CSK22_ARATH
ID CSK22_ARATH Reviewed; 403 AA.
AC Q08466; Q8H120; Q8H765; Q9SN18;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Casein kinase II subunit alpha-2;
DE Short=CK II;
DE EC=2.7.11.1;
DE AltName: Full=Casein kinase alpha 2 {ECO:0000305};
DE Short=AtCKA2 {ECO:0000303|PubMed:7678767};
DE Flags: Precursor;
GN Name=CKA2 {ECO:0000303|PubMed:7678767}; OrderedLocusNames=At3g50000;
GN ORFNames=F3A4.80;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7678767; DOI=10.1007/bf00019944;
RA Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N., Kamada H.,
RA Shinozaki K.;
RT "Cloning and characterization of two cDNAs encoding casein kinase II
RT catalytic subunits in Arabidopsis thaliana.";
RL Plant Mol. Biol. 21:279-289(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (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 [5]
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 [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19509278; DOI=10.1074/jbc.m109.006692;
RA Dennis M.D., Browning K.S.;
RT "Differential phosphorylation of plant translation initiation factors by
RT Arabidopsis thaliana CK2 holoenzymes.";
RL J. Biol. Chem. 284:20602-20614(2009).
RN [7]
RP FUNCTION.
RX PubMed=21330376; DOI=10.1074/jbc.m110.186882;
RA Bu Q., Zhu L., Dennis M.D., Yu L., Lu S.X., Person M.D., Tobin E.M.,
RA Browning K.S., Huq E.;
RT "Phosphorylation by CK2 enhances the rapid light-induced degradation of
RT phytochrome interacting factor 1 in Arabidopsis.";
RL J. Biol. Chem. 286:12066-12074(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 (By similarity). The alpha chain contains the catalytic
CC site. The tetrameric holoenzyme CK2, composed of two alpha and two beta
CC subunits, phosphorylates the transcription factor PIF1 after an
CC exposure to light, resulting in a proteasome-dependent degradation of
CC PIF1 and promotion of photomorphogenesis (PubMed:21330376). CK2
CC phosphorylates translation initiation factors. May participate in the
CC regulation of the initiation of translation (PubMed:19509278). Acts as
CC circadian clock component that maintains the correct period length
CC through phosphorylation of CCA1 (PubMed:21900482). May act as an
CC ectokinase that phosphorylates several extracellular proteins.
CC {ECO:0000250|UniProtKB:Q08467, ECO:0000269|PubMed:19509278,
CC ECO:0000269|PubMed:21330376, 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:0000269|PubMed:19509278}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16926165}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:16926165}. Note=Enriched in the
CC nucleolus. {ECO:0000269|PubMed:16926165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08466-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08466-2; Sequence=VSP_043760;
CC -!- TISSUE SPECIFICITY: Seems to be present in all plant organs. But seems
CC to be more expressed than CKA1. {ECO:0000269|PubMed:7678767}.
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; D10247; BAA01091.1; -; mRNA.
DR EMBL; AL132978; CAB62108.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78615.1; -; Genomic_DNA.
DR EMBL; AF370308; AAK44123.2; -; mRNA.
DR EMBL; BT000888; AAN41288.1; -; mRNA.
DR PIR; S31099; S31099.
DR PIR; T45853; T45853.
DR RefSeq; NP_190569.2; NM_114860.4. [Q08466-1]
DR AlphaFoldDB; Q08466; -.
DR SMR; Q08466; -.
DR BioGRID; 9480; 26.
DR IntAct; Q08466; 1.
DR STRING; 3702.AT3G50000.1; -.
DR PaxDb; Q08466; -.
DR PRIDE; Q08466; -.
DR ProteomicsDB; 220498; -. [Q08466-1]
DR EnsemblPlants; AT3G50000.1; AT3G50000.1; AT3G50000. [Q08466-1]
DR GeneID; 824162; -.
DR Gramene; AT3G50000.1; AT3G50000.1; AT3G50000. [Q08466-1]
DR KEGG; ath:AT3G50000; -.
DR Araport; AT3G50000; -.
DR eggNOG; KOG0668; Eukaryota.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; Q08466; -.
DR OMA; RAYWDYD; -.
DR OrthoDB; 1098380at2759; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:Q08466; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q08466; baseline and differential.
DR Genevisible; Q08466; AT.
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: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; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
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; Glycoprotein; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..403
FT /note="Casein kinase II subunit alpha-2"
FT /id="PRO_0000417492"
FT DOMAIN 104..389
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 110..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7678767"
FT /id="VSP_043760"
FT CONFLICT 142
FT /note="K -> E (in Ref. 1; BAA01091)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="E -> G (in Ref. 1; BAA01091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 47233 MW; 495EA87AF560FE83 CRC64;
MHLIFFFSYF LRRYLLLLCA ILILRAPLAH SLIPPLTCVN TGTVESDVTG IRFDRCLDTD
SLAKISLSTV MSKARVYTDV NVIRPKDYWD YESLNVQWGE QDDYEVVRKV GRGKYSEVFE
GINMNNNEKC IIKILKPVKK KKIRREIKIL QNLCGGPNIV KLLDVVRDQH SKTPSLIFEY
VNSTDFKVLY PTLTDYDIRY YIYELLKALD FCHSQGIMHR DVKPHNVMID HELRKLRLID
WGLAEFYHPG KEYNVRVASR YFKGPELLVD LQDYDYSLDM WSLGCMFAGM IFRKEPFFYG
HDNQDQLVKI AKVLGTDELN AYLNKYQLEL DTQLEALVGR HSRKPWSKFI NADNRHLVSP
EAIDYLDKLL RYDHQDRLTA KEAMAHPYFA QVRAAESSRM RTQ
