CKI1_ORYSJ
ID CKI1_ORYSJ Reviewed; 463 AA.
AC Q6K9N1; Q70YQ4;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Casein kinase 1 {ECO:0000303|PubMed:14535884};
DE Short=OsCKI1 {ECO:0000303|PubMed:14535884};
DE EC=2.7.11.1 {ECO:0000269|PubMed:14535884};
DE AltName: Full=Protein HYBRID BREAKDOWN 2 {ECO:0000303|PubMed:20140455};
DE AltName: Full=Protein LOW TEMPERATURE GROWTH 1 {ECO:0000303|PubMed:24635058};
GN Name=CKI1;
GN Synonyms=HBD2 {ECO:0000303|PubMed:20140455},
GN LTG1 {ECO:0000303|PubMed:24635058};
GN OrderedLocusNames=Os02g0622100 {ECO:0000312|EMBL:BAF09379.1},
GN LOC_Os02g40860 {ECO:0000305};
GN ORFNames=OJ1234_B11.27 {ECO:0000312|EMBL:BAD21551.1},
GN OsJ_07571 {ECO:0000312|EMBL:EEE57397.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Zhonghua 11;
RX PubMed=14535884; DOI=10.1046/j.1365-313x.2003.01866.x;
RA Liu W., Xu Z.H., Luo D., Xue H.W.;
RT "Roles of OsCKI1, a rice casein kinase I, in root development and plant
RT hormone sensitivity.";
RL Plant J. 36:189-202(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16827922; DOI=10.1111/j.1365-313x.2006.02804.x;
RA Duan K., Li L., Hu P., Xu S.P., Xu Z.H., Xue H.W.;
RT "A brassinolide-suppressed rice MADS-box transcription factor, OsMDP1, has
RT a negative regulatory role in BR signaling.";
RL Plant J. 47:519-531(2006).
RN [8]
RP MUTAGENESIS OF ILE-357.
RX PubMed=20140455; DOI=10.1007/s00438-010-0514-y;
RA Yamamoto E., Takashi T., Morinaka Y., Lin S., Wu J., Matsumoto T.,
RA Kitano H., Matsuoka M., Ashikari M.;
RT "Gain of deleterious function causes an autoimmune response and Bateson-
RT Dobzhansky-Muller incompatibility in rice.";
RL Mol. Genet. Genomics 283:305-315(2010).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF ILE-357.
RX PubMed=24635058; DOI=10.1111/tpj.12487;
RA Lu G., Wu F.Q., Wu W., Wang H.J., Zheng X.M., Zhang Y., Chen X., Zhou K.,
RA Jin M., Cheng Z., Li X., Jiang L., Wang H., Wan J.;
RT "Rice LTG1 is involved in adaptive growth and fitness under low ambient
RT temperature.";
RL Plant J. 78:468-480(2014).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. Can phosphorylate casein in vitro. Required for normal root
CC development through modulation of cell elongation. Plants silencing
CC CKI1 show abnormal root development, with reduced number of lateral and
CC adventitious roots, and shortened primary roots as a result of reduced
CC cell elongation. May be involved in abscisic acid (ABA) and
CC brassinosteroid (BR) signaling pathways (PubMed:14535884). Plays an
CC important role in the adaptive growth and fitness under low temperature
CC (LT) conditions. May confer tolerance to LT through an auxin-dependent
CC process (PubMed:24635058). {ECO:0000269|PubMed:14535884,
CC ECO:0000269|PubMed:24635058}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:14535884};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:14535884};
CC -!- ACTIVITY REGULATION: Inhibited by N-(2-aminoethyl)-5-
CC chloroisoquinoline-8-sulfonamide (CKI-7).
CC {ECO:0000269|PubMed:14535884}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ZWB3}. Nucleus
CC {ECO:0000269|PubMed:14535884}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, panicles and seeds
CC (PubMed:14535884). Expressed in root tissues and lamina joints
CC (PubMed:16827922). {ECO:0000269|PubMed:14535884,
CC ECO:0000269|PubMed:16827922}.
CC -!- INDUCTION: Induced by 24-epi-brassinolide (24-eBL) and down-regulated
CC by abscisic acid (ABA). {ECO:0000269|PubMed:14535884}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P48730}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; AJ487966; CAD32377.1; -; mRNA.
DR EMBL; AP004053; BAD21551.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09379.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79831.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE57397.1; -; Genomic_DNA.
DR EMBL; AK101388; BAG95038.1; -; mRNA.
DR RefSeq; XP_015626436.1; XM_015770950.1.
DR AlphaFoldDB; Q6K9N1; -.
DR SMR; Q6K9N1; -.
DR STRING; 4530.OS02T0622100-01; -.
DR PaxDb; Q6K9N1; -.
DR PRIDE; Q6K9N1; -.
DR EnsemblPlants; Os02t0622100-01; Os02t0622100-01; Os02g0622100.
DR GeneID; 4330018; -.
DR Gramene; Os02t0622100-01; Os02t0622100-01; Os02g0622100.
DR KEGG; osa:4330018; -.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_2_1; -.
DR InParanoid; Q6K9N1; -.
DR OMA; PAEFPMY; -.
DR OrthoDB; 1097975at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:Gramene.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0009850; P:auxin metabolic process; IMP:Gramene.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0009741; P:response to brassinosteroid; IMP:Gramene.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:Gramene.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:Gramene.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Growth regulation; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transferase.
FT CHAIN 1..463
FT /note="Casein kinase 1"
FT /id="PRO_0000437421"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 296..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 357
FT /note="I->K: Poor growth, leading to a reduction in the
FT number of panicles and culm length. Reduced growth rate,
FT heading date and yield performance under low temperature."
FT /evidence="ECO:0000269|PubMed:20140455,
FT ECO:0000269|PubMed:24635058"
FT CONFLICT 151
FT /note="G -> V (in Ref. 1; CAD32377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 52727 MW; CEF2FD18047AD3EC CRC64;
MEHVIGGKFK LGRKIGSGSF GELYLGVNIQ SSEEVAIKLE SVKSRHPQLH YESKLYMLLQ
GGTGIPHLKW FGVEGEYNVM VIDLLGPSLE DLFNYCNRKF SLKTVLMLAD QMINRVEYMH
TRGFLHRDIK PDNFLMGLGR KASQVYVIDY GLAKKYRDLQ THKHIPYREN KNLTGTARYA
SVNTHLGVEQ SRRDDLESLG YVLMYFLRGS LPWQGLKAGT KKQKYDKISE KKMLTPVEVL
CKSYPTEFIS YFHYCRSLRF EDKPDYSYLK RLFRDLFIRE GYQLDYIFDW TKQGSESNRL
RSSGRTSGLV GPSAERTERA AARQDVPDRF SGTVDPFARR TGSGSGHYGE HTKHRNILDS
LLAPKTAVDL DKRRPTSSSR NGSTSRKALL SSSRPSSGDP IDPNRSNLIP TSSGSSRPST
MQRLHQSTGL ETRSSLTKTA RNVHDDPTLR TFERLSISAD RRK
