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Histidine kinase 3 (EC 2.7.13.3) (Arabidopsis histidine kinase 3) (AtHK3) (Protein AUTHENTIC HIS-KINASE 3) (Protein ORESARA 12)

 AHK3_ARATH              Reviewed;        1036 AA.
Q9C5U1; Q9FZK3;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 113.
RecName: Full=Histidine kinase 3;
EC=2.7.13.3;
AltName: Full=Arabidopsis histidine kinase 3;
Short=AtHK3;
AltName: Full=Protein AUTHENTIC HIS-KINASE 3;
AltName: Full=Protein ORESARA 12;
Name=AHK3; Synonyms=ORE12; OrderedLocusNames=At1g27320;
ORFNames=F17L21.11;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11230578; DOI=10.1093/pcp/pce015;
Ueguchi C., Koizumi H., Suzuki T., Mizuno T.;
"Novel family of sensor histidine kinase genes in Arabidopsis
thaliana.";
Plant Cell Physiol. 42:231-235(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, AND ACTIVATION BY CYTOKININS.
PubMed=11577198; DOI=10.1093/pcp/pce127;
Yamada H., Suzuki T., Terada K., Takei K., Ishikawa K., Miwa K.,
Yamashino T., Mizuno T.;
"The Arabidopsis AHK4 histidine kinase is a cytokinin-binding receptor
that transduces cytokinin signals across the membrane.";
Plant Cell Physiol. 42:1017-1023(2001).
[5]
REVIEW.
PubMed=12589073; DOI=10.1266/ggs.77.383;
Oka A., Sakai H., Iwakoshi S.;
"His-Asp phosphorelay signal transduction in higher plants: receptors
and response regulators for cytokinin signaling in Arabidopsis
thaliana.";
Genes Genet. Syst. 77:383-391(2002).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12068096; DOI=10.1104/pp.005504;
Hwang I., Chen H.-C., Sheen J.;
"Two-component signal transduction pathways in Arabidopsis.";
Plant Physiol. 129:500-515(2002).
[7]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=15155880; DOI=10.1105/tpc.021477;
Nishimura C., Ohashi Y., Sato S., Kato T., Tabata S., Ueguchi C.;
"Histidine kinase homologs that act as cytokinin receptors possess
overlapping functions in the regulation of shoot and root growth in
Arabidopsis.";
Plant Cell 16:1365-1377(2004).
[8]
FUNCTION.
PubMed=15509853; DOI=10.1093/pcp/pch132;
Spichal L., Rakova N.Y., Riefler M., Mizuno T., Romanov G.A.,
Strnad M., Schmuelling T.;
"Two cytokinin receptors of Arabidopsis thaliana, CRE1/AHK4 and AHK3,
differ in their ligand specificity in a bacterial assay.";
Plant Cell Physiol. 45:1299-1305(2004).
[9]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15166290; DOI=10.1073/pnas.0402887101;
Higuchi M., Pischke M.S., Maehoenen A.P., Miyawaki K., Hashimoto Y.,
Seki M., Kobayashi M., Shinozaki K., Kato T., Tabata S.,
Helariutta Y., Sussman M.R., Kakimoto T.;
"In planta functions of the Arabidopsis cytokinin receptor family.";
Proc. Natl. Acad. Sci. U.S.A. 101:8821-8826(2004).
[10]
FUNCTION, AND MUTAGENESIS OF SER-713.
PubMed=15923327; DOI=10.1104/pp.105.060517;
Franco-Zorrilla J.M., Martin A.C., Leyva A., Paz-Ares J.;
"Interaction between phosphate-starvation, sugar, and cytokinin
signaling in Arabidopsis and the roles of cytokinin receptors
CRE1/AHK4 and AHK3.";
Plant Physiol. 138:847-857(2005).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=16753566; DOI=10.1016/j.cub.2006.04.030;
Maehoenen A.P., Higuchi M., Toermaekangas K., Miyawaki K.,
Pischke M.S., Sussman M.R., Helariutta Y., Kakimoto T.;
"Cytokinins regulate a bidirectional phosphorelay network in
Arabidopsis.";
Curr. Biol. 16:1116-1122(2006).
