AHK3_ARATH
ID AHK3_ARATH Reviewed; 1036 AA.
AC Q9C5U1; Q9FZK3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Histidine kinase 3;
DE EC=2.7.13.3;
DE AltName: Full=Arabidopsis histidine kinase 3;
DE Short=AtHK3;
DE AltName: Full=Protein AUTHENTIC HIS-KINASE 3;
DE AltName: Full=Protein ORESARA 12;
GN Name=AHK3; Synonyms=ORE12; OrderedLocusNames=At1g27320; ORFNames=F17L21.11;
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], FUNCTION, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, AND ACTIVATION BY CYTOKININS.
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, AND MUTAGENESIS OF SER-713.
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 [11]
RP FUNCTION, 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 [12]
RP INTERACTION WITH AHP1; AHP2; AHP3; AHP5; AHK2 AND AHK4.
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 [13]
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 [14]
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 [15]
RP FUNCTION, MUTAGENESIS OF PRO-243 AND ASP-448, AND SUBCELLULAR LOCATION.
RX PubMed=16407152; DOI=10.1073/pnas.0505150103;
RA Kim H.J., Ryu H., Hong S.H., Woo H.R., Lim P.O., Lee I.C., Sheen J.,
RA Nam H.G., Hwang I.;
RT "Cytokinin-mediated control of leaf longevity by AHK3 through
RT phosphorylation of ARR2 in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:814-819(2006).
RN [16]
RP FUNCTION, AND MUTAGENESIS OF THR-281 AND VAL-449.
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 [17]
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 [18]
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 [19]
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 [20]
RP INTERACTION WITH AT5G43560.
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 [21]
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 [22]
RP 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 [23]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19622803; DOI=10.1105/tpc.109.066696;
RA Hejatko J., Ryu H., Kim G.-T., Dobesova R., Choi S., Choi S.M., Soucek P.,
RA Horak J., Pekarova B., Palme K., Brzobohaty B., Hwang I.;
RT "The histidine kinases CYTOKININ-INDEPENDENT1 and ARABIDOPSIS HISTIDINE
RT KINASE2 and 3 regulate vascular tissue development in Arabidopsis shoots.";
RL Plant Cell 21:2008-2021(2009).
RN [24]
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 [25]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19913077; DOI=10.1016/j.gene.2009.11.003;
RA Li X.G., Su Y.H., Zhao X.Y., Li W., Gao X.Q., Zhang X.S.;
RT "Cytokinin overproduction-caused alteration of flower development is
RT partially mediated by CUC2 and CUC3 in Arabidopsis.";
RL Gene 450:109-120(2010).
RN [26]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20463025; DOI=10.1074/jbc.m109.096644;
RA Jeon J., Kim N.Y., Kim S., Kang N.Y., Novak O., Ku S.-J., Cho C., Lee D.J.,
RA Lee E.-J., Strnad M., Kim J.;
RT "A subset of cytokinin two-component signaling system plays a role in cold
RT temperature stress response in Arabidopsis.";
RL J. Biol. Chem. 285:23371-23386(2010).
RN [27]
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 [28]
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).
CC -!- FUNCTION: Cytokinins (CK) receptor related to bacterial two-component
CC regulators. Functions as a histidine kinase and transmits the stress
CC signal to a downstream MAPK cascade. This protein undergoes an ATP-
CC dependent autophosphorylation at a conserved histidine residue in the
CC kinase core, and a phosphoryl group is then transferred to a conserved
CC aspartate residue in the receiver domain. In the presence of cytokinin,
CC feeds phosphate to phosphorelay-integrating histidine phosphotransfer
CC protein (HPt) and activates subsequent cascade. Involved in meristems
CC establishment in seedlings. Redundant negative regulator of drought and
CC salt stress responses and abscisic acid (ABA) signaling. Together with
CC AHK2, plays a negative regulatory role in cold stress signaling via
CC inhibition of ABA response, occurring independently of the cold
CC acclimation pathway. Redundant positive regulator of cytokinin
CC signaling that regulates many developmental processes including seed
CC germination, cell division, seed size, chlorophyll retention during
CC leaf senescence, root repression and shoot promotion. Can interact with
CC isoprenoid-type cytokinins trans-zeatin (tZ and tZR), cis-zeatin (cZ),
CC dihydrozeatin (DZ), buta-2,3-dienyladenine (HA-8), penta-2,3-
CC dienyladenine (HA-1), 4-methyl-penta-2,3-dienyladenine (HA-10), 4-
CC hydroxy-2-butynyladenine (RM1), 2-propynyladenine (RM3), 2-
CC butynyladenine (RM6), and cytokinin ribosides and ribotides. Together
CC with AHK4, involved in the cytokinin-dependent responses to Pi
CC starvation and sucrose stresses. Promotes cytokinin-mediated leaf
CC longevity through a specific phosphorylation of the response regulator
CC ARR2. Involved in alkamides (e.g. N-isobutyl decanamide) and N-
CC acylethanolamides (NAE) signaling that control meristematic activity
CC and differentiation processes during plant development. Contributes to
CC vascular bundle formation and secondary growth in a cytokinin-dependent
CC manner, probably by promoting the maintenance of mitotic activity
CC and/or identity of procambial cells. Plays a role in the cytokinin-
CC mediated repression of the iron uptake pathway. Required by the
CC cytokinin-dependent flower development regulation pathway.
