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Casein kinase II subunit alpha-4, chloroplastic (CK2-alpha4) (EC 2.7.11.1) (Plastid-targeted casein kinase 2 alpha) (cpCK2alpha)

 CSK2P_ARATH             Reviewed;         432 AA.
O64816; Q6QJ31;
16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
18-JUL-2018, entry version 127.
RecName: Full=Casein kinase II subunit alpha-4, chloroplastic {ECO:0000305};
Short=CK2-alpha4 {ECO:0000303|PubMed:26025542};
EC=2.7.11.1;
AltName: Full=Plastid-targeted casein kinase 2 alpha {ECO:0000303|PubMed:27064346};
Short=cpCK2alpha {ECO:0000303|PubMed:27064346};
Flags: Precursor;
Name=CKA4 {ECO:0000303|PubMed:26025542}; OrderedLocusNames=At2g23070;
ORFNames=F21P24.13;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 200-425.
STRAIN=cv. Columbia; TISSUE=Leaf;
Kurth J., Leister D.;
"Protein kinases in chloroplasts.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
SUBCELLULAR LOCATION.
PubMed=16926165; DOI=10.1093/pcp/pcj100;
Salinas P., Fuentes D., Vidal E., Jordana X., Echeverria M.,
Holuigue L.;
"An extensive survey of CK2 alpha and beta subunits in Arabidopsis:
multiple isoforms exhibit differential subcellular localization.";
Plant Cell Physiol. 47:1295-1308(2006).
[6]
FUNCTION.
PubMed=24803505; DOI=10.1093/jxb/eru190;
Wang Y., Chang H., Hu S., Lu X., Yuan C., Zhang C., Wang P., Xiao W.,
Xiao L., Xue G.P., Guo X.;
"Plastid casein kinase 2 knockout reduces abscisic acid (ABA)
sensitivity, thermotolerance, and expression of ABA- and heat-stress-
responsive nuclear genes.";
J. Exp. Bot. 65:4159-4175(2014).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26025542; DOI=10.1016/j.plantsci.2015.04.013;
Mulekar J.J., Huq E.;
"Arabidopsis casein kinase 2 alpha4 subunit regulates various
developmental pathways in a functionally overlapping manner.";
Plant Sci. 236:295-303(2015).
[8]
FUNCTION.
PubMed=27064346; DOI=10.3389/fpls.2016.00404;
Kim S.Y., Bender K.W., Walker B.J., Zielinski R.E., Spalding M.H.,
Ort D.R., Huber S.C.;
"The plastid casein kinase 2 phosphorylates Rubisco activase at the
Thr-78 Site but is not essential for regulation of Rubisco activation
state.";
Front. Plant Sci. 7:404-404(2016).
[9]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=26883224; DOI=10.1007/s00299-016-1939-5;
Wang W.S., Zhu J., Zhang K.X., Lue Y.T., Xu H.H.;
"A mutation of casein kinase 2 alpha4 subunit affects multiple
developmental processes in Arabidopsis.";
Plant Cell Rep. 35:1071-1080(2016).
-!- FUNCTION: Casein kinases are operationally defined by their
preferential utilization of acidic proteins such as caseins as
substrates. The alpha chain contains the catalytic site (By
similarity). Involved in the regulation of various developmental
processes (PubMed:26025542). Involved in the regulation of plant
growth and flowering time (PubMed:26883224). Involved in
retrograde signaling in plant responses to abscisic acid (ABA) and
heat stress. May act as an enhancing factor in abiotic stress
signaling through modulation of the expression of some molecular
players in retrograde signaling (PubMed:24803505). Phosphorylates
RuBisCo activase (RCA) at Thr-78 (PubMed:27064346).
{ECO:0000250|UniProtKB:Q08467, ECO:0000269|PubMed:24803505,
ECO:0000269|PubMed:26025542, ECO:0000269|PubMed:26883224,
ECO:0000269|PubMed:27064346}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:16926165}.
-!- TISSUE SPECIFICITY: Expressed in root tips, lateral root
primordia, cotyledons, leaf primordia, sepals, filaments, stigma,
and anthers. {ECO:0000269|PubMed:26883224}.
-!- DISRUPTION PHENOTYPE: Defects in root, hypocotyl, cotyledon and
leaf development. Delayed flowering. Reduced growth, delayed
flowering and hyperaccumulation of anthocyanins.
{ECO:0000269|PubMed:26883224}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CK2 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AC004401; AAC17823.1; -; Genomic_DNA.
EMBL; CP002685; AEC07404.1; -; Genomic_DNA.
EMBL; AY062631; AAL32709.1; -; mRNA.
EMBL; AY081478; AAM10040.1; -; mRNA.
EMBL; AY536852; AAS65790.1; -; mRNA.
PIR; B84620; B84620.
RefSeq; NP_179889.1; NM_127871.5.
UniGene; At.26849; -.
ProteinModelPortal; O64816; -.
SMR; O64816; -.
BioGrid; 2190; 12.
IntAct; O64816; 12.
MINT; O64816; -.
STRING; 3702.AT2G23070.1; -.
iPTMnet; O64816; -.
PaxDb; O64816; -.
PRIDE; O64816; -.
EnsemblPlants; AT2G23070.1; AT2G23070.1; AT2G23070.
GeneID; 816837; -.
Gramene; AT2G23070.1; AT2G23070.1; AT2G23070.
KEGG; ath:AT2G23070; -.
Araport; AT2G23070; -.
TAIR; locus:2045339; AT2G23070.
eggNOG; KOG0668; Eukaryota.
eggNOG; ENOG410XNPP; LUCA.
HOGENOM; HOG000233021; -.
InParanoid; O64816; -.
KO; K03097; -.
OMA; CFKGPEL; -.
OrthoDB; EOG09360EPL; -.
PhylomeDB; O64816; -.
Reactome; R-ATH-2514853; Condensation of Prometaphase Chromosomes.
Reactome; R-ATH-6804756; Regulation of TP53 Activity through Phosphorylation.
PRO; PR:O64816; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O64816; baseline and differential.
Genevisible; O64816; AT.
GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0010019; P:chloroplast-nucleus signaling pathway; IMP:UniProtKB.
GO; GO:0040008; P:regulation of growth; IMP:UniProtKB.
GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
ATP-binding; Chloroplast; Complete proteome; Kinase;
Nucleotide-binding; Plastid; Reference proteome;
Serine/threonine-protein kinase; Transferase; Transit peptide.
TRANSIT 1 55 Chloroplast. {ECO:0000255}.
CHAIN 56 432 Casein kinase II subunit alpha-4,
chloroplastic.
/FTId=PRO_0000417493.
DOMAIN 132 417 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 138 146 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 61 75 Gln-rich.
ACT_SITE 249 249 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 161 161 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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


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