[12]
INTERACTION WITH AHP1; AHP2; AHP3; AHP5; AHK2 AND AHK4.
PubMed=16965536; DOI=10.1111/j.1742-4658.2006.05467.x;
Dortay H., Mehnert N., Buerkle L., Schmuelling T., Heyl A.;
"Analysis of protein interactions within the cytokinin-signaling
pathway of Arabidopsis thaliana.";
FEBS J. 273:4631-4644(2006).
[13]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17075078; DOI=10.1093/jxb/erl179;
Romanov G.A., Lomin S.N., Schmuelling T.;
"Biochemical characteristics and ligand-binding properties of
Arabidopsis cytokinin receptor AHK3 compared to CRE1/AHK4 as revealed
by a direct binding assay.";
J. Exp. Bot. 57:4051-4058(2006).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16361392; DOI=10.1105/tpc.105.037796;
Riefler M., Novak O., Strnad M., Schmuelling T.;
"Arabidopsis cytokinin receptor mutants reveal functions in shoot
growth, leaf senescence, seed size, germination, root development, and
cytokinin metabolism.";
Plant Cell 18:40-54(2006).
[15]
FUNCTION, MUTAGENESIS OF PRO-243 AND ASP-448, AND SUBCELLULAR
LOCATION.
PubMed=16407152; DOI=10.1073/pnas.0505150103;
Kim H.J., Ryu H., Hong S.H., Woo H.R., Lim P.O., Lee I.C., Sheen J.,
Nam H.G., Hwang I.;
"Cytokinin-mediated control of leaf longevity by AHK3 through
phosphorylation of ARR2 in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 103:814-819(2006).
[16]
FUNCTION, AND MUTAGENESIS OF THR-281 AND VAL-449.
PubMed=17956858; DOI=10.1093/pcp/pcm145;
Miwa K., Ishikawa K., Terada K., Yamada H., Suzuki T., Yamashino T.,
Mizuno T.;
"Identification of amino acid substitutions that render the
Arabidopsis cytokinin receptor histidine kinase AHK4 constitutively
active.";
Plant Cell Physiol. 48:1809-1814(2007).
[17]
FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=18077346; DOI=10.1073/pnas.0706547105;
Tran L.S., Urao T., Qin F., Maruyama K., Kakimoto T., Shinozaki K.,
Yamaguchi-Shinozaki K.;
"Functional analysis of AHK1/ATHK1 and cytokinin receptor histidine
kinases in response to abscisic acid, drought, and salt stress in
Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 104:20623-20628(2007).
[18]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17965178; DOI=10.1104/pp.107.107953;
Lopez-Bucio J., Millan-Godinez M., Mendez-Bravo A.,
Morquecho-Contreras A., Ramirez-Chavez E., Molina-Torres J.,
Perez-Torres A., Higuchi M., Kakimoto T., Herrera-Estrella L.;
"Cytokinin receptors are involved in alkamide regulation of root and
shoot development in Arabidopsis.";
Plant Physiol. 145:1703-1713(2007).
[19]
FUNCTION.
PubMed=18571199; DOI=10.1016/j.jmb.2008.05.044;
Kopecny D., Sebela M., Briozzo P., Spichal L., Houba-Herin N.,
Masek V., Joly N., Madzak C., Anzenbacher P., Laloue M.;
"Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack
FAD cofactor.";
J. Mol. Biol. 380:886-899(2008).
[20]
INTERACTION WITH AT5G43560.