CC {ECO:0000269|PubMed:11230578, ECO:0000269|PubMed:11577198,
CC ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290,
CC ECO:0000269|PubMed:15509853, ECO:0000269|PubMed:15923327,
CC ECO:0000269|PubMed:16361392, ECO:0000269|PubMed:16407152,
CC ECO:0000269|PubMed:16753566, ECO:0000269|PubMed:17075078,
CC ECO:0000269|PubMed:17956858, ECO:0000269|PubMed:17965178,
CC ECO:0000269|PubMed:18077346, ECO:0000269|PubMed:18397377,
CC ECO:0000269|PubMed:18571199, ECO:0000269|PubMed:19622803,
CC ECO:0000269|PubMed:19913077, ECO:0000269|PubMed:20110319,
CC ECO:0000269|PubMed:20463025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
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:19032596, ECO:0000269|PubMed:20189204}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH to bind cytokinin is about 8.5 at 0 degrees Celsius.
CC {ECO:0000269|PubMed:17075078};
CC Temperature dependence:
CC Cytokinin-binding is stable at 0 degrees Celsius but transient at 37
CC degrees Celsius. {ECO:0000269|PubMed:17075078};
CC -!- SUBUNIT: Interacts with AHK2, AHK4, AHP1, AHP2, AHP3, AHP5 and
CC At5g43560. {ECO:0000269|PubMed:16965536, ECO:0000269|PubMed:18642946}.
CC -!- INTERACTION:
CC Q9C5U1; Q9C5U2: AHK2; NbExp=2; IntAct=EBI-1100653, EBI-1100634;
CC Q9C5U1; Q9C5U0: AHK4; NbExp=2; IntAct=EBI-1100653, EBI-1100775;
CC Q9C5U1; Q9ZNV9: AHP1; NbExp=2; IntAct=EBI-1100653, EBI-1100673;
CC Q9C5U1; Q9ZNV8: AHP2; NbExp=2; IntAct=EBI-1100653, EBI-1100687;
CC Q9C5U1; Q9SAZ5: AHP3; NbExp=2; IntAct=EBI-1100653, EBI-1100711;
CC Q9C5U1; Q67XQ1: At1g03430; NbExp=3; IntAct=EBI-1100653, EBI-1100725;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=The
CC plasma membrane localization is supported by the over-expression of an
CC AHK3-GFP fusion protein. {ECO:0000269|PubMed:16407152}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers, and, to a
CC lower extent, in roots, stems, and siliques, especially in the vascular
CC tissues. Present in seedlings. {ECO:0000269|PubMed:11230578,
CC ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, mainly localized in meristematic
CC tissues (e.g. shoot apical meristem SAM, root tips, and growing leaf
CC and lateral root primordia). Present in all the vasculature and the
CC shoot apical meristem (SAM) of the adult plant. In the root tips,
CC strongest expression in the procambium. {ECO:0000269|PubMed:15155880,
CC ECO:0000269|PubMed:16753566}.
CC -!- INDUCTION: Rapidly induced by dehydration, high salinity and cold
CC stresses. {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 (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to ABA, and strong drought and
CC salinity tolerance. Reduced sensitivity to cytokinin (mostly in roots).
CC More rapid germination, reduced requirement for light, and decreased
CC far-red light sensitivity. Early senescence promoted by darkness.
CC Reduced sensitivity to N-isobutyl decanamide. Defects in procambium
CC proliferation and absence of secondary growth. Enhanced freezing
CC tolerance. Impaired benzyladenine (6-BA)-mediated repression of the
CC iron uptake pathway. Disturbed cytokinin-mediated flower development
CC abnormality. Impaired meristematic development in seedlings.
CC {ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290,
CC ECO:0000269|PubMed:16361392, ECO:0000269|PubMed:16753566,
CC ECO:0000269|PubMed:17965178, ECO:0000269|PubMed:18077346,
CC ECO:0000269|PubMed:18397377, ECO:0000269|PubMed:19622803,
CC ECO:0000269|PubMed:19913077, ECO:0000269|PubMed:20110319,
CC ECO:0000269|PubMed:20463025}.
CC -!- MISCELLANEOUS: 'Oresara' means 'long living' in Korean.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99730.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB046870; BAB40775.1; -; mRNA.
DR EMBL; AC004557; AAF99730.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30806.1; -; Genomic_DNA.
DR RefSeq; NP_564276.1; NM_102494.4.
DR AlphaFoldDB; Q9C5U1; -.
DR SMR; Q9C5U1; -.
DR BioGRID; 24856; 7.
DR IntAct; Q9C5U1; 7.
DR STRING; 3702.AT1G27320.1; -.
DR BindingDB; Q9C5U1; -.
DR ChEMBL; CHEMBL6125; -.
DR PaxDb; Q9C5U1; -.
DR PRIDE; Q9C5U1; -.
DR ProteomicsDB; 244661; -.
