1242/dev.041426;
RA Skylar A., Hong F., Chory J., Weigel D., Wu X.;
RT "STIMPY mediates cytokinin signaling during shoot meristem establishment in
RT Arabidopsis seedlings.";
RL Development 137:541-549(2010).
RN [38]
RP ACTIVITY REGULATION.
RX PubMed=20189204; DOI=10.1016/j.phytochem.2010.01.018;
RA Nisler J., Zatloukal M., Popa I., Dolezal K., Strnad M., Spichal L.;
RT "Cytokinin receptor antagonists derived from 6-benzylaminopurine.";
RL Phytochemistry 71:823-830(2010).
RN [39]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21709172; DOI=10.1104/pp.111.180539;
RA Wulfetange K., Lomin S.N., Romanov G.A., Stolz A., Heyl A., Schmuelling T.;
RT "The cytokinin receptors of Arabidopsis are located mainly to the
RT endoplasmic reticulum.";
RL Plant Physiol. 156:1808-1818(2011).
RN [40]
RP INTERACTION WITH FBR12 AND AHP1.
RX PubMed=24163315; DOI=10.1105/tpc.113.116236;
RA Ren B., Chen Q., Hong S., Zhao W., Feng J., Feng H., Zuo J.;
RT "The Arabidopsis eukaryotic translation initiation factor eIF5A-2 regulates
RT root protoxylem development by modulating cytokinin signaling.";
RL Plant Cell 25:3841-3857(2013).
RN [41] {ECO:0007744|PDB:3T4J, ECO:0007744|PDB:3T4K, ECO:0007744|PDB:3T4L, ECO:0007744|PDB:3T4O, ECO:0007744|PDB:3T4Q, ECO:0007744|PDB:3T4S, ECO:0007744|PDB:3T4T}
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 149-418 IN COMPLEXES WITH THE
RP CYTOKININS TRANS-ZEATIN; DIHYDROZEATIN; N(6)-DIMETHYLALLYLADENINE AND
RP KINETIN OR THE HERBICIDE THIDIAZURON, SUBUNIT, AND MUTAGENESIS OF ALA-225;
RP ALA-227; TYR-273; MET-279; ASP-285; THR-301; PRO-303; PHE-304; LEU-306;
RP LEU-307; THR-317 AND GLY-343.
RX PubMed=21964459; DOI=10.1038/nchembio.667;
RA Hothorn M., Dabi T., Chory J.;
RT "Structural basis for cytokinin recognition by Arabidopsis thaliana
RT histidine kinase 4.";
RL Nat. Chem. Biol. 7:766-768(2011).
CC -!- FUNCTION: Cytokinins (CK) receptor related to bacterial two-component
CC regulators. Binds also the synthetic urea-type cytokinin thidiazuron, a
CC potent defoliant and herbicide. Functions as a histidine kinase and
CC transmits the stress signal to a downstream MAPK cascade. This protein
CC undergoes an ATP-dependent autophosphorylation at a conserved histidine
CC residue in the kinase core, and a phosphoryl group is then transferred
CC to a conserved aspartate residue in the receiver domain. In the
CC presence of cytokinin, feeds phosphate to phosphorelay-integrating
CC histidine phosphotransfer protein (HPt) and activates subsequent
CC cascade. In the absence of cytokinin, removes phosphate from HPt
CC proteins, decreasing the system phosphoload. Involved in meristems
CC establishment in seedlings. Acts as a redundant negative regulator of
CC drought and salt stress responses, and abscisic acid (ABA) signaling in
CC a cytokinin-dependent manner. Required to set vascular asymmetric cell
CC divisions that establish phloem and procambium cell lines. Redundant
CC positive regulator of cytokinin signaling that regulates many
CC developmental processes including seed germination, cell division, seed
CC size, chlorophyll retention during leaf senescence, root repression and
CC shoot promotion. Can interact with isoprenoid-type cytokinins trans-
CC zeatin (tZ and tZR), isopentenyladenine (iP), and isopentenyladenosine