PubMed=18642946; DOI=10.1021/pr0703831;
Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T.,
Heyl A.;
"Toward an interaction map of the two-component signaling pathway of
Arabidopsis thaliana.";
J. Proteome Res. 7:3649-3660(2008).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18397377; DOI=10.1111/j.1365-313X.2008.03502.x;
Seguela M., Briat J.-F., Vert G., Curie C.;
"Cytokinins negatively regulate the root iron uptake machinery in
Arabidopsis through a growth-dependent pathway.";
Plant J. 55:289-300(2008).
[22]
ENZYME REGULATION.
PubMed=19032596; DOI=10.1111/j.1742-4658.2008.06777.x;
Spichal L., Werner T., Popa I., Riefler M., Schmuelling T., Strnad M.;
"The purine derivative PI-55 blocks cytokinin action via receptor
inhibition.";
FEBS J. 276:244-253(2009).
[23]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19622803; DOI=10.1105/tpc.109.066696;
Hejatko J., Ryu H., Kim G.-T., Dobesova R., Choi S., Choi S.M.,
Soucek P., Horak J., Pekarova B., Palme K., Brzobohaty B., Hwang I.;
"The histidine kinases CYTOKININ-INDEPENDENT1 and ARABIDOPSIS
HISTIDINE KINASE2 and 3 regulate vascular tissue development in
Arabidopsis shoots.";
Plant Cell 21:2008-2021(2009).
[24]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20110319; DOI=10.1242/dev.041426;
Skylar A., Hong F., Chory J., Weigel D., Wu X.;
"STIMPY mediates cytokinin signaling during shoot meristem
establishment in Arabidopsis seedlings.";
Development 137:541-549(2010).
[25]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19913077; DOI=10.1016/j.gene.2009.11.003;
Li X.G., Su Y.H., Zhao X.Y., Li W., Gao X.Q., Zhang X.S.;
"Cytokinin overproduction-caused alteration of flower development is
partially mediated by CUC2 and CUC3 in Arabidopsis.";
Gene 450:109-120(2010).
[26]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20463025; DOI=10.1074/jbc.M109.096644;
Jeon J., Kim N.Y., Kim S., Kang N.Y., Novak O., Ku S.-J., Cho C.,
Lee D.J., Lee E.-J., Strnad M., Kim J.;
"A subset of cytokinin two-component signaling system plays a role in
cold temperature stress response in Arabidopsis.";
J. Biol. Chem. 285:23371-23386(2010).
[27]
ENZYME REGULATION.
PubMed=20189204; DOI=10.1016/j.phytochem.2010.01.018;
Nisler J., Zatloukal M., Popa I., Dolezal K., Strnad M., Spichal L.;
"Cytokinin receptor antagonists derived from 6-benzylaminopurine.";
Phytochemistry 71:823-830(2010).
[28]
SUBCELLULAR LOCATION.
STRAIN=cv. Columbia;
PubMed=21709172; DOI=10.1104/pp.111.180539;
Wulfetange K., Lomin S.N., Romanov G.A., Stolz A., Heyl A.,
Schmuelling T.;
"The cytokinin receptors of Arabidopsis are located mainly to the
endoplasmic reticulum.";
Plant Physiol. 156:1808-1818(2011).
