CKI1_ARATH
ID CKI1_ARATH Reviewed; 1122 AA.
AC O22267; A5YY37;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Histidine kinase CKI1;
DE EC=2.7.13.3;
DE AltName: Full=Protein CYTOKININ-INDEPENDENT 1;
GN Name=CKI1; OrderedLocusNames=At2g47430; ORFNames=T30B22.27;
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 FUNCTION.
RC STRAIN=cv. Wassilewskija; TISSUE=Shoot;
RX PubMed=8875940; DOI=10.1126/science.274.5289.982;
RA Kakimoto T.;
RT "CKI1, a histidine kinase homolog implicated in cytokinin signal
RT transduction.";
RL Science 274:982-985(1996).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 740-1003.
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. Lz-0,
RC cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Se-0, cv. Sorbo,
RC 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 [5]
RP FUNCTION, AND MUTAGENESIS OF ASP-1050.
RX PubMed=10610126; DOI=10.1271/bbb.63.1627;
RA Nakamura A., Kakimoto T., Imamura A., Suzuki T., Ueguchi C., Mizuno T.;
RT "Biochemical characterization of a putative cytokinin-responsive His-
RT kinase, CKI1, from Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 63:1627-1630(1999).
RN [6]
RP INTERACTION WITH AHP2 AND AHP3.
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=12426401; DOI=10.1073/pnas.232580499;
RA Pischke M.S., Jones L.G., Otsuga D., Fernandez D.E., Drews G.N.,
RA Sussman M.R.;
RT "An Arabidopsis histidine kinase is essential for megagametogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15800-15805(2002).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 150-ARG--TYR-153, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12774227; DOI=10.1007/s00438-003-0858-7;
RA Hejatko J., Pernisova M., Eneva T., Palme K., Brzobohaty B.;
RT "The putative sensor histidine kinase CKI1 is involved in female
RT gametophyte development in Arabidopsis.";
RL Mol. Genet. Genomics 269:443-453(2003).
RN [9]
RP FUNCTION.
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 [10]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, HOMODIMERIZATION, AND
RP MUTAGENESIS OF HIS-405.
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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=20363773; DOI=10.1105/tpc.108.065128;
RA Deng Y., Dong H., Mu J., Ren B., Zheng B., Ji Z., Yang W.-C., Liang Y.,
RA Zuo J.;
RT "Arabidopsis histidine kinase CKI1 acts upstream of histidine
RT phosphotransfer proteins to regulate female gametophyte development and
RT vegetative growth.";
RL Plant Cell 22:1232-1248(2010).
CC -!- FUNCTION: Essential protein. 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. Required for
CC the development of megagametophyte in female gametophyte (embryo sac)
CC independently of cytokinin. Contributes to vascular bundle formation
CC and secondary growth in a cytokinin-independent manner, probably by
CC promoting the maintenance of mitotic activity and/or identity of
CC procambial cells. Seems to influence and promote the cytokinin
CC signaling pathway. {ECO:0000269|PubMed:10610126,
CC ECO:0000269|PubMed:12426401, ECO:0000269|PubMed:12774227,
CC ECO:0000269|PubMed:18077346, ECO:0000269|PubMed:19622803,
CC ECO:0000269|PubMed:20363773, ECO:0000269|PubMed:8875940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Homodimer. Interacts with AHP2 and AHP3.
CC {ECO:0000269|PubMed:10930573}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19622803};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19622803}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissues of inflorescence
CC stems and floral organs, especially in procambium cells, and in
CC siliques. {ECO:0000269|PubMed:12426401, ECO:0000269|PubMed:19622803,
CC ECO:0000269|PubMed:20363773}.
CC -!- DEVELOPMENTAL STAGE: Present at low levels in developing ovules. Within
CC mature female gametophytes, high levels in the central cell nucleus and
CC weak levels in the egg cell nucleus. In fertilized ovules, expressed in
CC the endosperm nuclei during 2 days after pollination.
CC {ECO:0000269|PubMed:12426401, ECO:0000269|PubMed:12774227}.
CC -!- DISRUPTION PHENOTYPE: Cannot be transmitted through the female germ
CC line. Impaired megagametogenesis visible from the four-nucleate stage,
CC with two normal nuclei and two degenerated nuclei, leading to female
CC sterility. Normal response to cytokinins. {ECO:0000269|PubMed:12426401,
CC ECO:0000269|PubMed:12774227, ECO:0000269|PubMed:20363773}.