CC (iPR), the meta hydroxylated derivative of benzyladenine m-topolin,
CC buta-2,3-dienyladenine (HA-8), penta-2,3-dienyladenine (HA-1), 4-
CC methyl-penta-2,3-dienyladenine (HA-10), 4-hydroxy-2-butynyladenine
CC (RM1), 2-butynyladenine (RM6), and to a lower extent, with cis-zeatin
CC (cZ), zeatin riboside and dihydrozeatin (DZ). Together with AHK3,
CC involved in the cytokinin-dependent responses to Pi starvation and
CC sucrose stresses. Required for the formation of auxin-transporting
CC vascular tissues in the hypocotyl, and primary and lateral roots, but
CC not in adventitious roots, thus leading to auxin basipetal transport
CC that regulates root development and branching. Involved in alkamides
CC (e.g. N-isobutyl decanamide) and N-acylethanolamides (NAE) signaling
CC that control meristematic activity and differentiation processes during
CC plant development. Prevents the uptake of sulfate by mediating
CC cytokinin-dependent down-regulation of high-affinity sulfate
CC transporters (e.g. SULTR1;1 and SULTR1;2) expression in roots. Together
CC with AHK2, required for growth and reproduction promotion stimulated by
CC the endophytic fungus Piriformospora indica in a trans-zeatin-dependent
CC manner. Required to trigger the phytotoxic effect of the snapdragon
CC (Antirrhinum majus) flowers volatile organic compound (VOC) methyl
CC benzoate (MB). Plays a role in the cytokinin-mediated repression of the
CC iron uptake pathway. {ECO:0000269|PubMed:11114883,
CC ECO:0000269|PubMed:11230563, ECO:0000269|PubMed:11234017,
CC ECO:0000269|PubMed:11479382, ECO:0000269|PubMed:11577198,
CC ECO:0000269|PubMed:12354925, ECO:0000269|PubMed:12410813,
CC ECO:0000269|PubMed:15053761, ECO:0000269|PubMed:15144379,
CC ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290,
CC ECO:0000269|PubMed:15509853, ECO:0000269|PubMed:15728338,
CC ECO:0000269|PubMed:15923327, ECO:0000269|PubMed:16246292,
CC ECO:0000269|PubMed:16357038, ECO:0000269|PubMed:16361392,
CC ECO:0000269|PubMed:16753566, ECO:0000269|PubMed:17075078,
CC ECO:0000269|PubMed:17216481, ECO:0000269|PubMed:17956858,
CC ECO:0000269|PubMed:17965178, ECO:0000269|PubMed:18077346,
CC ECO:0000269|PubMed:18397377, ECO:0000269|PubMed:18571199,
CC ECO:0000269|PubMed:18785832, ECO:0000269|PubMed:19032596,
CC ECO:0000269|PubMed:20110319}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- ACTIVITY REGULATION: Activated by cytokinins to initiate phosphorelay
CC signaling. This cytokinin-mediated activation is repressed by the
CC trans-zeatin antagonists 6-(2-hydroxy-3-methylbenzylamino)purine (PI-
CC 55) and 6-(2,5-dihydroxybenzylamino)purine (LGR-991).
CC {ECO:0000269|PubMed:11234017, ECO:0000269|PubMed:19032596,
CC ECO:0000269|PubMed:20189204}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH to bind cytokinin is about 7-8.5 at 0 degrees Celsius.
CC {ECO:0000269|PubMed:16246292, ECO:0000269|PubMed:17075078};
CC Temperature dependence:
CC Cytokinin-binding is more stable at 0 degrees Celsius than at 20 and
CC 37 degrees Celsius. {ECO:0000269|PubMed:16246292,
CC ECO:0000269|PubMed:17075078};
CC -!- SUBUNIT: Homodimer. Interacts with AHP1, AHP2, AHP3, AHP5, AHK3, AMPD,
CC FBR12, WNK5 and At4g15630. {ECO:0000269|PubMed:11230563,
CC ECO:0000269|PubMed:16965536, ECO:0000269|PubMed:18642946,
CC ECO:0000269|PubMed:21964459, ECO:0000269|PubMed:24163315}.