-!- FUNCTION: Cytokinins (CK) receptor related to bacterial two-
component regulators. Functions as a histidine kinase and
transmits the stress signal to a downstream MAPK cascade. This
protein undergoes an ATP-dependent autophosphorylation at a
conserved histidine residue in the kinase core, and a phosphoryl
group is then transferred to a conserved aspartate residue in the
receiver domain. In the presence of cytokinin, feeds phosphate to
phosphorelay-integrating histidine phosphotransfer protein (HPt)
and activates subsequent cascade. Involved in meristems
establishment in seedlings. Redundant negative regulator of
drought and salt stress responses and abscisic acid (ABA)
signaling. Together with AHK2, plays a negative regulatory role in
cold stress signaling via inhibition of ABA response, occurring
independently of the cold acclimation pathway. Redundant positive
regulator of cytokinin signaling that regulates many developmental
processes including seed germination, cell division, seed size,
chlorophyll retention during leaf senescence, root repression and
shoot promotion. Can interact with isoprenoid-type cytokinins
trans-zeatin (tZ and tZR), cis-zeatin (cZ), dihydrozeatin (DZ),
buta-2,3-dienyladenine (HA-8), penta-2,3-dienyladenine (HA-1), 4-
methyl-penta-2,3-dienyladenine (HA-10), 4-hydroxy-2-butynyladenine
(RM1), 2-propynyladenine (RM3), 2-butynyladenine (RM6), and
cytokinin ribosides and ribotides. Together with AHK4, involved in
the cytokinin-dependent responses to Pi starvation and sucrose
stresses. Promotes cytokinin-mediated leaf longevity through a
specific phosphorylation of the response regulator ARR2. Involved
in alkamides (e.g. N-isobutyl decanamide) and N-acylethanolamides
(NAE) signaling that control meristematic activity and
differentiation processes during plant development. Contributes to
vascular bundle formation and secondary growth in a cytokinin-
dependent manner, probably by promoting the maintenance of mitotic
activity and/or identity of procambial cells. Plays a role in the
cytokinin-mediated repression of the iron uptake pathway. Required
by the cytokinin-dependent flower development regulation pathway.
{ECO:0000269|PubMed:11230578, ECO:0000269|PubMed:11577198,
ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290,
ECO:0000269|PubMed:15509853, ECO:0000269|PubMed:15923327,
ECO:0000269|PubMed:16361392, ECO:0000269|PubMed:16407152,
ECO:0000269|PubMed:16753566, ECO:0000269|PubMed:17075078,
ECO:0000269|PubMed:17956858, ECO:0000269|PubMed:17965178,
ECO:0000269|PubMed:18077346, ECO:0000269|PubMed:18397377,
ECO:0000269|PubMed:18571199, ECO:0000269|PubMed:19622803,
ECO:0000269|PubMed:19913077, ECO:0000269|PubMed:20110319,
ECO:0000269|PubMed:20463025}.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine.
-!- ENZYME REGULATION: Activated by cytokinins to initiate
phosphorelay signaling. This cytokinin-mediated activation is
repressed by the trans-zeatin antagonists 6-(2-hydroxy-3-
methylbenzylamino)purine (PI-55) and 6-(2,5-
Dihydroxybenzylamino)purine (LGR-991).
{ECO:0000269|PubMed:19032596, ECO:0000269|PubMed:20189204}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH to bind cytokinin is about 8.5 at 0 degrees Celsius.
{ECO:0000269|PubMed:17075078};
Temperature dependence:
Cytokinin-binding is stable at 0 degrees Celsius but transient
at 37 degrees Celsius. {ECO:0000269|PubMed:17075078};
-!- SUBUNIT: Interacts with AHK2, AHK4, AHP1, AHP2, AHP3, AHP5 and
At5g43560. {ECO:0000269|PubMed:16965536,
ECO:0000269|PubMed:18642946}.
-!- INTERACTION:
Q9C5U2:AHK2; NbExp=2; IntAct=EBI-1100653, EBI-1100634;
Q9C5U0:AHK4; NbExp=2; IntAct=EBI-1100653, EBI-1100775;
Q9ZNV9:AHP1; NbExp=2; IntAct=EBI-1100653, EBI-1100673;
Q9ZNV8:AHP2; NbExp=2; IntAct=EBI-1100653, EBI-1100687;
Q9SAZ5:AHP3; NbExp=2; IntAct=EBI-1100653, EBI-1100711;
Q67XQ1:At1g03430; NbExp=3; IntAct=EBI-1100653, EBI-1100725;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Note=The plasma membrane localization is supported by the over-
expression of an AHK3-GFP fusion protein.
{ECO:0000269|PubMed:16407152}.
-!- TISSUE SPECIFICITY: Mostly expressed in leaves and flowers, and,
to a lower extent, in roots, stems, and siliques, especially in
the vascular tissues. Present in seedlings.
