CKL6_ARATH
ID CKL6_ARATH Reviewed; 479 AA.
AC Q8LPJ1; O65463; Q8LFV8;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Casein kinase 1-like protein 6 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:16126836};
DE AltName: Full=Plasmodesmal-associated protein kinase 1 {ECO:0000303|PubMed:16126836};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 6 {ECO:0000303|PubMed:16126836};
GN Name=CKL6 {ECO:0000303|PubMed:16126836};
GN Synonyms=PAPK1 {ECO:0000303|PubMed:16126836};
GN OrderedLocusNames=At4g28540 {ECO:0000312|Araport:AT4G28540};
GN ORFNames=F20O9.240 {ECO:0000312|EMBL:CAA16895.1};
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, AND CATALYTIC ACTIVITY.
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, ACTIVE SITE, MUTAGENESIS OF LYS-42 AND ASP-132, SUBCELLULAR
RP LOCATION, SUBUNIT, DISRUPTION PHENOTYPE, AND TUBULIN-BINDING DOMAIN.
RC STRAIN=cv. Col-1;
RX PubMed=18945931; DOI=10.1104/pp.108.129346;
RA Ben-Nissan G., Cui W., Kim D.-J., Yang Y., Yoo B.-C., Lee J.-Y.;
RT "Arabidopsis casein kinase 1-like 6 contains a microtubule-binding domain
RT and affects the organization of cortical microtubules.";
RL Plant Physiol. 148:1897-1907(2008).
RN [7]
RP FUNCTION, ACTIVE SITE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-42 AND
RP ASP-132.
RX PubMed=19820321; DOI=10.4161/psb.4.7.8991;
RA Lee J.-Y.;
RT "Versatile casein kinase 1: multiple locations and functions.";
RL Plant Signal. Behav. 4:652-654(2009).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19941015; DOI=10.1007/s00709-009-0087-y;
RA Ben-Nissan G., Yang Y., Lee J.-Y.;
RT "Partitioning of casein kinase 1-like 6 to late endosome-like vesicles.";
RL Protoplasma 240:45-56(2010).
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 (By
CC similarity). Phosphorylates tubulins and microtubules in vitro
CC (PubMed:18945931). Involved in anisotropic cell growth and cell shape
CC formation via the regulation of microtubule organization
CC (PubMed:18945931, PubMed:19820321). {ECO:0000250|UniProtKB:P48730,
CC ECO:0000269|PubMed:18945931, ECO:0000269|PubMed:19820321}.
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:16126836};
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:16126836};
CC -!- SUBUNIT: Monomer (By similarity). Binds tubulins (PubMed:18945931).
CC {ECO:0000250|UniProtKB:P48730, ECO:0000269|PubMed:18945931}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48730}. Cell
CC junction, plasmodesma {ECO:0000269|PubMed:16126836}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:18945931,
CC ECO:0000269|PubMed:19820321}. Endomembrane system
CC {ECO:0000269|PubMed:19941015}. Cell junction
CC {ECO:0000269|PubMed:19941015}. Note=Present in punctate particles with
CC granular structure (PubMed:16126836, PubMed:18945931, PubMed:19820321,
CC PubMed:19941015). Associates transiently with cortical microtubules.
CC Shuttles between microtubules and punctate particles in a kinase
CC activity-dependent manner (PubMed:18945931, PubMed:19820321). Localizes
CC to motile vesicle-like structures (late endosomal-like compartments)
CC found both in the cytoplasm and at the cell periphery, especially at
CC the cellular junctions (PubMed:19941015). {ECO:0000269|PubMed:16126836,
CC ECO:0000269|PubMed:18945931, ECO:0000269|PubMed:19820321,
CC ECO:0000269|PubMed:19941015}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P48730}.
CC -!- DISRUPTION PHENOTYPE: Abnormal cortical microtubule organization
CC leading to anisotropic cell expansion. {ECO:0000269|PubMed:18945931}.
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=AAM61183.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA16895.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81442.1; Type=Erroneous gene model prediction; 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; AY943845; AAY24535.1; -; mRNA.