CC -!- INTERACTION:
CC Q9C5U0; Q9C5U1: AHK3; NbExp=2; IntAct=EBI-1100775, EBI-1100653;
CC Q9C5U0; O80452: AMPD; NbExp=2; IntAct=EBI-1100775, EBI-1807679;
CC Q9C5U0; Q67XQ1: At1g03430; NbExp=3; IntAct=EBI-1100775, EBI-1100725;
CC Q9C5U0; Q8L8Z1: At4g15630; NbExp=2; IntAct=EBI-1100775, EBI-1807704;
CC Q9C5U0; Q9SCU5: WNK5; NbExp=2; IntAct=EBI-1100775, EBI-1807651;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21709172}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21709172}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CRE1b;
CC IsoId=Q9C5U0-1; Sequence=Displayed;
CC Name=2; Synonyms=CRE1a;
CC IsoId=Q9C5U0-2; Sequence=VSP_039770;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, specifically in the
CC vascular cylinder and pericycle, and, to a lower extent, in leaves and
CC flowers. Present in seedlings. {ECO:0000269|PubMed:11114883,
CC ECO:0000269|PubMed:11230578, ECO:0000269|PubMed:15155880,
CC ECO:0000269|PubMed:15166290}.
CC -!- DEVELOPMENTAL STAGE: Expressed specifically in the vasculature since
CC the early stages of embryogenesis. At the globular stage of
CC embryogenesis, detected in the four innermost cells, which are the
CC precursors of the vascular tissue. During the heart, torpedo, and
CC nearly mature stages, expressed in the procambium of the cotyledon
CC shoulders, prospective hypocotyl, and embryonic root. In seedlings,
CC mainly localized in meristematic tissues (e.g. shoot apical meristem
CC SAM, root tips, and growing leaf and lateral root primordia),
CC especially in vasculature. Present in all the vasculature and the shoot
CC apical meristem (SAM) of the adult plant. In flowers, localized in
CC carpels and developing ovules. In the root tips, expressed in the
CC central cylinder. {ECO:0000269|PubMed:11114883,
CC ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:16753566}.
CC -!- INDUCTION: Rapidly induced by dehydration. Down-regulated by Pi
CC starvation and induced by cytokinins. {ECO:0000269|PubMed:12410813,
CC ECO:0000269|PubMed:18077346}.
CC -!- PTM: Autophosphorylated predominantly on His residues. Activation
CC probably requires a transfer of a phosphate group between a His in the
CC transmitter domain and an Asp of the receiver domain.
CC {ECO:0000269|PubMed:16753566}.
CC -!- DISRUPTION PHENOTYPE: Reduced sensitivity to cytokinin (mostly in
CC shoots). Narrow vascular cylinder composed mainly of protoxylem cell
CC files, with no apparent metaxylem or phloem. Hypersensitivity to ABA.
CC Strong drought and salinity tolerance only in the presence of CK.
CC Reduced cytokinin repression of several Pi starvation-responsive genes
CC and increased sucrose sensitivity. More rapid germination, reduced
CC requirement for light, and decreased far-red light sensitivity. Reduced
CC sensitivity to N-isobutyl decanamide. Impaired benzyladenine (6-BA)-
CC mediated repression of the iron uptake pathway. Impaired meristematic
CC development in seedlings. {ECO:0000269|PubMed:11479382,
CC ECO:0000269|PubMed:12410813, ECO:0000269|PubMed:15155880,
CC ECO:0000269|PubMed:15166290, ECO:0000269|PubMed:15923327,
CC ECO:0000269|PubMed:16357038, ECO:0000269|PubMed:16361392,
CC ECO:0000269|PubMed:16753566, ECO:0000269|PubMed:17965178,
CC ECO:0000269|PubMed:18077346, ECO:0000269|PubMed:18397377,
CC ECO:0000269|PubMed:20110319}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ278528; CAC18521.1; -; mRNA.
DR EMBL; AJ278529; CAC18522.1; -; mRNA.
DR EMBL; AJ278530; CAC18523.1; -; mRNA.
DR EMBL; AB049934; BAB33310.1; -; mRNA.
DR EMBL; AB049935; BAB33311.1; -; mRNA.
DR EMBL; AB046871; BAB40776.1; -; mRNA.
DR EMBL; AC007069; AAD21777.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05505.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05506.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05507.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62256.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62257.1; -; Genomic_DNA.
DR EMBL; EF598292; ABQ85264.1; -; Genomic_DNA.
DR EMBL; EF598293; ABQ85265.1; -; Genomic_DNA.
DR EMBL; EF598294; ABQ85266.1; -; Genomic_DNA.
DR EMBL; EF598295; ABQ85267.1; -; Genomic_DNA.
DR EMBL; EF598296; ABQ85268.1; -; Genomic_DNA.
