AHK2_ARATH
ID AHK2_ARATH Reviewed; 1176 AA.
AC Q9C5U2; Q680Y4; Q8GUG0; Q9FKH3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Histidine kinase 2;
DE EC=2.7.13.3;
DE AltName: Full=Arabidopsis histidine kinase 2;
DE Short=AtHK2;
DE AltName: Full=Protein AUTHENTIC HIS-KINASE 2;
GN Name=AHK2; OrderedLocusNames=At5g35750; ORFNames=MXH1.16;
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], 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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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] OF 519-1176.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1095-1176.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [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, 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 [11]
RP HOMODIMERIZATION, AND INTERACTION WITH AHK3; AHP1; AHP2; AHP3 AND AHP5.
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 [12]
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 [13]
RP FUNCTION, AND MUTAGENESIS OF THR-418 AND ILE-586.
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 [14]
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 [15]
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 [16]
RP INTERACTION WITH AT2S3; ATAF2; BETAA-AD; CYP20-2; DRP1A; HIR1; HIR2;
RP PI4KB1; PI4KG5; AT4G12060; AHP3 AND AHP2.
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 AHK3, 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. Involved in
CC alkamides (e.g. N-isobutyl decanamide) and N-acylethanolamides (NAE)
CC signaling that control meristematic activity and differentiation
CC processes during plant development. Contributes to vascular bundle
CC formation and secondary growth in a cytokinin-dependent manner,
CC probably by promoting the maintenance of mitotic activity and/or
CC identity of procambial cells. Together with AHK4, required for growth
CC and reproduction promotion stimulated by the endophytic fungus
CC Piriformospora indica in a trans-zeatin-dependent manner. Required by
CC the cytokinin-dependent flower development regulation pathway.
CC {ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290,
CC ECO:0000269|PubMed:16361392, ECO:0000269|PubMed:16753566,
CC ECO:0000269|PubMed:17956858, ECO:0000269|PubMed:17965178,
CC ECO:0000269|PubMed:18077346, ECO:0000269|PubMed:18785832,
CC ECO:0000269|PubMed:19622803, ECO:0000269|PubMed:19913077,
CC ECO:0000269|PubMed:20110319, 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. {ECO:0000250}.
CC -!- SUBUNIT: Self-interacts. Interacts with AHK3, AHP1, AHP2, AHP3, AHP5,
CC ATAF2, AT2S3, BETAA-AD, CYP20-2, DRP1A, HIR1, HIR2, PI4KB1, PI4KG5 and
CC At4g12060. {ECO:0000269|PubMed:16965536, ECO:0000269|PubMed:18642946}.
CC -!- INTERACTION:
CC Q9C5U2; Q9C5U2: AHK2; NbExp=2; IntAct=EBI-1100634, EBI-1100634;
CC Q9C5U2; Q9C5U1: AHK3; NbExp=2; IntAct=EBI-1100634, EBI-1100653;
CC Q9C5U2; Q9ZNV9: AHP1; NbExp=2; IntAct=EBI-1100634, EBI-1100673;
CC Q9C5U2; Q9ZNV8: AHP2; NbExp=3; IntAct=EBI-1100634, EBI-1100687;
CC Q9C5U2; Q9SAZ5: AHP3; NbExp=3; IntAct=EBI-1100634, EBI-1100711;
CC Q9C5U2; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-1100634, EBI-1100737;
CC Q9C5U2; Q67XQ1: At1g03430; NbExp=3; IntAct=EBI-1100634, EBI-1100725;
CC Q9C5U2; P15459: AT2S3; NbExp=2; IntAct=EBI-1100634, EBI-1807552;
CC Q9C5U2; P42697: DRP1A; NbExp=3; IntAct=EBI-1100634, EBI-994234;
CC Q9C5U2; Q9FM19: HIR1; NbExp=2; IntAct=EBI-1100634, EBI-1807466;
CC Q9C5U2; Q9CAR7: HIR2; NbExp=2; IntAct=EBI-1100634, EBI-1807580;
CC Q9C5U2; Q9FMJ0: PI4KB1; NbExp=2; IntAct=EBI-1100634, EBI-1807432;
CC Q9C5U2; Q9ASS6: PNSL5; NbExp=2; IntAct=EBI-1100634, EBI-1807485;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21709172}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21709172}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers, mostly in
CC the vascular tissues. Present in seedlings.
CC {ECO:0000269|PubMed:11230578, ECO:0000269|PubMed:15155880,
CC 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 flowers, localized
CC in carpels and developing ovules. In the root tips, expressed in and
CC near the vascular initial cells. {ECO:0000269|PubMed:15155880,
CC ECO:0000269|PubMed:16753566}.
CC -!- INDUCTION: Rapidly induced by dehydration, slightly induced by high
CC salinity and abscisic acid (ABA). {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. Slightly reduced sensitivity to cytokinin. More
CC rapid germination, reduced requirement for light, and decreased far-red
CC light sensitivity. Reduced sensitivity to N-isobutyl decanamide.
CC Defects in procambium proliferation and absence of secondary growth.
CC Enhanced freezing tolerance. Impaired meristematic development in
CC seedlings. Disturbed cytokinin-mediated flower development abnormality.
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:19622803, ECO:0000269|PubMed:19913077,
CC ECO:0000269|PubMed:20110319, ECO:0000269|PubMed:20463025}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO00890.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB09274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD43496.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046869; BAB40774.1; -; mRNA.