DR EMBL; AL021749; CAA16895.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161573; CAB81442.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85503.1; -; Genomic_DNA.
DR EMBL; AY099715; AAM20566.1; -; mRNA.
DR EMBL; BT000286; AAN15605.1; -; mRNA.
DR EMBL; AY084620; AAM61183.1; ALT_INIT; mRNA.
DR PIR; T04626; T04626.
DR RefSeq; NP_567812.1; NM_118996.5.
DR AlphaFoldDB; Q8LPJ1; -.
DR SMR; Q8LPJ1; -.
DR STRING; 3702.AT4G28540.1; -.
DR iPTMnet; Q8LPJ1; -.
DR PaxDb; Q8LPJ1; -.
DR PRIDE; Q8LPJ1; -.
DR ProteomicsDB; 246874; -.
DR EnsemblPlants; AT4G28540.1; AT4G28540.1; AT4G28540.
DR GeneID; 828972; -.
DR Gramene; AT4G28540.1; AT4G28540.1; AT4G28540.
DR KEGG; ath:AT4G28540; -.
DR Araport; AT4G28540; -.
DR TAIR; locus:2121338; AT4G28540.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_2_1; -.
DR InParanoid; Q8LPJ1; -.
DR OMA; QNHTRHR; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q8LPJ1; -.
DR PRO; PR:Q8LPJ1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LPJ1; baseline and differential.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0055028; C:cortical microtubule; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; TAS: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:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:UniProtKB.
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; Cell junction; Cytoplasm; Cytoskeleton; Kinase; Membrane;
KW Microtubule; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..479
FT /note="Casein kinase 1-like protein 6"
FT /id="PRO_0000436429"
FT DOMAIN 13..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 302..479
FT /note="Cortical microtubules-binding domain (CTD)"
FT /evidence="ECO:0000269|PubMed:18945931"
FT REGION 302..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:18945931, ECO:0000269|PubMed:19820321"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:18945931, ECO:0000269|PubMed:19820321"
FT MUTAGEN 42
FT /note="K->R: Loss of kinase activity and constitutive
FT localization to both punctate structures and microtubules,
FT leading to disturbed cortical microtubule organization and
FT polarized cell expansion; when associated with N-132."
FT /evidence="ECO:0000269|PubMed:18945931,
FT ECO:0000269|PubMed:19820321"
FT MUTAGEN 132
FT /note="D->N: Loss of kinase activity and constitutive
FT localization to both punctate structures and microtubules,
FT leading to disturbed cortical microtubule organization and
FT polarized cell expansion; when associated with R-42."
FT /evidence="ECO:0000269|PubMed:18945931,
FT ECO:0000269|PubMed:19820321"
SQ SEQUENCE 479 AA; 54025 MW; 53226DAD20B238FC CRC64;
MDLKMDNVIG GKFKLGRKIG GGSFGELFLA VSLQTGEEAA VKLEPAKTKH PQLHYESKIY
MLLQGGSGIP SLKWFGVQGD YNAMVIDLLG PSLEDLFNYC NRRLTLKAVL MLADQLISRV
EYMHSRGFLH RDIKPDNFLM GLGRKANQVY IIDFGLAKKY RDLQTHRHIP YRENKNLTGT
ARYASVNTHL GVEQSRRDDL ESLGYVLMYF LRGSLPWQGL KAGTKKQKYD RISEKKVSTP
IEVLCKSYPP EFVSYFQYCR SLRFEDKPDY SYLKRLFRDL FIREGYQFDY VFDWTALKHP
QSSARSHSST HERHRTGKPG MGAGPSAEKP ERISVGNIRD KFSGAVEAFA RRNVRGPSPH
QNHTRHRTLD EIPSMKPAVN MVSEKGRNTS RYGSASRRAV ASGSRPSSSG EQRESRDSSR
VASSGGGVRP SVFQRTQAAA AVSGYESKTA SAFNRDRVAA SRTARDEALR SFELLSIRK