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DR EMBL; D87545; BAA13416.1; -; mRNA.
DR EMBL; AC002535; AAC62867.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10840.1; -; Genomic_DNA.
DR EMBL; EF598269; ABQ85241.1; -; Genomic_DNA.
DR EMBL; EF598270; ABQ85242.1; -; Genomic_DNA.
DR EMBL; EF598271; ABQ85243.1; -; Genomic_DNA.
DR EMBL; EF598272; ABQ85244.1; -; Genomic_DNA.
DR EMBL; EF598273; ABQ85245.1; -; Genomic_DNA.
DR EMBL; EF598274; ABQ85246.1; -; Genomic_DNA.
DR EMBL; EF598275; ABQ85247.1; -; Genomic_DNA.
DR EMBL; EF598276; ABQ85248.1; -; Genomic_DNA.
DR EMBL; EF598277; ABQ85249.1; -; Genomic_DNA.
DR EMBL; EF598278; ABQ85250.1; -; Genomic_DNA.
DR EMBL; EF598279; ABQ85251.1; -; Genomic_DNA.
DR EMBL; EF598280; ABQ85252.1; -; Genomic_DNA.
DR EMBL; EF598281; ABQ85253.1; -; Genomic_DNA.
DR EMBL; EF598282; ABQ85254.1; -; Genomic_DNA.
DR EMBL; EF598283; ABQ85255.1; -; Genomic_DNA.
DR EMBL; EF598284; ABQ85256.1; -; Genomic_DNA.
DR EMBL; EF598285; ABQ85257.1; -; Genomic_DNA.
DR EMBL; EF598286; ABQ85258.1; -; Genomic_DNA.
DR EMBL; EF598287; ABQ85259.1; -; Genomic_DNA.
DR EMBL; EF598288; ABQ85260.1; -; Genomic_DNA.
DR EMBL; EF598289; ABQ85261.1; -; Genomic_DNA.
DR EMBL; EF598290; ABQ85262.1; -; Genomic_DNA.
DR EMBL; EF598291; ABQ85263.1; -; Genomic_DNA.
DR PIR; T00441; T00441.
DR RefSeq; NP_182265.1; NM_130311.2.
DR PDB; 3MM4; X-ray; 2.00 A; A=944-1122.
DR PDB; 3MMN; X-ray; 2.20 A; A=944-1122.
DR PDB; 5LNM; X-ray; 1.95 A; A=944-1122.
DR PDB; 5LNN; X-ray; 1.60 A; A=944-1122.
DR PDB; 5N2N; X-ray; 2.05 A; A=944-1122.
DR PDBsum; 3MM4; -.
DR PDBsum; 3MMN; -.
DR PDBsum; 5LNM; -.
DR PDBsum; 5LNN; -.
DR PDBsum; 5N2N; -.
DR AlphaFoldDB; O22267; -.
DR SMR; O22267; -.
DR BioGRID; 4691; 5.
DR IntAct; O22267; 3.
DR STRING; 3702.AT2G47430.1; -.
DR PaxDb; O22267; -.
DR PRIDE; O22267; -.
DR ProteomicsDB; 246811; -.
DR EnsemblPlants; AT2G47430.1; AT2G47430.1; AT2G47430.
DR GeneID; 819356; -.
DR Gramene; AT2G47430.1; AT2G47430.1; AT2G47430.
DR KEGG; ath:AT2G47430; -.
DR Araport; AT2G47430; -.
DR TAIR; locus:2061971; AT2G47430.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_104_16_1; -.
DR InParanoid; O22267; -.
DR OMA; FHAYSTI; -.
DR OrthoDB; 244938at2759; -.
DR PhylomeDB; O22267; -.
DR BRENDA; 2.7.13.3; 399.
DR PRO; PR:O22267; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22267; baseline and differential.
DR Genevisible; O22267; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA: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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0009736; P:cytokinin-activated signaling pathway; TAS:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:UniProtKB.
DR GO; GO:0080117; P:secondary growth; IMP:UniProtKB.
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 3D-structure; Cell membrane; Developmental protein; Kinase; Membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1122
FT /note="Histidine kinase CKI1"
FT /id="PRO_0000398591"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..1122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 402..671
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 987..1120
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 918..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 405
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1050
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MUTAGEN 150..153
FT /note="RGDY->GT: In cki1-r; normal phenotype rescued from
FT En-1 insertional disruption phenotype."
