CKL10_ARATH
ID CKL10_ARATH Reviewed; 442 AA.
AC Q9LW62; Q39051;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Casein kinase 1-like protein 10 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 10 {ECO:0000303|PubMed:16126836};
GN Name=CKL10 {ECO:0000303|PubMed:16126836};
GN Synonyms=CKI2 {ECO:0000303|PubMed:7480353};
GN OrderedLocusNames=At3g23340 {ECO:0000312|Araport:AT3G23340};
GN ORFNames=MLM24.7 {ECO:0000312|EMBL:BAB02278.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 26-442.
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; AY943849; AAY24539.1; -; mRNA.
DR EMBL; AB015474; BAB02278.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76754.1; -; Genomic_DNA.
DR EMBL; AY054179; AAL06840.1; -; mRNA.
DR EMBL; AY074556; AAL67096.1; -; mRNA.
DR EMBL; X78819; CAA55396.1; -; mRNA.
DR RefSeq; NP_188976.1; NM_113237.3.
DR AlphaFoldDB; Q9LW62; -.
DR SMR; Q9LW62; -.
DR IntAct; Q9LW62; 5.
DR STRING; 3702.AT3G23340.1; -.
DR PaxDb; Q9LW62; -.
DR PRIDE; Q9LW62; -.
DR EnsemblPlants; AT3G23340.1; AT3G23340.1; AT3G23340.
DR GeneID; 821915; -.
DR Gramene; AT3G23340.1; AT3G23340.1; AT3G23340.
DR KEGG; ath:AT3G23340; -.
DR Araport; AT3G23340; -.
DR TAIR; locus:2090875; AT3G23340.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_2_1; -.
DR InParanoid; Q9LW62; -.
DR OMA; IYLAVNV; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q9LW62; -.
DR PRO; PR:Q9LW62; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LW62; 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; IEA:UniProtKB-SubCell.
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..442
FT /note="Casein kinase 1-like protein 10"
FT /id="PRO_0000437149"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 299..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..415
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 442 AA; 50381 MW; A57C7C2ABBCCB25D CRC64;
MDHVIGGKFK LGRKIGSGSF GELYIGINVQ TGEEVALKLE PVKTKHPQLH YESKVYMLLQ
GGTGVPHIKW FGVEGNYNCM AIDLLGPSLE DLFNYCTRSF SLKTVLMLAD QLINRVEYMH
SRGFLHRDIK PDNFLMGLGR KANQVYIIDY GLAKKYRDLQ THKHIPYREN KNLTGTARYA
SVNTHLGIEQ SRRDDLESLG YVLMYFIRGS LPWQGLKAGT KKQKYEKISE KKMLTPVEVL
CKSYPSEFTS YFHYCRSLRF EDKPDYSYLK RLFRDLFIRE GYQFDYVFDW TILKYPQSGS
ISKPRPNPKP ALDPPGPSAE RNEKPIVGQD LRERFSGAVE AFARRNVPSH GIRPKHIFSD
DASKEVQVSE KTRNEIATKM AVMSSSQPGS SGELSENRSS KLFSSSAQKI QPVQETKLSA
RLGRDDGLRS FDMLTIGSGK RK
