CKL8_ARATH
ID CKL8_ARATH Reviewed; 480 AA.
AC Q9LSX4; Q39052;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Casein kinase 1-like protein 8 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 8 {ECO:0000303|PubMed:16126836};
GN Name=CKL8 {ECO:0000303|PubMed:16126836};
GN Synonyms=CKI3 {ECO:0000303|PubMed:7480353};
GN OrderedLocusNames=At5g43320 {ECO:0000312|Araport:AT5G43320};
GN ORFNames=MWF20.1 {ECO:0000312|EMBL:BAA97411.1};
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], AND SUBCELLULAR LOCATION.
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 [MRNA] OF 117-480.
RX PubMed=7480353; DOI=10.1104/pp.109.2.687;
RA Klimczak L.J., Farini D., Lin C., Ponti D., Cashmore A.R., Giuliano G.;
RT "Multiple isoforms of Arabidopsis casein kinase I combine conserved
RT catalytic domains with variable carboxyl-terminal extensions.";
RL Plant Physiol. 109:687-696(1995).
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.
CC {ECO:0000250|UniProtKB:P48730}.
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:0000305};
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:0000305};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48730}. Cell
CC junction, plasmodesma {ECO:0000269|PubMed:16126836}. Note=Present in
CC punctate particles with granular structure.
CC {ECO:0000269|PubMed:16126836}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P48730}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; AY943854; AAY24544.1; -; mRNA.
DR EMBL; AB025638; BAA97411.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94945.1; -; Genomic_DNA.
DR EMBL; AF360257; AAK25967.1; -; mRNA.
DR EMBL; AY040071; AAK64129.1; -; mRNA.
DR EMBL; X78820; CAA55397.1; -; mRNA.
DR RefSeq; NP_199146.1; NM_123698.4.
DR AlphaFoldDB; Q9LSX4; -.
DR SMR; Q9LSX4; -.
DR IntAct; Q9LSX4; 2.
DR STRING; 3702.AT5G43320.1; -.
DR iPTMnet; Q9LSX4; -.
DR PaxDb; Q9LSX4; -.
DR PRIDE; Q9LSX4; -.
DR ProteomicsDB; 246708; -.
DR EnsemblPlants; AT5G43320.1; AT5G43320.1; AT5G43320.
DR GeneID; 834350; -.
DR Gramene; AT5G43320.1; AT5G43320.1; AT5G43320.
DR KEGG; ath:AT5G43320; -.
DR Araport; AT5G43320; -.
DR TAIR; locus:2176431; AT5G43320.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_2_1; -.
DR InParanoid; Q9LSX4; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q9LSX4; -.
DR PRO; PR:Q9LSX4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSX4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Cell junction; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..480
FT /note="Casein kinase 1-like protein 8"
FT /id="PRO_0000437147"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 298..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..461
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"
SQ SEQUENCE 480 AA; 54441 MW; E8950A1940A551C5 CRC64;
MDRVVGGKYK LGRKLGSGSF GELFLGVNVQ TGEEVAVKLE PARARHPQLH YESKLYMLLQ
GGTGIPHLKW YGVEGEYNCM VIDLLGPSME DLFNYCSRRF NLKTVLMLAD QMINRVEYMH
VRGFLHRDIK PDNFLMGLGR KANQVYIIDY GLAKKYRDLQ THRHIPYREN KNLTGTARYA
SVNTHLGIEQ SRRDDLESLG YVLMYFLRGS LPWQGLRAGT KKQKYDKISE KKRLTPVEVL
CKSFPPEFTS YFLYVRSLRF EDKPDYPYLK RLFRDLFIRE GYQFDYVFDW TILKYPQFSS
GSSSSSKPRS SLRPAMNPPV PIAERPDKPS AGAGQDSRDR FSGALEAYAR RNGSGSGVVQ
ADRSRPRTSE NVLASSKDTT PQNYERVERP ISSTRHASSS RKAVVSSVRA TSSADFTENR
SSRVVPSNGR SSTAQRTQLV PDPTTRPSSS SFTRAAPSRT ARDITLQSFE LLTIGNGKRK
