AHK1_ARATH
ID AHK1_ARATH Reviewed; 1207 AA.
AC Q9SXL4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Histidine kinase 1;
DE EC=2.7.13.3;
DE AltName: Full=Arabidopsis histidine kinase 1;
DE Short=AtHK1;
DE AltName: Full=Protein AUTHENTIC HIS-KINASE 1;
GN Name=AHK1; OrderedLocusNames=At2g17820; ORFNames=T13L16.16, T17A5;
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, TISSUE SPECIFICITY, INDUCTION, AND
RP MUTAGENESIS OF HIS-508 AND ASP-1075.
RX PubMed=10488240; DOI=10.2307/3871051;
RA Urao T., Yakubov B., Satoh R., Yamaguchi-Shinozaki K., Seki M.,
RA Hirayama T., Shinozaki K.;
RT "A transmembrane hybrid-type histidine kinase in Arabidopsis functions as
RT an osmosensor.";
RL Plant Cell 11:1743-1754(1999).
RN [2]
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 [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 INTERACTION WITH AHP2, AND MUTAGENESIS OF ASP-1075.
RX PubMed=10930573; DOI=10.1016/s0014-5793(00)01860-3;
RA Urao T., Miyata S., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "Possible His to Asp phosphorelay signaling in an Arabidopsis two-component
RT system.";
RL FEBS Lett. 478:227-232(2000).
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, 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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18441212; DOI=10.1105/tpc.107.055871;
RA Wohlbach D.J., Quirino B.F., Sussman M.R.;
RT "Analysis of the Arabidopsis histidine kinase ATHK1 reveals a connection
RT between vegetative osmotic stress sensing and seed maturation.";
RL Plant Cell 20:1101-1117(2008).
CC -!- FUNCTION: Functions as an osmosensor histidine kinase that detects
CC water stress and transmits the stress signal to a downstream MAPK
CC cascade. This protein undergoes an ATP-dependent autophosphorylation at
CC a conserved histidine residue in the kinase core, and a phosphoryl
CC group is then transferred to a conserved aspartate residue in the
CC receiver domain. Positive regulator of drought and salt stress
CC responses, and abscisic acid (ABA) signaling. Confers drought
CC tolerance, probably by regulating levels of ABA accumulation. Plays a
CC redundant role in regulating plant growth and development. Required for
CC the regulation of desiccation processes during seed formation.
CC {ECO:0000269|PubMed:10488240, ECO:0000269|PubMed:18077346,
CC ECO:0000269|PubMed:18441212}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Interacts with AHP2, depending of the phosphorylation state of
CC Asp-1075 in the receiver domain, but probably not with AHP1 and AHP3.
CC {ECO:0000269|PubMed:10930573}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, and, to a lower extent,
CC in stems, leaves and flowers. {ECO:0000269|PubMed:10488240}.
CC -!- INDUCTION: Up-regulated in response to changes in external osmolarity,
CC low temperature, cytokinin (CK) treatment, and dehydration.
CC {ECO:0000269|PubMed:10488240, 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: Insensitivity to ABA, but hypersensitivity to
CC drought and high salinity stresses. Loss of seed viability over time
CC dur to altered desiccation. {ECO:0000269|PubMed:18077346,
CC ECO:0000269|PubMed:18441212}.
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DR EMBL; AB010914; BAA32085.1; -; mRNA.
DR EMBL; CP002685; AEC06691.1; -; Genomic_DNA.
DR PIR; T08856; T08856.
DR PIR; T52459; T52459.
DR RefSeq; NP_565424.1; NM_127335.2.
DR AlphaFoldDB; Q9SXL4; -.
DR SMR; Q9SXL4; -.
DR BioGRID; 1648; 2.
DR IntAct; Q9SXL4; 1.
DR STRING; 3702.AT2G17820.1; -.
DR PaxDb; Q9SXL4; -.
DR PRIDE; Q9SXL4; -.
DR ProteomicsDB; 244720; -.
DR EnsemblPlants; AT2G17820.1; AT2G17820.1; AT2G17820.
DR GeneID; 816291; -.
DR Gramene; AT2G17820.1; AT2G17820.1; AT2G17820.
DR KEGG; ath:AT2G17820; -.
DR Araport; AT2G17820; -.
