CKL4_ARATH
ID CKL4_ARATH Reviewed; 414 AA.
AC Q8LPI7; Q56YK2; Q67Y90; Q9SVV3;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Casein kinase 1-like protein 4 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:23897926};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 4 {ECO:0000303|PubMed:16126836};
DE Short=CK1.4 {ECO:0000303|PubMed:23897926};
GN Name=CKL4 {ECO:0000303|PubMed:16126836};
GN OrderedLocusNames=At4g28860 {ECO:0000312|Araport:AT4G28860};
GN ORFNames=F16A16.30 {ECO:0000312|EMBL:CAA22966.2};
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] (ISOFORM 1), SUBCELLULAR LOCATION, GENE FAMILY,
RP AND 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] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 Q8LPI7; Q9MA55: ACBP4; NbExp=3; IntAct=EBI-25516910, EBI-2009699;
CC Q8LPI7; Q9FDW1: MYB44; NbExp=3; IntAct=EBI-25516910, EBI-15192813;
CC Q8LPI7; O23160: MYB73; NbExp=3; IntAct=EBI-25516910, EBI-25506855;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LPI7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LPI7-2; Sequence=VSP_058211;
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: 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=CAA22966.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81474.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY943853; AAY24543.1; -; mRNA.
DR EMBL; AL035353; CAA22966.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161573; CAB81474.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85555.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85556.1; -; Genomic_DNA.
DR EMBL; AK118912; BAC43495.1; -; mRNA.
DR EMBL; AY099731; AAM20582.1; -; mRNA.
DR EMBL; BT002172; AAN72183.1; -; mRNA.
DR EMBL; AK175508; BAD43271.1; -; mRNA.
DR EMBL; AK176345; BAD44108.1; -; mRNA.
DR EMBL; AK176578; BAD44341.1; -; mRNA.
DR EMBL; AK176894; BAD44657.1; -; mRNA.
DR EMBL; AK221320; BAD94106.1; -; mRNA.
DR PIR; T04513; T04513.
DR RefSeq; NP_001078465.1; NM_001084996.2. [Q8LPI7-2]
DR RefSeq; NP_194615.2; NM_119030.4. [Q8LPI7-1]
DR AlphaFoldDB; Q8LPI7; -.
DR SMR; Q8LPI7; -.
DR IntAct; Q8LPI7; 3.
DR STRING; 3702.AT4G28860.1; -.
DR iPTMnet; Q8LPI7; -.
DR PaxDb; Q8LPI7; -.
DR PRIDE; Q8LPI7; -.
DR ProteomicsDB; 246873; -. [Q8LPI7-1]
DR DNASU; 829007; -.
DR EnsemblPlants; AT4G28860.1; AT4G28860.1; AT4G28860. [Q8LPI7-1]
DR EnsemblPlants; AT4G28860.2; AT4G28860.2; AT4G28860. [Q8LPI7-2]
DR GeneID; 829007; -.
DR Gramene; AT4G28860.1; AT4G28860.1; AT4G28860. [Q8LPI7-1]
DR Gramene; AT4G28860.2; AT4G28860.2; AT4G28860. [Q8LPI7-2]
DR KEGG; ath:AT4G28860; -.
DR Araport; AT4G28860; -.
DR TAIR; locus:2117843; AT4G28860.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_2_3_1; -.
DR InParanoid; Q8LPI7; -.
DR OMA; HQGQGVR; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q8LPI7; -.
DR PRO; PR:Q8LPI7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LPI7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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; 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:0046777; P:protein autophosphorylation; HDA: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 Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..414
FT /note="Casein kinase 1-like protein 4"
FT /id="PRO_0000436022"
FT DOMAIN 9..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 302..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..407
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 VAR_SEQ 369..413
FT /note="MNMPSSTSLSPAGTSKRNVRPETSNSGFGSGNKTGGWTSPFMSPG -> VRA
FT YSFASS (in isoform 2)"
FT /id="VSP_058211"
FT CONFLICT 27
FT /note="T -> A (in Ref. 6; BAD44341)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="I -> V (in Ref. 6; BAD44341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 46709 MW; 0EB3281A1AF0A850 CRC64;
MERIIGGKYK LGRKIGGGSF GEIFLATHID TFEIVAVKIE NSKTKHPQLL YEAKLYRTLE
GGSGIPRIRW FGVDGTENAL VMDLLGPSLE DLFVYCGRKF SPKTVLMLAD QMLTRIEYVH
SKGYLHRDIK PDNFLMGLGR KANQVYLIDF GLAKRYRDAN TNRHIPYREN KNLTGTARYA
SCNTHLGIEQ GRRDDLESLG YVLLYFLRGS LPWQGLKAVD KKQKYDKICE KKISTPIEVL
CKSHPVEFAS YFHYCHTLTF DQRPDYGFLK RLFRDLFSRE GYEFDYIYDW TIIKYQQSQK
TRSQSQAVPG SSNARAIPMD TSNHRGGTKI SHEAQVSDRV RPANASGPSP QINTAVGRSL
GFDQVHKNMN MPSSTSLSPA GTSKRNVRPE TSNSGFGSGN KTGGWTSPFM SPGK
