GENTAUR Molecular Products.

 CKL3_ARATH              Reviewed;         415 AA.
 Q93Z18; Q9SVV5;
 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
 01-DEC-2001, sequence version 1.
 28-MAR-2018, entry version 142.
 RecName: Full=Casein kinase 1-like protein 3 {ECO:0000305};
          EC=2.7.11.1 {ECO:0000269|PubMed:23897926};
 AltName: Full=Protein CASEIN KINASE I-LIKE 3 {ECO:0000303|PubMed:16126836};
          Short=CK1.3 {ECO:0000303|PubMed:23897926};
 Name=CKL3 {ECO:0000303|PubMed:16126836};
 OrderedLocusNames=At4g28880 {ECO:0000312|Araport:AT4G28880};
 ORFNames=F16A16.10 {ECO:0000312|EMBL:CAA22964.2};
 Arabidopsis thaliana (Mouse-ear cress).
 Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
 Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
 Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
 Arabidopsis.
 NCBI_TaxID=3702;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, GENE FAMILY, AND
 NOMENCLATURE.
 PubMed=16126836; DOI=10.1105/tpc.105.034330;
 Lee J.-Y., Taoka K., Yoo B.-C., Ben-Nissan G., Kim D.-J., Lucas W.J.;
 "Plasmodesmal-associated protein kinase in tobacco and Arabidopsis
 recognizes a subset of non-cell-autonomous proteins.";
 Plant Cell 17:2817-2831(2005).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=cv. Columbia;
 PubMed=10617198; DOI=10.1038/47134;
 Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
 Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
 Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
 Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
 Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
 Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
 Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
 Langham S.-A., McCullagh B., Bilham L., Robben J.,
 van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
 Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
 Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
 Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
 Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
 Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
 De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
 van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
 Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
 Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
 Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
 Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
 Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
 Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
 Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
 Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
 Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
 Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
 Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
 Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
 Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
 Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
 Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
 Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
 Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
 Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
 Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
 Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
 Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
 Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
 Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
 Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
 Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
 Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
 Chen E., Marra M.A., Martienssen R., McCombie W.R.;
 "Sequence and analysis of chromosome 4 of the plant Arabidopsis
 thaliana.";
 Nature 402:769-777(1999).
 [3]
 GENOME REANNOTATION.
 STRAIN=cv. Columbia;
 The Arabidopsis Information Portal (Araport);
 Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=cv. Columbia;
 PubMed=14593172; DOI=10.1126/science.1088305;
 Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
 Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
 Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
 Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
 Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
 Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
 Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
 Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
 Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
 Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
 Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
 Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
 "Empirical analysis of transcriptional activity in the Arabidopsis
 genome.";
 Science 302:842-846(2003).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=cv. Columbia;
 PubMed=11910074; DOI=10.1126/science.1071006;
 Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
 Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
 Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
 Shibata K., Shinagawa A., Shinozaki K.;
 "Functional annotation of a full-length Arabidopsis cDNA collection.";
 Science 296:141-145(2002).
 [6]
 AUTOPHOSPHORYLATION.
 PubMed=21477822; DOI=10.1016/j.phytochem.2011.02.029;
 Nemoto K., Seto T., Takahashi H., Nozawa A., Seki M., Shinozaki K.,
 Endo Y., Sawasaki T.;
 "Autophosphorylation profiling of Arabidopsis protein kinases using
 the cell-free system.";
 Phytochemistry 72:1136-1144(2011).
 [7]
 FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY BLUE LIGHT, TISSUE
 SPECIFICITY, AND SUBCELLULAR LOCATION.
 STRAIN=cv. Columbia;
 PubMed=23897926; DOI=10.1105/tpc.113.114322;
 Tan S.-T., Dai C., Liu H.-T., Xue H.-W.;
 "Arabidopsis casein kinase1 proteins CK1.3 and CK1.4 phosphorylate
 cryptochrome2 to regulate blue light signaling.";
 Plant Cell 25:2618-2632(2013).
 -!- FUNCTION: Protein kinase involved in blue light responses (e.g.
     hypocotyl elongation and flowering) by phosphorylating CRY2 to
     reduce its stability. {ECO:0000269|PubMed:23897926}.
 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
     {ECO:0000269|PubMed:23897926}.
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16126836,
     ECO:0000269|PubMed:23897926}. Nucleus
     {ECO:0000269|PubMed:16126836, ECO:0000269|PubMed:23897926}.
     Note=Translocates mostly in nucleus upon blue light treatment,
     especially in nuclear bodies. {ECO:0000269|PubMed:23897926}.
 -!- TISSUE SPECIFICITY: Expressed in seedlings, stems, leaves and
     flowers. {ECO:0000269|PubMed:23897926}.