DR EMBL; EF598297; ABQ85269.1; -; Genomic_DNA.
DR EMBL; EF598298; ABQ85270.1; -; Genomic_DNA.
DR EMBL; EF598299; ABQ85271.1; -; Genomic_DNA.
DR EMBL; EF598300; ABQ85272.1; -; Genomic_DNA.
DR EMBL; EF598301; ABQ85273.1; -; Genomic_DNA.
DR EMBL; EF598302; ABQ85274.1; -; Genomic_DNA.
DR EMBL; EF598303; ABQ85275.1; -; Genomic_DNA.
DR EMBL; EF598304; ABQ85276.1; -; Genomic_DNA.
DR EMBL; EF598305; ABQ85277.1; -; Genomic_DNA.
DR EMBL; EF598306; ABQ85278.1; -; Genomic_DNA.
DR EMBL; EF598307; ABQ85279.1; -; Genomic_DNA.
DR EMBL; EF598308; ABQ85280.1; -; Genomic_DNA.
DR EMBL; EF598309; ABQ85281.1; -; Genomic_DNA.
DR EMBL; EF598310; ABQ85282.1; -; Genomic_DNA.
DR EMBL; EF598311; ABQ85283.1; -; Genomic_DNA.
DR EMBL; EF598312; ABQ85284.1; -; Genomic_DNA.
DR EMBL; EF598313; ABQ85285.1; -; Genomic_DNA.
DR EMBL; EF598314; ABQ85286.1; -; Genomic_DNA.
DR EMBL; EF598315; ABQ85287.1; -; Genomic_DNA.
DR PIR; F84429; F84429.
DR RefSeq; NP_001324428.1; NM_001335080.1. [Q9C5U0-2]
DR RefSeq; NP_001324429.1; NM_001335082.1. [Q9C5U0-2]
DR RefSeq; NP_565277.1; NM_126244.3. [Q9C5U0-2]
DR RefSeq; NP_849925.1; NM_179594.2. [Q9C5U0-1]
DR RefSeq; NP_973396.1; NM_201667.1. [Q9C5U0-2]
DR PDB; 3T4J; X-ray; 1.65 A; A/B=149-418.
DR PDB; 3T4K; X-ray; 1.77 A; A/B=149-418.
DR PDB; 3T4L; X-ray; 1.53 A; A/B=149-418.
DR PDB; 3T4O; X-ray; 1.75 A; A/B=149-418.
DR PDB; 3T4Q; X-ray; 2.30 A; A/B=149-418.
DR PDB; 3T4S; X-ray; 1.60 A; A/B=149-418.
DR PDB; 3T4T; X-ray; 1.70 A; A/B=149-418.
DR PDB; 7P8C; X-ray; 2.15 A; A/B=941-1071.
DR PDB; 7P8D; X-ray; 1.70 A; A/B=941-1080.
DR PDBsum; 3T4J; -.
DR PDBsum; 3T4K; -.
DR PDBsum; 3T4L; -.
DR PDBsum; 3T4O; -.
DR PDBsum; 3T4Q; -.
DR PDBsum; 3T4S; -.
DR PDBsum; 3T4T; -.
DR PDBsum; 7P8C; -.
DR PDBsum; 7P8D; -.
DR AlphaFoldDB; Q9C5U0; -.
DR SMR; Q9C5U0; -.
DR BioGRID; 117; 32.
DR IntAct; Q9C5U0; 29.
DR STRING; 3702.AT2G01830.2; -.
DR BindingDB; Q9C5U0; -.
DR ChEMBL; CHEMBL6124; -.
DR iPTMnet; Q9C5U0; -.
DR PaxDb; Q9C5U0; -.
DR PRIDE; Q9C5U0; -.
DR EnsemblPlants; AT2G01830.1; AT2G01830.1; AT2G01830. [Q9C5U0-2]
DR EnsemblPlants; AT2G01830.2; AT2G01830.2; AT2G01830. [Q9C5U0-1]
DR EnsemblPlants; AT2G01830.3; AT2G01830.3; AT2G01830. [Q9C5U0-2]
DR EnsemblPlants; AT2G01830.4; AT2G01830.4; AT2G01830. [Q9C5U0-2]
DR EnsemblPlants; AT2G01830.6; AT2G01830.6; AT2G01830. [Q9C5U0-2]
DR GeneID; 814714; -.
