CKL9_ARATH
ID CKL9_ARATH Reviewed; 471 AA.
AC Q9ZWB3; Q38926;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Casein kinase 1-like protein 9 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:7527390};
DE AltName: Full=Dual specificity kinase 1 {ECO:0000303|PubMed:7527390};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 9 {ECO:0000305};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 9 ALPHA {ECO:0000303|PubMed:16126836};
DE AltName: Full=Protein CASEIN KINASE I-LIKE 9 BETA {ECO:0000303|PubMed:16126836};
GN Name=CKL9 {ECO:0000305};
GN Synonyms=ADK1 {ECO:0000303|PubMed:7527390}, CKI4 {ECO:0000305},
GN CKI5 {ECO:0000305}, CKL9ALPHA {ECO:0000303|PubMed:16126836},
GN CKL9BETA {ECO:0000303|PubMed:16126836};
GN OrderedLocusNames=At1g03930 {ECO:0000312|Araport:AT1G03930};
GN ORFNames=F21M11.14 {ECO:0000312|EMBL:AAD10678.1};
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=7527390; DOI=10.1016/s0021-9258(18)31740-x;
RA Ali N., Halfter U., Chua N.H.;
RT "Cloning and biochemical characterization of a plant protein kinase that
RT phosphorylates serine, threonine, and tyrosine.";
RL J. Biol. Chem. 269:31626-31629(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [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. Can phosphorylate casein on serine and threonine residues,
CC and poly(Glu,Tyr) in vitro. {ECO:0000269|PubMed:7527390}.
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:0000269|PubMed:7527390};
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:0000269|PubMed:7527390};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16126836}. Nucleus
CC {ECO:0000269|PubMed:16126836}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:7527390}.
CC -!- PTM: Autophosphorylated on serine, threonine and tyrosine residues.
CC {ECO:0000269|PubMed:7527390}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB47968.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAY24537.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; U48779; AAB47968.1; ALT_SEQ; mRNA.
DR EMBL; AY943847; AAY24537.1; ALT_SEQ; mRNA.
DR EMBL; AY943848; AAY24538.1; -; mRNA.
DR EMBL; AC003027; AAD10678.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27635.1; -; Genomic_DNA.
DR EMBL; AY065409; AAL38850.1; -; mRNA.
DR EMBL; AY075642; AAL77651.1; -; mRNA.
DR EMBL; AY096519; AAM20169.1; -; mRNA.
DR EMBL; AY101520; AAM26641.1; -; mRNA.
DR PIR; B86170; B86170.
DR RefSeq; NP_563695.2; NM_100274.3.
DR AlphaFoldDB; Q9ZWB3; -.
DR SMR; Q9ZWB3; -.
DR STRING; 3702.AT1G03930.1; -.
DR iPTMnet; Q9ZWB3; -.
DR PaxDb; Q9ZWB3; -.
DR PRIDE; Q9ZWB3; -.
DR ProteomicsDB; 246875; -.
DR EnsemblPlants; AT1G03930.1; AT1G03930.1; AT1G03930.
DR GeneID; 839368; -.
DR Gramene; AT1G03930.1; AT1G03930.1; AT1G03930.
DR KEGG; ath:AT1G03930; -.
DR Araport; AT1G03930; -.
DR TAIR; locus:2024147; AT1G03930.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_0_2_1; -.
DR InParanoid; Q9ZWB3; -.
DR OMA; KHPPGDS; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q9ZWB3; -.
DR PRO; PR:Q9ZWB3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZWB3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:TAIR.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..471
FT /note="Casein kinase 1-like protein 9"
FT /id="PRO_0000437148"
FT DOMAIN 9..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 300..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..471
FT /note="Basic and acidic 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 471 AA; 53002 MW; 0C69AE74B16C39B7 CRC64;
MDLVIGGKFK LGRKIGSGSF GELYLGINVQ TGEEVAVKLE SVKTKHPQLH YESKLYMLLQ
GGTGVPNLKW YGVEGDYNVM VIDLLGPSLE DLFNYCNRKL SLKTVLMLAD QLINRVEFMH
TRGFLHRDIK PDNFLMGLGR KANQVYIIDF GLGKKYRDLQ THRHIPYREN KNLTGTARYA
SVNTHLGVEQ SRRDDLEALG YVLMYFLKGS LPWQGLKAGT KKQKYDRISE KKVATPIEVL
CKNQPSEFVS YFRYCRSLRF DDKPDYSYLK RLFRDLFIRE GYQFDYVFDW TVLKYPQIGS
SSGSSSRTRN HTTANPGLTA GASLEKQERI AGKETRENRF SGAVEAFSRR HPATSTTRDR
SASRNSVDGP LSKHPPGDSE RPRSSSRYGS SSRRAIPSSS RPSSAGGPSD SRSSSRLVTS
TGGVGTVSNR ASTSQRIQAG NESRTSSFSR AARNTREDPL RRSLELLTLR K
