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Casein kinase 1-like protein 1 (EC 2.7.11.1) (Casein kinase 1) (Casein kinase I isoform delta-like) (CKI-delta) (Protein CASEIN KINASE I-LIKE 1)

 CKL1_ARATH              Reviewed;         450 AA.
P42158; Q3KT07; Q9SZI1;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
10-JAN-2003, sequence version 2.
28-MAR-2018, entry version 144.
RecName: Full=Casein kinase 1-like protein 1 {ECO:0000305};
EC=2.7.11.1 {ECO:0000305};
AltName: Full=Casein kinase 1 {ECO:0000303|PubMed:7923358};
AltName: Full=Casein kinase I isoform delta-like {ECO:0000305};
Short=CKI-delta {ECO:0000305};
AltName: Full=Protein CASEIN KINASE I-LIKE 1 {ECO:0000303|PubMed:16126836};
Name=CKL1 {ECO:0000303|PubMed:16126836};
Synonyms=CK1 {ECO:0000303|PubMed:7923358}, CKI6 {ECO:0000305};
OrderedLocusNames=At4g26100; ORFNames=F20B18.210;
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].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=7923358; DOI=10.1016/0092-8674(94)90282-8;
Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M.;
"The A. thaliana disease resistance gene RPS2 encodes a protein
containing a nucleotide-binding site and leucine-rich repeats.";
Cell 78:1089-1099(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
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).
[3]
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).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
TISSUE SPECIFICITY.
PubMed=15010618; DOI=10.1023/B:PLAN.0000019063.18097.62;
Hu W., Wang Y., Bowers C., Ma H.;
"Isolation, sequence analysis, and expression studies of florally
expressed cDNAs in Arabidopsis.";
Plant Mol. Biol. 53:545-563(2003).
-!- FUNCTION: Casein kinases are operationally defined by their
preferential utilization of acidic proteins such as caseins as
substrates. It can phosphorylate a large number of proteins.
{ECO:0000250|UniProtKB:P48730}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000305}.
-!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48730}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48730}.
Cell junction, plasmodesma {ECO:0000269|PubMed:16126836}.
Note=Present in punctate particles with granular structure.
{ECO:0000269|PubMed:16126836}.
-!- TISSUE SPECIFICITY: Expressed in flowers.
{ECO:0000269|PubMed:15010618}.
-!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P48730}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA50233.1; Type=Frameshift; Positions=381, 414; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U12857; AAA50233.1; ALT_FRAME; mRNA.
EMBL; AY943842; AAY24532.1; -; mRNA.
EMBL; AL049483; CAB39675.1; -; Genomic_DNA.
EMBL; AL161564; CAB79465.1; -; Genomic_DNA.
EMBL; CP002687; AEE85157.1; -; Genomic_DNA.
EMBL; AY050784; AAK92719.1; -; mRNA.
EMBL; AY091299; AAM14238.1; -; mRNA.
PIR; T04265; T04265.
RefSeq; NP_194340.1; NM_118743.3.
UniGene; At.46720; -.
UniGene; At.69675; -.
ProteinModelPortal; P42158; -.
SMR; P42158; -.
BioGrid; 14003; 5.
IntAct; P42158; 3.
STRING; 3702.AT4G26100.1; -.
iPTMnet; P42158; -.
PaxDb; P42158; -.
EnsemblPlants; AT4G26100.1; AT4G26100.1; AT4G26100.
GeneID; 828716; -.
Gramene; AT4G26100.1; AT4G26100.1; AT4G26100.
KEGG; ath:AT4G26100; -.
Araport; AT4G26100; -.
TAIR; locus:2120765; AT4G26100.
eggNOG; KOG1164; Eukaryota.
eggNOG; ENOG410XPGP; LUCA.
HOGENOM; HOG000182055; -.
InParanoid; P42158; -.
KO; K02218; -.
OMA; VRNGPEQ; -.
OrthoDB; EOG09360AD1; -.
PhylomeDB; P42158; -.
BRENDA; 2.7.11.1; 399.
PRO; PR:P42158; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; P42158; baseline and differential.
Genevisible; P42158; AT.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0006897; P:endocytosis; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
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.
2: Evidence at transcript level;
ATP-binding; Cell junction; Complete proteome; Cytoplasm; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 450 Casein kinase 1-like protein 1.
/FTId=PRO_0000192855.
DOMAIN 9 278 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, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 38 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CONFLICT 47 47 P -> Q (in Ref. 1; AAA50233).
{ECO:0000305}.
CONFLICT 131 132 PD -> QT (in Ref. 1; AAA50233).
{ECO:0000305}.
CONFLICT 159 159 S -> M (in Ref. 1; AAA50233).
{ECO:0000305}.
CONFLICT 197 197 E -> K (in Ref. 1; AAA50233).
{ECO:0000305}.
CONFLICT 223 223 Q -> K (in Ref. 1; AAA50233).
{ECO:0000305}.
CONFLICT 241 241 C -> CPIEALC (in Ref. 1; AAA50233).
{ECO:0000305}.
CONFLICT 338 338 M -> T (in Ref. 1; AAA50233).
{ECO:0000305}.
CONFLICT 387 387 A -> V (in Ref. 1; AAA50233).
{ECO:0000305}.
CONFLICT 399 400 EE -> GG (in Ref. 1; AAA50233).
{ECO:0000305}.
SEQUENCE 450 AA; 50947 MW; 79DEE92E9353CA35 CRC64;
MEPRVGNKFR LGRKIGSGSF GEIYLGTNIH TNEELAIKLE NVKTKHPQLL YESKLYRILQ
GGTGVPNVKW FGVEGDYNVL VMDLLGPSLE DLFNFCSRKL SLKSVLMLAD QMINRVEFFH
SKSFLHRDLK PDNFLMGLGR RANQVYIIDF GLAKKYRDST THQHIPYREN KNLTGTARYA
SMNTHLGIEQ SRRDDLESLG YILMYFLKGS LPWQGLKAGT KKQKYERISE KKVSTSIEAL
CRGYPSEFAS YFHYCRSLRF DDKPDYAYLK RIFRDLFIRE GFQFDYVFDW TILKYQQSQL
TAPPSRALNP AVGTSAALPP GISNIDRYTG EEEGRPHMES SRRRVSGALD NSGNISNQPT
SSSARDSMIP SSSLFAQSAG SSRRVTAVSG SRDNFPGSEE LLQRSRTGDV SRGVIPRNSP
GEAGKSTRRH YESVVKGIDN LQVSDEHHPH


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