DR Gramene; AT2G01830.1; AT2G01830.1; AT2G01830. [Q9C5U0-2]
DR Gramene; AT2G01830.2; AT2G01830.2; AT2G01830. [Q9C5U0-1]
DR Gramene; AT2G01830.3; AT2G01830.3; AT2G01830. [Q9C5U0-2]
DR Gramene; AT2G01830.4; AT2G01830.4; AT2G01830. [Q9C5U0-2]
DR Gramene; AT2G01830.6; AT2G01830.6; AT2G01830. [Q9C5U0-2]
DR KEGG; ath:AT2G01830; -.
DR Araport; AT2G01830; -.
DR TAIR; locus:2059718; AT2G01830.
DR eggNOG; KOG0519; Eukaryota.
DR InParanoid; Q9C5U0; -.
DR OrthoDB; 51398at2759; -.
DR PhylomeDB; Q9C5U0; -.
DR EvolutionaryTrace; Q9C5U0; -.
DR PRO; PR:Q9C5U0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9C5U0; baseline and differential.
DR Genevisible; Q9C5U0; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0009884; F:cytokinin receptor activity; IDA:TAIR.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:TAIR.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:TAIR.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0009885; F:transmembrane histidine kinase cytokinin receptor activity; IDA:UniProtKB.
DR GO; GO:0033500; P:carbohydrate homeostasis; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:UniProtKB.
DR GO; GO:0071329; P:cellular response to sucrose stimulus; IMP:UniProtKB.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; TAS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IDA:TAIR.
DR GO; GO:0010086; P:embryonic root morphogenesis; IMP:TAIR.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:TAIR.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IGI:TAIR.
DR GO; GO:0048509; P:regulation of meristem development; IMP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR GO; GO:0048831; P:regulation of shoot system development; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0008272; P:sulfate transport; IMP:UniProtKB.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.30.450.350; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytokinin signaling pathway;
KW Developmental protein; Endoplasmic reticulum; Hydrolase; Kinase; Membrane;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1080
FT /note="Histidine kinase 4"
FT /id="PRO_0000398589"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..1080
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 198..411
FT /note="CHASE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00049"
FT DOMAIN 479..760
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 786..920
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 946..1071
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 285
FT /ligand="dihydrozeatin"
FT /ligand_id="ChEBI:CHEBI:17874"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4O"
FT BINDING 285
FT /ligand="kinetin"
FT /ligand_id="ChEBI:CHEBI:27407"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4S"
FT BINDING 285
FT /ligand="N(6)-dimethylallyladenine"
FT /ligand_id="ChEBI:CHEBI:17660"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4J"
FT BINDING 285
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4L, ECO:0007744|PDB:3T4Q"
FT BINDING 307
FT /ligand="dihydrozeatin"
FT /ligand_id="ChEBI:CHEBI:17874"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4O"
FT BINDING 307
FT /ligand="kinetin"
FT /ligand_id="ChEBI:CHEBI:27407"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4S"
FT BINDING 307
FT /ligand="N(6)-dimethylallyladenine"
FT /ligand_id="ChEBI:CHEBI:17660"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4J"
FT BINDING 307
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4L, ECO:0007744|PDB:3T4Q"
FT BINDING 317
FT /ligand="dihydrozeatin"
FT /ligand_id="ChEBI:CHEBI:17874"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4O"
FT BINDING 317
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /evidence="ECO:0000269|PubMed:21964459,
FT ECO:0007744|PDB:3T4L, ECO:0007744|PDB:3T4Q"
FT MOD_RES 482
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:16753566"
FT MOD_RES 996
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11114883,
FT ECO:0000303|PubMed:11230578, ECO:0000303|PubMed:11234017"
FT /id="VSP_039770"
FT VARIANT 765
FT /note="S -> N (in strain: cv. Se-0)"
FT /evidence="ECO:0000269|PubMed:17435248"
FT MUTAGEN 225
FT /note="A->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 227
FT /note="A->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 273
FT /note="Y->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 279
FT /note="M->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 285
FT /note="D->A,E,R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 301
FT /note="T->I: In wol-1; locked in the phosphoprotein
FT phosphatase active form, retardation of the primary root
FT growth with reduced cell number and exclusive xylem
FT differentiation within the vascular tissue associated with
FT abnormal vascular asymmetric cell divisions, impaired
FT metaxylem and phloem differentiation, and reduced
FT cytokinin-binding ability leading to impaired kinase
FT activity and cyokinin-mediated activation."