FT /evidence="ECO:0000269|PubMed:12774227"
FT MUTAGEN 405
FT /note="H->Q: Dysfunction of the two-component signaling
FT pathway leading to defects in procambial cell maintenance
FT and proliferation, as well as the absence of secondary
FT growth."
FT /evidence="ECO:0000269|PubMed:19622803"
FT MUTAGEN 1050
FT /note="D->Q,E: Loss of histidine kinase activity."
FT /evidence="ECO:0000269|PubMed:10610126"
FT TURN 980..985
FT /evidence="ECO:0007829|PDB:5LNN"
FT STRAND 987..991
FT /evidence="ECO:0007829|PDB:5LNN"
FT HELIX 995..1007
FT /evidence="ECO:0007829|PDB:5LNN"
FT STRAND 1011..1018
FT /evidence="ECO:0007829|PDB:5LNN"
FT HELIX 1019..1036
FT /evidence="ECO:0007829|PDB:5LNN"
FT STRAND 1045..1051
FT /evidence="ECO:0007829|PDB:5LNN"
FT STRAND 1054..1056
FT /evidence="ECO:0007829|PDB:5LNN"
FT HELIX 1058..1070
FT /evidence="ECO:0007829|PDB:5LNN"
FT TURN 1071..1073
FT /evidence="ECO:0007829|PDB:5LNN"
FT STRAND 1078..1084
FT /evidence="ECO:0007829|PDB:5LNN"
FT HELIX 1088..1097
FT /evidence="ECO:0007829|PDB:5LNN"
FT STRAND 1101..1104
FT /evidence="ECO:0007829|PDB:5LNN"
FT HELIX 1110..1119
FT /evidence="ECO:0007829|PDB:5LNN"
SQ SEQUENCE 1122 AA; 125033 MW; C6833F731DA84781 CRC64;
MMVKVTKLVA SRPIVVFCVL AFLVVVFECI WISNWRTTTE NLVKEVASFT EDLRTSLVSE
IENIGKFTYA KTNLSTIGLA RVIDSYITNN DTGFTEIQTQ IAPLLFVAYS TILQVSQVSY
ISRDGLMFSY IAESNTSVAV FANSSSNSSR GDYTWYTQTV DQLTGRLNGN STKSQSLDVT
HTDWFQAAQS NNYTTAFVGT SLGGEDNETL IQSVVSLYSK KGLVSLGFPV KTLTEVLNSL
NLHGEELYMW TKDGTVLVRE GSLNDSFFIS NGSICFGRES NSLWSQCIPE NCSSSGYEVE
IKRLRYQAFC SVIEVSGVPL RYTLMFPNKG GATRIKHQAE KAKYQLIVVM IFLGFGWPVW
FVWFMMQATR REMHMRATLI NQMEATQQAE RKSMNKSQAF ANASHDIRGA LAGMKGLIDI
CRDGVKPGSD VDTTLNQVNV CAKDLVALLN SVLDMSKIES GKMQLVEEDF NLSKLLEDVI
DFYHPVAMKK GVDVVLDPHD GSVFKFSNVR GDSGRLKQIL NNLVSNAVKF TVDGHIAVRA
WAQRPGSNSS VVLASYPKGV SKFVKSMFCK NKEESSTYET EISNSIRNNA NTMEFVFEVD
DTGKGIPMEM RKSVFENYVQ VRETAQGHQG TGLGLGIVQS LVRLMGGEIR ITDKAMGEKG
TCFQFNVLLT TLESPPVSDM KVRQEIEAGG DYVSTPNLGL TINTSLGGSM NIRNLSPRFN
NCLSSSPKQE GSRVVLLLKN EERRRVTEKY IKNLGIKVTV VEKWEHLSYA LERLFGFSPQ
SSMGRAECSL SCPSSRELPF IGMDGIDSRS QLPKRRSISF SAVVLLVIDA KTGPFFELCD
IVKQFRRGLP HGISCKVVWL NESSTRVSER GDISCSRPLH GSRLMEVLKM LPEFGGTVLK
EPPTELQRES LLRHSFVAER SPKHKVQEEG PSSMFNKKLG KRIMASTDSE SETRVKSVRT
GRKPIGNPED EQETSKPSDD EFLRGKRVLV VDDNFISRKV ATGKLKKMGV SEVEQCDSGK
EALRLVTEGL TQREEQGSVD KLPFDYIFMD CQMPEMDGYE ATREIRKVEK SYGVRTPIIA
VSGHDPGSEE ARETIQAGMD AFLDKSLNQL ANVIREIESK RH
