CKL12_ARATH
ID CKL12_ARATH Reviewed; 435 AA.
AC Q8VYK9;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Casein kinase 1-like protein 12 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 12 {ECO:0000303|PubMed:16126836};
GN Name=CKL12 {ECO:0000303|PubMed:16126836};
GN OrderedLocusNames=At5g57015 {ECO:0000312|Araport:AT5G57015};
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=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].
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).
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: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; AY943855; AAY24545.1; -; mRNA.
DR EMBL; AB024035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED96834.1; -; Genomic_DNA.
DR EMBL; AK118919; BAC43502.1; -; mRNA.
DR EMBL; AY070458; AAL49861.1; -; mRNA.
DR EMBL; AY091321; AAM14260.1; -; mRNA.
DR RefSeq; NP_680447.1; NM_148142.3.
DR AlphaFoldDB; Q8VYK9; -.
DR SMR; Q8VYK9; -.
DR STRING; 3702.AT5G57015.1; -.
DR iPTMnet; Q8VYK9; -.
DR PaxDb; Q8VYK9; -.
DR PRIDE; Q8VYK9; -.
DR ProteomicsDB; 246812; -.
DR EnsemblPlants; AT5G57015.1; AT5G57015.1; AT5G57015.
DR GeneID; 835804; -.
DR Gramene; AT5G57015.1; AT5G57015.1; AT5G57015.
DR KEGG; ath:AT5G57015; -.
DR Araport; AT5G57015; -.
DR TAIR; locus:504954933; AT5G57015.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_0_1; -.
DR InParanoid; Q8VYK9; -.
DR OMA; FWRIAKR; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q8VYK9; -.
DR PRO; PR:Q8VYK9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VYK9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..435
FT /note="Casein kinase 1-like protein 12"
FT /id="PRO_0000437151"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 313..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
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 435 AA; 49401 MW; FBC86AECAFF37903 CRC64;
MEPRVGNKYR LGRKIGSGSF GEIYLGTHIQ TNEEVAIKLE NVKTKHPQLL YESKLYRILQ
GGTGVPNIKW FGVEGDYNTL VMDLLGPSLE DLFNFCSRKL SLKSVLMLAD QMINRVEYFH
SKSFLHRDLK PDNFLMGLGR RANQVHIIDF GLAKKYRDNT THQHIPYREN KNLTGTARYA
SMNTHLGIEQ SRRDDLESLG YILMYFLKGS LPWQGLKAGT KKQKYERISE KKVSTSIESL
CRGYPSEFAS YFHYCRSLRF DDKPDYGYLK RIFRDLFIRE GFQFDYVFDW TILKYQQSQL
TAPPSRGLVS PAVGTSAGLP PGLTSIDRYG GEEEGGRPPM DSSRRRMSGA LENSGNLSSR
GPMMPSSSLF AQSAGSSRRV TSEELQRCRT GAGLRNSPVV TTPEGKRSSS TRKHYDSAIK
GIETLQVSDE RFHHH