FT /evidence="ECO:0000269|PubMed:11114883,
FT ECO:0000269|PubMed:11577198, ECO:0000269|PubMed:15053761,
FT ECO:0000269|PubMed:16753566, ECO:0000269|PubMed:17956858,
FT ECO:0000269|PubMed:21964459"
FT MUTAGEN 303
FT /note="P->V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 304
FT /note="F->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 306
FT /note="L->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 307
FT /note="L->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 317
FT /note="T->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 343
FT /note="G->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21964459"
FT MUTAGEN 435
FT /note="G->C: Constitutively activated independently of
FT cytokinin."
FT /evidence="ECO:0000269|PubMed:17956858"
FT MUTAGEN 436
FT /note="F->S: Constitutively activated independently of
FT cytokinin."
FT /evidence="ECO:0000269|PubMed:17956858"
FT MUTAGEN 447
FT /note="M->T: Constitutively activated independently of
FT cytokinin."
FT /evidence="ECO:0000269|PubMed:17956858"
FT MUTAGEN 459
FT /note="M->I: In wol-3; retardation of the primary root
FT growth, no production of lateral roots and enhanced
FT formation of adventitious roots associated with impaired
FT auxin basipetal transport."
FT /evidence="ECO:0000269|PubMed:16357038"
FT MUTAGEN 471
FT /note="V->A: Constitutively activated independently of
FT cytokinin."
FT /evidence="ECO:0000269|PubMed:17956858"
FT MUTAGEN 482
FT /note="H->Q: Reduced phosphoprotein phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11234017,
FT ECO:0000269|PubMed:16753566"
FT MUTAGEN 490
FT /note="G->D: In cre1-1; impaired histidine-kinase receptor
FT activity and reduced responses to cytokinins, including
FT rapid cell proliferation and shoot formation in tissue
FT culture, repression of sulfate uptake, retardation of the
FT primary root growth, no production of lateral roots and
FT enhanced formation of adventitious roots associated with
FT impaired auxin basipetal transport, as well as reduced cell
FT number within the vascular tissues in roots."
FT /evidence="ECO:0000269|PubMed:11234017,
FT ECO:0000269|PubMed:12354925, ECO:0000269|PubMed:15144379,
FT ECO:0000269|PubMed:16357038"
FT MUTAGEN 493
FT /note="G->R: In cre1-6; reduced sensitivity to cytokinin."
FT /evidence="ECO:0000269|PubMed:12410813"
FT MUTAGEN 494
FT /note="M->L: Constitutively activated independently of
FT cytokinin."
FT /evidence="ECO:0000269|PubMed:17956858"
FT MUTAGEN 529
FT /note="L->F: In wol-2/raw1; impaired metaxylem and phloem
FT differentiation, and reduced sensitivity to cytokinins."
FT /evidence="ECO:0000269|PubMed:15053761"
FT MUTAGEN 529
FT /note="L->F: In wol-2; retardation of the primary root
FT growth with reduced cell number and exclusive xylem
FT differentiation within the vascular tissue associated with
FT abnormal vascular asymmetric cell divisions, and impaired
FT cytokinin-binding ability."
FT /evidence="ECO:0000269|PubMed:15053761"
FT MUTAGEN 708
FT /note="F->L: No histidine kinase activity, but normal
FT phosphoprotein phosphatase activity."
FT /evidence="ECO:0000269|PubMed:16753566"
FT MUTAGEN 996
FT /note="D->N: Cytokinin-mediated autophosphorylation but
FT impaired phosphotransfer to an HPt, abolished
FT phosphoprotein phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11234017,
FT ECO:0000269|PubMed:16753566"
FT MUTAGEN 1008
FT /note="T->I: In cre1-4; slightly reduced sensitivity to
FT cytokinin, and impaired cytokinin repression of several Pi
FT starvation-responses."
FT /evidence="ECO:0000269|PubMed:12410813"
FT MUTAGEN 1032
FT /note="A->T: In cre1-9; impaired cytokinin repression of
FT several Pi starvation-responses."
