CKL3_ARATH
ID CKL3_ARATH Reviewed; 415 AA.
AC Q93Z18; Q9SVV5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Casein kinase 1-like protein 3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:23897926};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 3 {ECO:0000303|PubMed:16126836};
DE Short=CK1.3 {ECO:0000303|PubMed:23897926};
GN Name=CKL3 {ECO:0000303|PubMed:16126836};
GN OrderedLocusNames=At4g28880 {ECO:0000312|Araport:AT4G28880};
GN ORFNames=F16A16.10 {ECO:0000312|EMBL:CAA22964.2};
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], SUBCELLULAR LOCATION, GENE FAMILY, AND
RP NOMENCLATURE.
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 [2]
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 [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 [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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP AUTOPHOSPHORYLATION.
RX PubMed=21477822; DOI=10.1016/j.phytochem.2011.02.029;
RA Nemoto K., Seto T., Takahashi H., Nozawa A., Seki M., Shinozaki K.,
RA Endo Y., Sawasaki T.;
RT "Autophosphorylation profiling of Arabidopsis protein kinases using the
RT cell-free system.";
RL Phytochemistry 72:1136-1144(2011).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY BLUE LIGHT, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23897926; DOI=10.1105/tpc.113.114322;
RA Tan S.-T., Dai C., Liu H.-T., Xue H.-W.;
RT "Arabidopsis casein kinase1 proteins CK1.3 and CK1.4 phosphorylate
RT cryptochrome2 to regulate blue light signaling.";
RL Plant Cell 25:2618-2632(2013).
CC -!- FUNCTION: Protein kinase involved in blue light responses (e.g.
CC hypocotyl elongation and flowering) by phosphorylating CRY2 to reduce
CC its stability. {ECO:0000269|PubMed:23897926}.
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:23897926};
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:23897926};
CC -!- INTERACTION:
CC Q93Z18; Q9MA55: ACBP4; NbExp=3; IntAct=EBI-4442347, EBI-2009699;
CC Q93Z18; Q8H1G0: GATA28; NbExp=3; IntAct=EBI-4442347, EBI-4435064;
CC Q93Z18; Q9M000: SCL22; NbExp=3; IntAct=EBI-4442347, EBI-4424954;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16126836,
CC ECO:0000269|PubMed:23897926}. Nucleus {ECO:0000269|PubMed:16126836,
CC ECO:0000269|PubMed:23897926}. Note=Translocates mostly in nucleus upon
CC blue light treatment, especially in nuclear bodies.
CC {ECO:0000269|PubMed:23897926}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, stems, leaves and flowers.
CC {ECO:0000269|PubMed:23897926}.
CC -!- INDUCTION: Induced by blue light. {ECO:0000269|PubMed:23897926}.
CC -!- PTM: Slightly autophosphorylated. {ECO:0000269|PubMed:21477822}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to blue light (BL) leading to
CC shortened hypocotyls in BL. {ECO:0000269|PubMed:23897926}.
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=CAA22964.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81476.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY943852; AAY24542.1; -; mRNA.
DR EMBL; AL035353; CAA22964.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161573; CAB81476.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85558.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67211.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67212.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67213.1; -; Genomic_DNA.
DR EMBL; AY058842; AAL24230.1; -; mRNA.
DR EMBL; AY079031; AAL79581.1; -; mRNA.
DR EMBL; AK118601; BAC43200.1; -; mRNA.
DR PIR; T04511; T04511.
DR RefSeq; NP_001329054.1; NM_001341953.1.
DR RefSeq; NP_001329055.1; NM_001341952.1.
DR RefSeq; NP_001329056.1; NM_001341951.1.
DR RefSeq; NP_194617.2; NM_119032.5.
DR AlphaFoldDB; Q93Z18; -.
DR SMR; Q93Z18; -.
DR IntAct; Q93Z18; 5.
DR STRING; 3702.AT4G28880.1; -.
DR iPTMnet; Q93Z18; -.
DR PaxDb; Q93Z18; -.
DR PRIDE; Q93Z18; -.
DR ProteomicsDB; 246872; -.
DR DNASU; 829009; -.
DR EnsemblPlants; AT4G28880.1; AT4G28880.1; AT4G28880.
DR EnsemblPlants; AT4G28880.2; AT4G28880.2; AT4G28880.
DR EnsemblPlants; AT4G28880.3; AT4G28880.3; AT4G28880.
DR EnsemblPlants; AT4G28880.4; AT4G28880.4; AT4G28880.
DR GeneID; 829009; -.
DR Gramene; AT4G28880.1; AT4G28880.1; AT4G28880.
DR Gramene; AT4G28880.2; AT4G28880.2; AT4G28880.
DR Gramene; AT4G28880.3; AT4G28880.3; AT4G28880.
DR Gramene; AT4G28880.4; AT4G28880.4; AT4G28880.
DR KEGG; ath:AT4G28880; -.
DR Araport; AT4G28880; -.
DR TAIR; locus:2117778; AT4G28880.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_2_3_1; -.
DR InParanoid; Q93Z18; -.
DR OMA; LMYEAKL; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q93Z18; -.
DR PRO; PR:Q93Z18; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93Z18; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA:TAIR.
DR GO; GO:0009785; P:blue light signaling pathway; IMP:TAIR.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0009637; P:response to blue light; IEP:TAIR.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..415
FT /note="Casein kinase 1-like protein 3"
FT /id="PRO_0000436021"
FT DOMAIN 9..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 303..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..415
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"
SQ SEQUENCE 415 AA; 46891 MW; B7ED9B5A52F30C2D CRC64;
MERIIGGKYK LGRKIGGGSF GEIFLATHVD TFEIVAVKIE NSKTKHPQLL YEAKLYRILE
GGSGIPRIKW FGVDGTENAL VMDLLGPSLE DLFVYCGRKF SPKTVLMLAD QMLTRIEFVH
SKGYLHRDIK PDNFLMGLGR KANQVYLIDF GLAKRYRDAN TNRHIPYREN KNLTGTARYA
SCNTHLGIEQ SRRDDLESLG YVLLYFLRGS LPWQGLKAVD KKQKYDKICE KKISTPIEVL
CKNHPVEFAS YFHYCHTLTF DQRPDYGFLK RLFRDLFSRE GYEFDYIFDW TIIKYQQAQK
SRNQSQAVPG SSNPRAMPVD TSNHRGGPNI SYEAEASERV RSANAIGPSP QINNNTAAGR
TPGFDHPVHK NMNMPSTSLS PAGTSKRNVG PETSNSGYGS GNRTGWTSSF MSPEK