DR EMBL; AB011485; BAB09274.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94014.1; -; Genomic_DNA.
DR EMBL; BT002530; AAO00890.1; ALT_INIT; mRNA.
DR EMBL; BT008407; AAP37766.1; -; mRNA.
DR EMBL; AK175733; BAD43496.1; ALT_INIT; mRNA.
DR RefSeq; NP_568532.1; NM_122966.3.
DR AlphaFoldDB; Q9C5U2; -.
DR SMR; Q9C5U2; -.
DR BioGRID; 18805; 44.
DR IntAct; Q9C5U2; 45.
DR STRING; 3702.AT5G35750.1; -.
DR iPTMnet; Q9C5U2; -.
DR PaxDb; Q9C5U2; -.
DR PRIDE; Q9C5U2; -.
DR ProteomicsDB; 245072; -.
DR EnsemblPlants; AT5G35750.1; AT5G35750.1; AT5G35750.
DR GeneID; 833552; -.
DR Gramene; AT5G35750.1; AT5G35750.1; AT5G35750.
DR KEGG; ath:AT5G35750; -.
DR Araport; AT5G35750; -.
DR TAIR; locus:2177261; AT5G35750.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_16_1_1; -.
DR InParanoid; Q9C5U2; -.
DR OMA; QATFEGC; -.
DR OrthoDB; 51398at2759; -.
DR PhylomeDB; Q9C5U2; -.
DR PRO; PR:Q9C5U2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5U2; baseline and differential.
DR Genevisible; Q9C5U2; 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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0009884; F:cytokinin receptor activity; TAS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
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:0009736; P:cytokinin-activated signaling pathway; TAS: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:0009737; P:response to abscisic acid; 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:0009636; P:response to toxic substance; IMP:UniProtKB.
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 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; 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 Cytokinin signaling pathway; Developmental protein; Endoplasmic reticulum;
KW Kinase; Membrane; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1176
FT /note="Histidine kinase 2"
FT /id="PRO_0000398587"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..1176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 302..526
FT /note="CHASE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00049"
FT DOMAIN 594..867
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 891..1013
FT /note="Response regulatory 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1036..1173
FT /note="Response regulatory 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 597
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 942
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 1086
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 418
FT /note="T->I: Loss of cyokinin-mediated activation."
FT /evidence="ECO:0000269|PubMed:17956858"
FT MUTAGEN 586
FT /note="I->A: Constitutively activated independently of
FT cytokinin."
FT /evidence="ECO:0000269|PubMed:17956858"
FT CONFLICT 1103
FT /note="E -> K (in Ref. 5; BAD43496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1176 AA; 131860 MW; AC0019CC612361BC CRC64;
MSITCELLNL TSKKAKKSSS SDKKWLKKPL FFLILCGSLV IVLVMFLRLG RSQKEETDSC
NGEEKVLYRH QNVTRSEIHD LVSLFSDSDQ VTSFECHKES SPGMWTNYGI TCSLSVRSDK
QETRGLPWNL GLGHSISSTS CMCGNLEPIL QQPENLEEEN HEEGLEQGLS SYLRNAWWCL
ILGVLVCHKI YVSHSKARGE RKEKVHLQEA LAPKKQQQRA QTSSRGAGRW RKNILLLGIL
GGVSFSVWWF WDTNEEIIMK RRETLANMCD ERARVLQDQF NVSLNHVHAL SILVSTFHHG
KIPSAIDQRT FEEYTERTNF ERPLTSGVAY ALKVPHSERE KFEKEHGWAI KKMETEDQTV
VQDCVPENFD PAPIQDEYAP VIFAQETVSH IVSVDMMSGE EDRENILRAR ASGKGVLTSP
FKLLKSNHLG VVLTFAVYDT SLPPDATEEQ RVEATIGYLG ASYDMPSLVE KLLHQLASKQ
TIAVDVYDTT NTSGLIKMYG SEIGDISEQH ISSLDFGDPS RNHEMHCRFK HKLPIPWTAI
TPSILVLVIT FLVGYILYEA INRIATVEED CQKMRELKAR AEAADIAKSQ FLATVSHEIR
TPMNGVLGML KMLMDTDLDA KQMDYAQTAH GSGKDLTSLI NEVLDQAKIE SGRLELENVP
FDMRFILDNV SSLLSGKANE KGIELAVYVS SQVPDVVVGD PSRFRQIITN LVGNSIKFTQ
ERGHIFISVH LADEVKEPLT IEDAVLKQRL ALGCSESGET VSGFPAVNAW GSWKNFKTCY
STESQNSDQI KLLVTVEDTG VGIPVDAQGR IFTPFMQADS STSRTYGGTG IGLSISKRLV
ELMQGEMGFV SEPGIGSTFS FTGVFGKAET NTSITKLERF DLAIQEFTGL RALVIDNRNI
RAEVTRYELR RLGISADIVS SLRMACTCCI SKLENLAMIL IDKDAWNKEE FSVLDELFTR
SKVTFTRVPK IFLLATSATL TERSEMKSTG LIDEVVIKPL RMSVLICCLQ ETLVNGKKRQ
PNRQRRNLGH LLREKQILVV DDNLVNRRVA EGALKKYGAI VTCVESGKAA LAMLKPPHNF
DACFMDLQMP EMDGFEATRR VRELEREINK KIASGEVSAE MFCKFSSWHV PILAMTADVI
QATHEECMKC GMDGYVSKPF EEEVLYTAVA RFFEPC
