CSK23_ARATH
ID CSK23_ARATH Reviewed; 333 AA.
AC O64817; F4ILF5; Q8L5T7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Casein kinase II subunit alpha-3 {ECO:0000305};
DE Short=CK II;
DE EC=2.7.11.1;
GN Name=CKA3 {ECO:0000305}; OrderedLocusNames=At2g23080; ORFNames=F21P24.14;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16926165; DOI=10.1093/pcp/pcj100;
RA Salinas P., Fuentes D., Vidal E., Jordana X., Echeverria M., Holuigue L.;
RT "An extensive survey of CK2 alpha and beta subunits in Arabidopsis:
RT multiple isoforms exhibit differential subcellular localization.";
RL Plant Cell Physiol. 47:1295-1308(2006).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21735091; DOI=10.1007/s11010-011-0969-0;
RA Tosoni K., Costa A., Sarno S., D'Alessandro S., Sparla F., Pinna L.A.,
RA Zottini M., Ruzzene M.;
RT "The p23 co-chaperone protein is a novel substrate of CK2 in Arabidopsis.";
RL Mol. Cell. Biochem. 356:245-254(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21900482; DOI=10.1104/pp.111.179846;
RA Lu S.X., Liu H., Knowles S.M., Li J., Ma L., Tobin E.M., Lin C.;
RT "A role for protein kinase casein kinase2 alpha-subunits in the Arabidopsis
RT circadian clock.";
RL Plant Physiol. 157:1537-1545(2011).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. The alpha chain contains the catalytic site. The tetrameric
CC holoenzyme CK2 is composed of two alpha and two beta subunits (By
CC similarity). Acts as circadian clock component that maintains the
CC correct period length through phosphorylation of CCA1
CC (PubMed:21900482). {ECO:0000250|UniProtKB:Q08467,
CC ECO:0000269|PubMed:21900482}.
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 -!- 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;
CC -!- SUBUNIT: Heterotetramer of two catalytic alpha subunits and two
CC regulatory beta subunits. {ECO:0000305}.
CC -!- INTERACTION:
CC O64817; P25854: CAM4; NbExp=2; IntAct=EBI-1235683, EBI-1235664;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16926165,
CC ECO:0000269|PubMed:21735091}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:16926165}. Cytoplasm {ECO:0000269|PubMed:21735091}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O64817-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O64817-2; Sequence=VSP_043761, VSP_043762;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the triple mutant cka1, cka2 and cka3 show altered
CC circadian rhythms and delayed flowering under long day conditions.
CC {ECO:0000269|PubMed:21900482}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC004401; AAC17824.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07405.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07406.1; -; Genomic_DNA.
DR EMBL; AY035088; AAK59593.1; -; mRNA.
DR EMBL; AY062954; AAL33786.1; -; mRNA.
DR EMBL; BX819262; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY087736; AAM65273.1; -; mRNA.
DR PIR; C84620; C84620.
DR RefSeq; NP_179890.1; NM_127872.4. [O64817-1]
DR RefSeq; NP_973518.1; NM_201789.2. [O64817-2]
DR AlphaFoldDB; O64817; -.
DR SMR; O64817; -.
DR BioGRID; 2191; 28.
DR IntAct; O64817; 8.
DR STRING; 3702.AT2G23080.1; -.
DR iPTMnet; O64817; -.
DR PaxDb; O64817; -.
DR PRIDE; O64817; -.
DR ProteomicsDB; 224424; -. [O64817-1]
DR EnsemblPlants; AT2G23080.1; AT2G23080.1; AT2G23080. [O64817-1]
DR EnsemblPlants; AT2G23080.2; AT2G23080.2; AT2G23080. [O64817-2]
DR GeneID; 816838; -.
DR Gramene; AT2G23080.1; AT2G23080.1; AT2G23080. [O64817-1]
DR Gramene; AT2G23080.2; AT2G23080.2; AT2G23080. [O64817-2]
DR KEGG; ath:AT2G23080; -.
DR Araport; AT2G23080; -.
DR TAIR; locus:2045349; AT2G23080.
DR eggNOG; KOG0668; Eukaryota.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; O64817; -.
DR OMA; KDPARMG; -.
DR PhylomeDB; O64817; -.
DR PRO; PR:O64817; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64817; baseline and differential.
DR Genevisible; O64817; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005956; C:protein kinase CK2 complex; 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:0006325; P:chromatin organization; IDA:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IGI:TAIR.
DR GO; GO:0006281; P:DNA repair; IDA:TAIR.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IEP:TAIR.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IEP:TAIR.
DR GO; GO:0010332; P:response to gamma radiation; IMP:TAIR.
DR GO; GO:0010225; P:response to UV-C; IMP:TAIR.
DR CDD; cd14132; STKc_CK2_alpha; 1.
DR InterPro; IPR045216; CK2_alpha.
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 PANTHER; PTHR24054; PTHR24054; 1.
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 Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..333
FT /note="Casein kinase II subunit alpha-3"
FT /id="PRO_0000085897"
FT DOMAIN 34..319
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 292..307
FT /note="AIDFLDKLLQYDHQDR -> VLLFFEKHSFASFWVY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_043761"
FT VAR_SEQ 308..333
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_043762"
SQ SEQUENCE 333 AA; 39309 MW; B84D4168F3AC127A CRC64;
MSKARVYTDV NVVRPKEYWD YESLVVQWGH QDDYEVVRKV GRGKYSEVFE GKNVNTNERC
VIKILKPVKK KKIKREIKIL QNLCGGPNIV KLYDIVRDEH SKTPSLVFEF VNSVDFKVLY
PTLTDYDIRY YIYELLKALD FCHSQGIMHR DVKPHNVMID HQLRKLRLID WGLAEFYHPG
KEYNVRVASR YFKGPELLVD LQDYDYSLDM WSLGCMFAGM IFRKEPFFYG HDNHDQLVKI
AKVLGTNELD HYLNKYQLDL DPQLEALVGR HVPKPWSKFI NADNQHLVSP EAIDFLDKLL
QYDHQDRLTA REAMDHPYFA QVKAAESSRL RTQ
