CSK2P_ARATH
ID CSK2P_ARATH Reviewed; 432 AA.
AC O64816; Q6QJ31;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Casein kinase II subunit alpha-4, chloroplastic {ECO:0000305};
DE Short=CK2-alpha4 {ECO:0000303|PubMed:26025542};
DE EC=2.7.11.1;
DE AltName: Full=Plastid-targeted casein kinase 2 alpha {ECO:0000303|PubMed:27064346};
DE Short=cpCK2alpha {ECO:0000303|PubMed:27064346};
DE Flags: Precursor;
GN Name=CKA4 {ECO:0000303|PubMed:26025542}; OrderedLocusNames=At2g23070;
GN ORFNames=F21P24.13;
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].
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 [MRNA] OF 200-425.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RA Kurth J., Leister D.;
RT "Protein kinases in chloroplasts.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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.
RX PubMed=24803505; DOI=10.1093/jxb/eru190;
RA Wang Y., Chang H., Hu S., Lu X., Yuan C., Zhang C., Wang P., Xiao W.,
RA Xiao L., Xue G.P., Guo X.;
RT "Plastid casein kinase 2 knockout reduces abscisic acid (ABA) sensitivity,
RT thermotolerance, and expression of ABA- and heat-stress-responsive nuclear
RT genes.";
RL J. Exp. Bot. 65:4159-4175(2014).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26025542; DOI=10.1016/j.plantsci.2015.04.013;
RA Mulekar J.J., Huq E.;
RT "Arabidopsis casein kinase 2 alpha4 subunit regulates various developmental
RT pathways in a functionally overlapping manner.";
RL Plant Sci. 236:295-303(2015).
RN [8]
RP FUNCTION.
RX PubMed=27064346; DOI=10.3389/fpls.2016.00404;
RA Kim S.Y., Bender K.W., Walker B.J., Zielinski R.E., Spalding M.H.,
RA Ort D.R., Huber S.C.;
RT "The plastid casein kinase 2 phosphorylates Rubisco activase at the Thr-78
RT Site but is not essential for regulation of Rubisco activation state.";
RL Front. Plant Sci. 7:404-404(2016).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26883224; DOI=10.1007/s00299-016-1939-5;
RA Wang W.S., Zhu J., Zhang K.X., Lue Y.T., Xu H.H.;
RT "A mutation of casein kinase 2 alpha4 subunit affects multiple
RT developmental processes in Arabidopsis.";
RL Plant Cell Rep. 35:1071-1080(2016).
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 (By
CC similarity). Involved in the regulation of various developmental
CC processes (PubMed:26025542). Involved in the regulation of plant growth
CC and flowering time (PubMed:26883224). Involved in retrograde signaling
CC in plant responses to abscisic acid (ABA) and heat stress. May act as
CC an enhancing factor in abiotic stress signaling through modulation of
CC the expression of some molecular players in retrograde signaling
CC (PubMed:24803505). Phosphorylates RuBisCo activase (RCA) at Thr-78
CC (PubMed:27064346). {ECO:0000250|UniProtKB:Q08467,
CC ECO:0000269|PubMed:24803505, ECO:0000269|PubMed:26025542,
CC ECO:0000269|PubMed:26883224, ECO:0000269|PubMed:27064346}.
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: Tetramer of two alpha and two beta chains. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16926165}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, lateral root primordia,
CC cotyledons, leaf primordia, sepals, filaments, stigma, and anthers.
CC {ECO:0000269|PubMed:26883224}.
CC -!- DISRUPTION PHENOTYPE: Defects in root, hypocotyl, cotyledon and leaf
CC development. Delayed flowering. Reduced growth, delayed flowering and
CC hyperaccumulation of anthocyanins. {ECO:0000269|PubMed:26883224}.
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; AAC17823.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07404.1; -; Genomic_DNA.
DR EMBL; AY062631; AAL32709.1; -; mRNA.
DR EMBL; AY081478; AAM10040.1; -; mRNA.
DR EMBL; AY536852; AAS65790.1; -; mRNA.
DR PIR; B84620; B84620.
DR RefSeq; NP_179889.1; NM_127871.5.
DR AlphaFoldDB; O64816; -.
DR SMR; O64816; -.
DR BioGRID; 2190; 33.
DR IntAct; O64816; 12.
DR MINT; O64816; -.
DR STRING; 3702.AT2G23070.1; -.
DR iPTMnet; O64816; -.
DR PaxDb; O64816; -.
DR PRIDE; O64816; -.
DR ProteomicsDB; 224535; -.
DR EnsemblPlants; AT2G23070.1; AT2G23070.1; AT2G23070.
DR GeneID; 816837; -.
DR Gramene; AT2G23070.1; AT2G23070.1; AT2G23070.
DR KEGG; ath:AT2G23070; -.
DR Araport; AT2G23070; -.
DR TAIR; locus:2045339; AT2G23070.
DR eggNOG; KOG0668; Eukaryota.
DR HOGENOM; CLU_000288_70_3_1; -.
DR InParanoid; O64816; -.
DR OMA; YHPEKEY; -.
DR OrthoDB; 1098380at2759; -.
DR PhylomeDB; O64816; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:O64816; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64816; baseline and differential.
DR Genevisible; O64816; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
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:0071215; P:cellular response to abscisic acid stimulus; IGI:TAIR.
DR GO; GO:0010019; P:chloroplast-nucleus signaling pathway; IMP:UniProtKB.
DR GO; GO:0010187; P:negative regulation of seed germination; IGI: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; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IMP:UniProtKB.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; 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 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Kinase; Nucleotide-binding; Plastid;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..432
FT /note="Casein kinase II subunit alpha-4, chloroplastic"
FT /id="PRO_0000417493"
FT DOMAIN 132..417
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 138..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 432 AA; 50236 MW; 6DFCF7453B225E4A CRC64;
MALRPCTGFT ISSLRNASAA NNNLFSLLSF SSSSPAKRNL LLSSLQDNLR RFASSASLYR
QHLRNQQQQH QQQQQSRVKE KSETLAQKIG KSIRRAGAPS KARVYADVNV VRPKDYWDYE
SLAVQWGVQD DYEVVRKVGR GKYSEVFEGI HATDNEKCVI KILKPVKKKK IKREIKILQN
LCGGPNIVKL LDIVRDQQSK TPSLIFEHVN NKDFKVLYPT LSDYDVRYYI FELLKALDFC
HSRGIMHRDV KPHNVMIDHE QRKLRLIDWG LAEFYHPGKE YNVRVASRYF KGPELLVDLQ
DYDYSLDLWS LGCMFAGMIF RKEPFFYGHD NYDQLVKIAK VLGTDELNAY LNKYRIELDP
NLTSLVGRHS RKPWTKFINS ENQHLAVPEA VDFVDKLLRY DHQERPTAKE AMAHPYFYPI
RNAESSRTPR SQ
