ID CKL1_ARATH Reviewed; 450 AA.
AC P42158; Q3KT07; Q9SZI1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 27-MAR-2024, entry version 173.
DE RecName: Full=Casein kinase 1-like protein 1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Casein kinase 1 {ECO:0000303|PubMed:7923358};
DE AltName: Full=Casein kinase I isoform delta-like {ECO:0000305};
DE Short=CKI-delta {ECO:0000305};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 1 {ECO:0000303|PubMed:16126836};
GN Name=CKL1 {ECO:0000303|PubMed:16126836};
GN Synonyms=CK1 {ECO:0000303|PubMed:7923358}, CKI6 {ECO:0000305};
GN OrderedLocusNames=At4g26100; ORFNames=F20B18.210;
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7923358; DOI=10.1016/0092-8674(94)90282-8;
RA Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M.;
RT "The A. thaliana disease resistance gene RPS2 encodes a protein containing
RT a nucleotide-binding site and leucine-rich repeats.";
RL Cell 78:1089-1099(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=16126836; DOI=10.1105/tpc.105.034330;
RA Lee J.-Y., Taoka K., Yoo B.-C., Ben-Nissan G., Kim D.-J., Lucas W.J.;
RT "Plasmodesmal-associated protein kinase in tobacco and Arabidopsis
RT recognizes a subset of non-cell-autonomous proteins.";
RL Plant Cell 17:2817-2831(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=15010618; DOI=10.1023/b:plan.0000019063.18097.62;
RA Hu W., Wang Y., Bowers C., Ma H.;
RT "Isolation, sequence analysis, and expression studies of florally expressed
RT cDNAs in Arabidopsis.";
RL Plant Mol. Biol. 53:545-563(2003).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. It can phosphorylate a large number of proteins.
CC {ECO:0000250|UniProtKB:P48730}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48730}. Cell
CC junction, plasmodesma {ECO:0000269|PubMed:16126836}. Note=Present in
CC punctate particles with granular structure.
CC {ECO:0000269|PubMed:16126836}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:15010618}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50233.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U12857; AAA50233.1; ALT_FRAME; mRNA.
DR EMBL; AY943842; AAY24532.1; -; mRNA.
DR EMBL; AL049483; CAB39675.1; -; Genomic_DNA.
DR EMBL; AL161564; CAB79465.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85157.1; -; Genomic_DNA.
DR EMBL; AY050784; AAK92719.1; -; mRNA.
DR EMBL; AY091299; AAM14238.1; -; mRNA.
DR PIR; T04265; T04265.
DR RefSeq; NP_194340.1; NM_118743.3.
DR AlphaFoldDB; P42158; -.
DR SMR; P42158; -.
DR BioGRID; 14003; 6.
DR IntAct; P42158; 3.
DR STRING; 3702.P42158; -.
DR iPTMnet; P42158; -.
DR PaxDb; 3702-AT4G26100-1; -.
DR ProteomicsDB; 246813; -.
DR EnsemblPlants; AT4G26100.1; AT4G26100.1; AT4G26100.
DR GeneID; 828716; -.
DR Gramene; AT4G26100.1; AT4G26100.1; AT4G26100.
DR KEGG; ath:AT4G26100; -.
DR Araport; AT4G26100; -.
DR TAIR; AT4G26100; CK1.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_0_1; -.
DR InParanoid; P42158; -.
DR OMA; TRRHYES; -.
DR OrthoDB; 1534388at2759; -.
DR PhylomeDB; P42158; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:P42158; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P42158; baseline and differential.
DR Genevisible; P42158; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; IDA:TAIR.
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; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14125; STKc_CK1_delta_epsilon; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR11909:SF18; CASEIN KINASE I ISOFORM DELTA; 1.
DR PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell junction; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..450
FT /note="Casein kinase 1-like protein 1"
FT /id="PRO_0000192855"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 311..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
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 CONFLICT 47
FT /note="P -> Q (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..132
FT /note="PD -> QT (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="S -> M (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="E -> K (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="Q -> K (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="C -> CPIEALC (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="M -> T (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="A -> V (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..400
FT /note="EE -> GG (in Ref. 1; AAA50233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 50947 MW; 79DEE92E9353CA35 CRC64;
MEPRVGNKFR LGRKIGSGSF GEIYLGTNIH TNEELAIKLE NVKTKHPQLL YESKLYRILQ
GGTGVPNVKW FGVEGDYNVL VMDLLGPSLE DLFNFCSRKL SLKSVLMLAD QMINRVEFFH
SKSFLHRDLK PDNFLMGLGR RANQVYIIDF GLAKKYRDST THQHIPYREN KNLTGTARYA
SMNTHLGIEQ SRRDDLESLG YILMYFLKGS LPWQGLKAGT KKQKYERISE KKVSTSIEAL
CRGYPSEFAS YFHYCRSLRF DDKPDYAYLK RIFRDLFIRE GFQFDYVFDW TILKYQQSQL
TAPPSRALNP AVGTSAALPP GISNIDRYTG EEEGRPHMES SRRRVSGALD NSGNISNQPT
SSSARDSMIP SSSLFAQSAG SSRRVTAVSG SRDNFPGSEE LLQRSRTGDV SRGVIPRNSP
GEAGKSTRRH YESVVKGIDN LQVSDEHHPH
//
