CKL7_ARATH
ID CKL7_ARATH Reviewed; 476 AA.
AC Q9FFH8; Q8W0Z0;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Casein kinase 1-like protein 7 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 7 {ECO:0000303|PubMed:16126836};
GN Name=CKL7 {ECO:0000303|PubMed:16126836};
GN OrderedLocusNames=At5g44100 {ECO:0000312|Araport:AT5G44100};
GN ORFNames=MLN1.2 {ECO:0000312|EMBL:BAB10977.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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; AY943846; AAY24536.1; -; mRNA.
DR EMBL; AB005239; BAB10977.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95058.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69172.1; -; Genomic_DNA.
DR EMBL; AF462864; AAL58949.1; -; mRNA.
DR EMBL; BT015795; AAU90085.1; -; mRNA.
DR EMBL; BT021097; AAX12867.1; -; mRNA.
DR RefSeq; NP_001330873.1; NM_001344533.1.
DR RefSeq; NP_199223.1; NM_123777.4.
DR AlphaFoldDB; Q9FFH8; -.
DR SMR; Q9FFH8; -.
DR STRING; 3702.AT5G44100.1; -.
DR iPTMnet; Q9FFH8; -.
DR PaxDb; Q9FFH8; -.
DR PRIDE; Q9FFH8; -.
DR ProteomicsDB; 246707; -.
DR EnsemblPlants; AT5G44100.1; AT5G44100.1; AT5G44100.
DR EnsemblPlants; AT5G44100.2; AT5G44100.2; AT5G44100.
DR GeneID; 834433; -.
DR Gramene; AT5G44100.1; AT5G44100.1; AT5G44100.
DR Gramene; AT5G44100.2; AT5G44100.2; AT5G44100.
DR KEGG; ath:AT5G44100; -.
DR Araport; AT5G44100; -.
DR TAIR; locus:2167634; AT5G44100.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_2_1; -.
DR InParanoid; Q9FFH8; -.
DR OMA; RVQAGYE; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q9FFH8; -.
DR PRO; PR:Q9FFH8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFH8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090397; C:stigma papilla; IDA: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; 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..476
FT /note="Casein kinase 1-like protein 7"
FT /id="PRO_0000437146"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 299..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..459
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"
FT CONFLICT 136
FT /note="M -> I (in Ref. 4; AAL58949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53593 MW; 79721AF51E30135C CRC64;
MDLVIGGKFK LGKKIGSGSF GELYLGVNVQ TGEEVAVKLE NVKTKHPQLH YESKLYMLLQ
GGSGIPNIKW FGVEGDYSVM VIDLLGPSLE DLFNYCNRKL TLKTVLMLAD QLLNRVEFMH
TRGFLHRDIK PDNFLMGLGR KANQVYIIDF GLGKKYRDLQ THKHIPYREN KNLTGTARYA
SVNTHLGVEQ SRRDDLESLG YVLMYFLKGS LPWQGLKAGT KKQKYDRISE KKVSTPIEVL
CKNQPSEFVS YFHYCRSLRF DDKPDYSYLK RLFRDLFIRE GYQFDYVFDW TVLKYPQIGS
SSGSSSRTRH HTTAKPGFNA DPIERQERIL GKETTRYKIP GAVEAFSRRH PTTTSSPRDR
SRSRNSDDGP FSKQTHGDSE RANSSSRYRA SSSRKAVAAS SSRPSSAGGP SESRTSSRLV
SSSGGGGSGS GNGRPSTSQR VQAGYESKTL SFSRATAARN TREDQLRSFE LLSLRK