DR TAIR; locus:2827836; AT2G17820.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_104_15_1; -.
DR InParanoid; Q9SXL4; -.
DR OMA; MVLWFEV; -.
DR OrthoDB; 184294at2759; -.
DR BRENDA; 2.7.13.3; 399.
DR PRO; PR:Q9SXL4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SXL4; baseline and differential.
DR Genevisible; Q9SXL4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IMP:TAIR.
DR GO; GO:0005034; F:osmosensor activity; IMP:TAIR.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0010431; P:seed maturation; IMP:TAIR.
DR GO; GO:0010375; P:stomatal complex patterning; IMP:TAIR.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cell membrane; Kinase; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..1207
FT /note="Histidine kinase 1"
FT /id="PRO_0000398586"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..1207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 505..763
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 1045..1196
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 508
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1127
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 508
FT /note="H->V: Loss of histidine kinase activity."
FT /evidence="ECO:0000269|PubMed:10488240"
FT MUTAGEN 1075
FT /note="D->E: Loss of histidine kinase activity and impaired
FT interaction with AHP2."
FT /evidence="ECO:0000269|PubMed:10488240,
FT ECO:0000269|PubMed:10930573"
FT CONFLICT 1046
FT /note="I -> F (in Ref. 1; BAA32085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1207 AA; 135449 MW; 76892FC99352E149 CRC64;
MRGDSFSMSI ENLPDSPMGS RKKKMQIRKV FDKMTEWVTP WRSNLESPRE MMILRGDVEQ
DEFQYASSHC LSSYYSVFVV RLAIMVMLAI LIGLLTVLTW HFTRIYTKQS LQTLAYGLRY
ELLQRPVLRM WSVLNTTSEL TTAQVKLSEY VIKKYDKPTT QEELVEMYQA MKDVTWALFA
SAKALNAITI NYRNGFVQAF HRDPASSSTF YIFSDLKNYS ISGTGPEDVS GWNNKSIHGN
MSAIWYQQQL DPVTGENLGK PLKIPPDDLI NIAGISQVPD GEASWHVTVS KYMDSPLLSA
ALPVFDASNK SIVAVVGVTT ALYSVGQLMR DLVEVHGGHI YLTSQEGYLL ATSTDGPLLK
NTSNGPQLMK ATDSEEWVIK SGAQWLEKTY GSKRPHVVHA ENVKLGDQRY YIDSFYLNLK
RLPIVGVVII PRKFIMGKVD ERAFKTLIIL ISASVCIFFI GCVCILILTN GVSKEMKLRA
ELIRQLDARR RAEASSNYKS QFLANMSHEL RTPMAAVIGL LDILISDDCL SNEQYATVTQ
IRKCSTALLR LLNNILDLSK VESGKLVLEE AEFDLGRELE GLVDMFSVQC INHNVETVLD
LSDDMPALVR GDSARLVQIF ANLISNSIKF TTTGHIILRG WCENINSLHD EMSVSVDRRK
PWAPMKTKQV QHRNHLQKSC KNANKMVLWF EVDDTGCGID PSKWDSVFES FEQADPSTTR
THGGTGLGLC IVRNLVNKMG GEIKVVQKNG LGTLMRLYLI LSTPDTVDQN IQPDFSKYGL
VVMLSMYGST ARMITSKWLR KHGIATVEAS DWNELTQIIR DLLETGSRDN SFDSQHNISD
PLRAELSNIV EIKNPVFVIV VDIGVLDLTT NIWKEQLNYL DRFSNKAKFA WLLKHDTSNT
VKTELRRKGH VMMVNKPLYK AKMIQILEAV IKNRKRGLCN DLRNRGNGSD ESHDCLEIDP
TQFDTCSSDD SSETSGEKQV DKSVKPSTLH SPVLKNYLID ATTSNDDSTS ASMTQKNPEE
EDWKDRLYSG IALDGKNQKS LEGIRILLAE DTPVLQRVAT IMLEKMGATV TAVWDGQQAV
DSLNYKSINA QAPTEEHKSF EEETANKVTT RETSLRNSSP YDLILMDCQM PKMDGYEATK
AIRRAEIGTE LHIPIVALTA HAMSSDEAKC LEVGMDAYLT KPIDRKLMVS TILSLTKPSA
FQTSLSA