{ECO:0000269|PubMed:11230578, ECO:0000269|PubMed:15155880,
ECO:0000269|PubMed:15166290}.
-!- DEVELOPMENTAL STAGE: In seedlings, mainly localized in
meristematic tissues (e.g. shoot apical meristem SAM, root tips,
and growing leaf and lateral root primordia). Present in all the
vasculature and the shoot apical meristem (SAM) of the adult
plant. In the root tips, strongest expression in the procambium.
{ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:16753566}.
-!- INDUCTION: Rapidly induced by dehydration, high salinity and cold
stresses. {ECO:0000269|PubMed:18077346}.
-!- PTM: Autophosphorylated predominantly on His residues. Activation
probably requires a transfer of a phosphate group between a His in
the transmitter domain and an Asp of the receiver domain (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Hypersensitivity to ABA, and strong drought
and salinity tolerance. Reduced sensitivity to cytokinin (mostly
in roots). More rapid germination, reduced requirement for light,
and decreased far-red light sensitivity. Early senescence promoted
by darkness. Reduced sensitivity to N-isobutyl decanamide. Defects
in procambium proliferation and absence of secondary growth.
Enhanced freezing tolerance. Impaired benzyladenine (6-BA)-
mediated repression of the iron uptake pathway. Disturbed
cytokinin-mediated flower development abnormality. Impaired
meristematic development in seedlings.
{ECO:0000269|PubMed:15155880, ECO:0000269|PubMed:15166290,
ECO:0000269|PubMed:16361392, ECO:0000269|PubMed:16753566,
ECO:0000269|PubMed:17965178, ECO:0000269|PubMed:18077346,
ECO:0000269|PubMed:18397377, ECO:0000269|PubMed:19622803,
ECO:0000269|PubMed:19913077, ECO:0000269|PubMed:20110319,
ECO:0000269|PubMed:20463025}.
-!- MISCELLANEOUS: 'Oresara' means 'long living' in Korean.
-!- SEQUENCE CAUTION:
Sequence=AAF99730.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB046870; BAB40775.1; -; mRNA.
EMBL; AC004557; AAF99730.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE30806.1; -; Genomic_DNA.
RefSeq; NP_564276.1; NM_102494.4.
UniGene; At.24547; -.
ProteinModelPortal; Q9C5U1; -.
SMR; Q9C5U1; -.
BioGrid; 24856; 7.
IntAct; Q9C5U1; 7.
STRING; 3702.AT1G27320.1; -.
BindingDB; Q9C5U1; -.
ChEMBL; CHEMBL6125; -.
PaxDb; Q9C5U1; -.
PRIDE; Q9C5U1; -.
EnsemblPlants; AT1G27320.1; AT1G27320.1; AT1G27320.
GeneID; 839621; -.
Gramene; AT1G27320.1; AT1G27320.1; AT1G27320.
KEGG; ath:AT1G27320; -.
Araport; AT1G27320; -.
TAIR; locus:2015964; AT1G27320.
eggNOG; KOG0519; Eukaryota.
eggNOG; COG0642; LUCA.
HOGENOM; HOG000116474; -.
InParanoid; Q9C5U1; -.
KO; K14489; -.
OMA; ADRQRSW; -.
OrthoDB; EOG093601CR; -.
PhylomeDB; Q9C5U1; -.
PRO; PR:Q9C5U1; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9C5U1; baseline and differential.
Genevisible; Q9C5U1; AT.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009884; F:cytokinin receptor activity; TAS:TAIR.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0004673; F:protein histidine kinase activity; IDA:UniProtKB.
GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
GO; GO:0070417; P:cellular response to cold; IMP:UniProtKB.
GO; GO:0016036; P:cellular response to phosphate starvation; IMP:UniProtKB.
GO; GO:0071329; P:cellular response to sucrose stimulus; IMP:UniProtKB.
GO; GO:0009736; P:cytokinin-activated signaling pathway; TAS:TAIR.