 -!- INDUCTION: Induced by blue light. {ECO:0000269|PubMed:23897926}.
 -!- PTM: Slightly autophosphorylated. {ECO:0000269|PubMed:21477822}.
 -!- DISRUPTION PHENOTYPE: Hypersensitivity to blue light (BL) leading
     to shortened hypocotyls in BL. {ECO:0000269|PubMed:23897926}.
 -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
     protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=CAA22964.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
     Sequence=CAB81476.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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 EMBL; AY943852; AAY24542.1; -; mRNA.
 EMBL; AL035353; CAA22964.2; ALT_SEQ; Genomic_DNA.
 EMBL; AL161573; CAB81476.1; ALT_SEQ; Genomic_DNA.
 EMBL; CP002687; AEE85558.1; -; Genomic_DNA.
 EMBL; CP002687; ANM67211.1; -; Genomic_DNA.
 EMBL; CP002687; ANM67212.1; -; Genomic_DNA.
 EMBL; CP002687; ANM67213.1; -; Genomic_DNA.
 EMBL; AY058842; AAL24230.1; -; mRNA.
 EMBL; AY079031; AAL79581.1; -; mRNA.
 EMBL; AK118601; BAC43200.1; -; mRNA.
 PIR; T04511; T04511.
 RefSeq; NP_001329054.1; NM_001341953.1.
 RefSeq; NP_001329055.1; NM_001341952.1.
 RefSeq; NP_001329056.1; NM_001341951.1.
 RefSeq; NP_194617.2; NM_119032.5.
 UniGene; At.70159; -.
 ProteinModelPortal; Q93Z18; -.
 SMR; Q93Z18; -.
 IntAct; Q93Z18; 2.
 STRING; 3702.AT4G28880.1; -.
 iPTMnet; Q93Z18; -.
 PaxDb; Q93Z18; -.
 DNASU; 829009; -.
 EnsemblPlants; AT4G28880.1; AT4G28880.1; AT4G28880.
 EnsemblPlants; AT4G28880.2; AT4G28880.2; AT4G28880.
 EnsemblPlants; AT4G28880.3; AT4G28880.3; AT4G28880.
 EnsemblPlants; AT4G28880.4; AT4G28880.4; AT4G28880.
 GeneID; 829009; -.
 Gramene; AT4G28880.1; AT4G28880.1; AT4G28880.
 Gramene; AT4G28880.2; AT4G28880.2; AT4G28880.
 Gramene; AT4G28880.3; AT4G28880.3; AT4G28880.
 Gramene; AT4G28880.4; AT4G28880.4; AT4G28880.
 KEGG; ath:AT4G28880; -.
 Araport; AT4G28880; -.
 TAIR; locus:2117778; AT4G28880.
 eggNOG; KOG1164; Eukaryota.
 eggNOG; ENOG410XPGP; LUCA.
 HOGENOM; HOG000182055; -.
 OMA; WLIELVH; -.
 OrthoDB; EOG09360B2G; -.
 PhylomeDB; Q93Z18; -.
 PRO; PR:Q93Z18; -.
 Proteomes; UP000006548; Chromosome 4.
 ExpressionAtlas; Q93Z18; baseline and differential.
 GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO; GO:0005634; C:nucleus; IDA:UniProtKB.
 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
 GO; GO:0009785; P:blue light signaling pathway; IMP:TAIR.
 GO; GO:0006897; P:endocytosis; IBA:GO_Central.
 GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
 GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
 GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
 GO; GO:0009637; P:response to blue light; IEP:TAIR.
 InterPro; IPR011009; Kinase-like_dom_sf.
 InterPro; IPR000719; Prot_kinase_dom.
 InterPro; IPR017441; Protein_kinase_ATP_BS.
 InterPro; IPR008271; Ser/Thr_kinase_AS.
 Pfam; PF00069; Pkinase; 1.
 SMART; SM00220; S_TKc; 1.
 SUPFAM; SSF56112; SSF56112; 1.
 PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
 PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
 PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
 1: Evidence at protein level;
 ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
 Nucleus; Phosphoprotein; Reference proteome;
 Serine/threonine-protein kinase; Transferase.
 CHAIN         1    415       Casein kinase 1-like protein 3.
                              /FTId=PRO_0000436021.
 DOMAIN        9    277       Protein kinase. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 NP_BIND      15     23       ATP. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 ACT_SITE    128    128       Proton acceptor. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 BINDING      38     38       ATP. {ECO:0000255|PROSITE-
                              ProRule:PRU00159}.
 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

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