FT /evidence="ECO:0000269|PubMed:12410813"
FT CONFLICT 567
FT /note="S -> G (in Ref. 2; BAB33311)"
FT /evidence="ECO:0000305"
FT CONFLICT 1018
FT /note="T -> A (in Ref. 2; BAB33311)"
FT /evidence="ECO:0000305"
FT HELIX 151..193
FT /evidence="ECO:0007829|PDB:3T4L"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:3T4L"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:3T4L"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:3T4L"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:3T4T"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:3T4L"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:3T4L"
FT TURN 941..944
FT /evidence="ECO:0007829|PDB:7P8D"
FT STRAND 946..950
FT /evidence="ECO:0007829|PDB:7P8D"
FT HELIX 954..966
FT /evidence="ECO:0007829|PDB:7P8D"
FT STRAND 970..976
FT /evidence="ECO:0007829|PDB:7P8D"
FT HELIX 977..983
FT /evidence="ECO:0007829|PDB:7P8D"
FT STRAND 991..997
FT /evidence="ECO:0007829|PDB:7P8D"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:7P8D"
FT HELIX 1004..1022
FT /evidence="ECO:0007829|PDB:7P8D"
FT STRAND 1030..1033
FT /evidence="ECO:0007829|PDB:7P8D"
FT HELIX 1035..1048
FT /evidence="ECO:0007829|PDB:7P8D"
FT STRAND 1052..1056
FT /evidence="ECO:0007829|PDB:7P8D"
FT HELIX 1063..1065
FT /evidence="ECO:0007829|PDB:7P8C"
SQ SEQUENCE 1080 AA; 120731 MW; 5950DB968B529401 CRC64;
MRRDFVYNNN AMFNPLTTHY SSDMNWALNN HQEEEEEPRR IEISDSESLE NLKSSDFYQL
GGGGALNSSE KPRKIDFWRS GLMGFAKMQQ QQQLQHSVAV KMNNNNNNDL MGNKKGSTFI
QEHRALLPKA LILWIIIVGF ISSGIYQWMD DANKIRREEV LVSMCDQRAR MLQDQFSVSV
NHVHALAILV STFHYHKNPS AIDQETFAEY TARTAFERPL LSGVAYAEKV VNFEREMFER
QHNWVIKTMD RGEPSPVRDE YAPVIFSQDS VSYLESLDMM SGEEDRENIL RARETGKAVL
TSPFRLLETH HLGVVLTFPV YKSSLPENPT VEERIAATAG YLGGAFDVES LVENLLGQLA
GNQAIVVHVY DITNASDPLV MYGNQDEEAD RSLSHESKLD FGDPFRKHKM ICRYHQKAPI
PLNVLTTVPL FFAIGFLVGY ILYGAAMHIV KVEDDFHEMQ ELKVRAEAAD VAKSQFLATV
SHEIRTPMNG ILGMLAMLLD TELSSTQRDY AQTAQVCGKA LIALINEVLD RAKIEAGKLE
LESVPFDIRS ILDDVLSLFS EESRNKSIEL AVFVSDKVPE IVKGDSGRFR QIIINLVGNS
VKFTEKGHIF VKVHLAEQSK DESEPKNALN GGVSEEMIVV SKQSSYNTLS GYEAADGRNS
WDSFKHLVSE EQSLSEFDIS SNVRLMVSIE DTGIGIPLVA QGRVFMPFMQ ADSSTSRNYG
GTGIGLSISK CLVELMRGQI NFISRPHIGS TFWFTAVLEK CDKCSAINHM KKPNVEHLPS
TFKGMKAIVV DAKPVRAAVT RYHMKRLGIN VDVVTSLKTA VVAAAAFERN GSPLPTKPQL
DMILVEKDSW ISTEDNDSEI RLLNSRTNGN VHHKSPKLAL FATNITNSEF DRAKSAGFAD
TVIMKPLRAS MIGACLQQVL ELRKTRQQHP EGSSPATLKS LLTGKKILVV DDNIVNRRVA
AGALKKFGAE VVCAESGQVA LGLLQIPHTF DACFMDIQMP QMDGFEATRQ IRMMEKETKE
KTNLEWHLPI LAMTADVIHA TYEECLKSGM DGYVSKPFEE ENLYKSVAKS FKPNPISPSS