GO; GO:0042742; P:defense response to bacterium; IDA:TAIR.
GO; GO:0010150; P:leaf senescence; IMP:TAIR.
GO; GO:0034757; P:negative regulation of iron ion transport; IMP:UniProtKB.
GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
GO; GO:0010087; P:phloem or xylem histogenesis; IMP:UniProtKB.
GO; GO:0010271; P:regulation of chlorophyll catabolic process; IMP:TAIR.
GO; GO:0009909; P:regulation of flower development; IMP:UniProtKB.
GO; GO:0048509; P:regulation of meristem development; IMP:UniProtKB.
GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
GO; GO:0048831; P:regulation of shoot system development; IMP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
GO; GO:0080117; P:secondary growth; IMP:UniProtKB.
CDD; cd00075; HATPase_c; 1.
CDD; cd00082; HisKA; 1.
CDD; cd06223; PRTases_typeI; 1.
CDD; cd00156; REC; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR006189; CHASE_dom.
InterPro; IPR011006; CheY-like_superfamily.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR003661; HisK_dim/P.
InterPro; IPR036097; HisK_dim/P_sf.
InterPro; IPR000836; PRibTrfase_dom.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
Pfam; PF03924; CHASE; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00512; HisKA; 1.
Pfam; PF00072; Response_reg; 2.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM01079; CHASE; 1.
SMART; SM00387; HATPase_c; 1.
SMART; SM00388; HisKA; 1.
SMART; SM00448; REC; 2.
SUPFAM; SSF47384; SSF47384; 1.
SUPFAM; SSF52172; SSF52172; 2.
SUPFAM; SSF55874; SSF55874; 2.
PROSITE; PS50839; CHASE; 1.
PROSITE; PS50109; HIS_KIN; 1.
PROSITE; PS50110; RESPONSE_REGULATORY; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytokinin signaling pathway;
Developmental protein; Endoplasmic reticulum; Kinase; Membrane;
Phosphoprotein; Reference proteome; Repeat; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 1036 Histidine kinase 3.
/FTId=PRO_0000398588.
TOPO_DOM 1 8 Extracellular. {ECO:0000255}.
TRANSMEM 9 29 Helical. {ECO:0000255}.
TOPO_DOM 30 94 Cytoplasmic. {ECO:0000255}.
TRANSMEM 95 115 Helical. {ECO:0000255}.
TOPO_DOM 116 399 Extracellular. {ECO:0000255}.
TRANSMEM 400 420 Helical. {ECO:0000255}.
TOPO_DOM 421 1036 Cytoplasmic. {ECO:0000255}.
DOMAIN 163 389 CHASE. {ECO:0000255|PROSITE-
ProRule:PRU00049}.
DOMAIN 457 723 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
DOMAIN 746 865 Response regulatory 1.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
DOMAIN 891 1028 Response regulatory 2.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
MOD_RES 460 460 Phosphohistidine; by autocatalysis.
{ECO:0000255|PROSITE-ProRule:PRU00107}.
MOD_RES 941 941 4-aspartylphosphate.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
MUTAGEN 243 243 P->S: In ore12-1; delayed leaf senescence
and abolished cytokinin-dependent
phosphorylation activity toward ARR2.
{ECO:0000269|PubMed:16407152}.
MUTAGEN 281 281 T->I: Loss of cyokinin-mediated
activation.
{ECO:0000269|PubMed:17956858}.
MUTAGEN 448 448 D->N: Delayed leaf senescence.
{ECO:0000269|PubMed:16407152}.
MUTAGEN 449 449 V->A: Constitutively activated
independently of cytokinin.
{ECO:0000269|PubMed:17956858}.
MUTAGEN 713 713 S->F: In ahk3-4; reduced sensitivity to
cytokinin (mostly in roots), and impaired
cytokinin repression of several Pi
starvation-responsive genes and increased
sucrose sensitivity.
{ECO:0000269|PubMed:15923327}.
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


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