DR EnsemblPlants; AT1G27320.1; AT1G27320.1; AT1G27320.
DR GeneID; 839621; -.
DR Gramene; AT1G27320.1; AT1G27320.1; AT1G27320.
DR KEGG; ath:AT1G27320; -.
DR Araport; AT1G27320; -.
DR TAIR; locus:2015964; AT1G27320.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_16_2_1; -.
DR InParanoid; Q9C5U1; -.
DR OMA; TQQDYVK; -.
DR OrthoDB; 51398at2759; -.
DR PhylomeDB; Q9C5U1; -.
DR PRO; PR:Q9C5U1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5U1; baseline and differential.
DR Genevisible; Q9C5U1; AT.
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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009884; F:cytokinin receptor activity; TAS:TAIR.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:UniProtKB.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; IMP:UniProtKB.
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:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0034757; P:negative regulation of iron ion transport; IMP:UniProtKB.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:UniProtKB.
DR GO; GO:0010271; P:regulation of chlorophyll catabolic process; IMP:TAIR.
DR GO; GO:0009909; P:regulation of flower development; IMP:UniProtKB.
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:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0080117; P:secondary growth; 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; 2.
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 Cell membrane; Cytokinin signaling pathway; Developmental protein;
KW Endoplasmic reticulum; Kinase; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1036
FT /note="Histidine kinase 3"
FT /id="PRO_0000398588"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..399
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..1036
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 163..389
FT /note="CHASE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00049"
FT DOMAIN 457..723
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 746..865
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 891..1028
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 460
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 941
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 243
FT /note="P->S: In ore12-1; delayed leaf senescence and
FT abolished cytokinin-dependent phosphorylation activity
FT toward ARR2."
FT /evidence="ECO:0000269|PubMed:16407152"
FT MUTAGEN 281
FT /note="T->I: Loss of cyokinin-mediated activation."
FT /evidence="ECO:0000269|PubMed:17956858"
FT MUTAGEN 448
FT /note="D->N: Delayed leaf senescence."
FT /evidence="ECO:0000269|PubMed:16407152"
FT MUTAGEN 449
FT /note="V->A: Constitutively activated independently of
FT cytokinin."
FT /evidence="ECO:0000269|PubMed:17956858"
FT MUTAGEN 713
FT /note="S->F: In ahk3-4; reduced sensitivity to cytokinin
FT (mostly in roots), and impaired cytokinin repression of
FT several Pi starvation-responsive genes and increased
FT sucrose sensitivity."
FT /evidence="ECO:0000269|PubMed:15923327"
SQ SEQUENCE 1036 AA; 116373 MW; 03F23DEE4B44C40B CRC64;
MSLFHVLGFG VKIGHLFWML CCWFVSWFVD NGIEDKSGLL VGSVGDLEKT KMTTLKKKNK
MWFWNKISSS GLKIPSFSYQ FLGSVKFNKA WWRKLVVVWV VFWVLVSIWT FWYFSSQAME
KRKETLASMC DERARMLQDQ FNVSMNHVQA MSILISTFHH GKIPSAIDQR TFSEYTDRTS
FERPLTSGVA YAMRVLHSER EEFERQQGWT IRKMYSLEQN PVHKDDYDLE ALEPSPVQEE
YAPVIFAQDT VSHVVSLDML SGKEDRENVL RARSSGKGVL TAPFPLIKTN RLGVILTFAV
YKRDLPSNAT PKERIEATNG YLGGVFDIES LVENLLQQLA SKQTILVNVY DITNHSQPIS
MYGTNVSADG LERVSPLIFG DPLRKHEMRC RFKQKPPWPV LSMVTSFGIL VIALLVAHII
HATVSRIHKV EEDCDKMKQL KKKAEAADVA KSQFLATVSH EIRTPMNGVL GMLHMLMDTE
LDVTQQDYVR TAQASGKALV SLINEVLDQA KIESGKLELE EVRFDLRGIL DDVLSLFSSK
SQQKGVELAV YISDRVPDML IGDPGRFRQI LTNLMGNSIK FTEKGHIFVT VHLVDELFES
IDGETASSPE STLSGLPVAD RQRSWENFKA FSSNGHRSFE PSPPDINLIV SVEDTGVGIP
VEAQSRIFTP FMQVGPSISR THGGTGIGLS ISKCLVGLMK GEIGFSSTPK VGSTFTFTAV
FSNGMQPAER KNDNNQPIFS EFRGMKAVVV DHRPARAKVS WYHFQRLGIR VEVVPRVEQA
LHYLKIGTTT VNMILIEQEI WNREADDFIK KLQKDPLFLS PKLILLANSV ESSISEALCT
GIDPPIVIVK PLRASMLAAT LQRGLGIGIR EPPQHKGPPA LILRNLLLGR KILIVDDNNV
NLRVAAGALK KYGADVVCAE SGIKAISLLK PPHEFDACFM DIQMPEMDGF EATRRIRDME
EEMNKRIKNG EALIVENGNK TSWHLPVLAM TADVIQATHE ECLKCGMDGY VSKPFEAEQL
YREVSRFFNS PSDTES
