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Casein kinase 1-like protein 3 (EC 2.7.11.1) (Protein CASEIN KINASE I-LIKE 3) (CK1.3)

 CKL3_ARATH              Reviewed;         415 AA.
Q93Z18; Q9SVV5;
13-APR-2016, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
23-MAY-2018, entry version 144.
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;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[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; -.
PRIDE; 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; 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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