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Chloroplast sensor kinase, chloroplastic (EC 2.7.13.3)

 CSK_ARATH               Reviewed;         611 AA.
F4HVG8; F4HVG9; Q94AA5; Q9FXE6;
29-APR-2015, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
25-OCT-2017, entry version 53.
RecName: Full=Chloroplast sensor kinase, chloroplastic {ECO:0000303|PubMed:18632566};
EC=2.7.13.3 {ECO:0000269|PubMed:18632566};
Flags: Precursor;
Name=CSK {ECO:0000303|PubMed:18632566};
OrderedLocusNames=At1g67840 {ECO:0000312|Araport:AT1G67840};
ORFNames=F12A21.3 {ECO:0000312|EMBL:AAG28912.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=14993207; DOI=10.1101/gr.1515604;
Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G.,
Caboche M., Weissenbach J., Salanoubat M.;
"Whole genome sequence comparisons and 'full-length' cDNA sequences: a
combined approach to evaluate and improve Arabidopsis genome
annotation.";
Genome Res. 14:406-413(2004).
[5]
FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND AUTOPHOSPHORYLATION.
STRAIN=cv. Columbia;
PubMed=18632566; DOI=10.1073/pnas.0803928105;
Puthiyaveetil S., Kavanagh T.A., Cain P., Sullivan J.A., Newell C.A.,
Gray J.C., Robinson C., van der Giezen M., Rogers M.B., Allen J.F.;
"The ancestral symbiont sensor kinase CSK links photosynthesis with
gene expression in chloroplasts.";
Proc. Natl. Acad. Sci. U.S.A. 105:10061-10066(2008).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=22039472; DOI=10.1371/journal.pone.0026372;
Allen J.F., Santabarbara S., Allen C.A., Puthiyaveetil S.;
"Discrete redox signaling pathways regulate photosynthetic light-
harvesting and chloroplast gene transcription.";
PLoS ONE 6:E26372-E26372(2011).
[7]
REVIEW.
PubMed=21554328; DOI=10.1111/j.1365-3040.2011.02349.x;
Puthiyaveetil S., Ibrahim I.M., Allen J.F.;
"Oxidation-reduction signalling components in regulatory pathways of
state transitions and photosystem stoichiometry adjustment in
chloroplasts.";
Plant Cell Environ. 35:347-359(2012).
[8]
FUNCTION, INTERACTION WITH QUINONE ANALOG AND SIGA/SIG1, AND SUBUNIT.
PubMed=23754813; DOI=10.1098/rstb.2012.0260;
Puthiyaveetil S., Ibrahim I.M., Allen J.F.;
"Evolutionary rewiring: a modified prokaryotic gene-regulatory pathway
in chloroplasts.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci.
368:20120260-20120260(2013).
-!- FUNCTION: Sensor kinase required for sensing the plastoquinone
redox state involved in both photosystems stoichiometry adjustment
(e.g. long-term adaptation via transcriptional regulation of
reaction center genes of photosystems I and II) and state
transitions (e.g. short-term adaptation involving reversible post-
translational phosphorylation of light-harvesting complex II, LHC
II), thus linking photosynthesis with gene expression in
chloroplasts (PubMed:18632566, PubMed:22039472). Probably
phosphorylates SIGA/SIG1 in response to plastoquinone redox state
modification (PubMed:23754813). {ECO:0000269|PubMed:18632566,
ECO:0000269|PubMed:22039472, ECO:0000269|PubMed:23754813}.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine. {ECO:0000269|PubMed:18632566}.
-!- SUBUNIT: Self-interacts. Interacts with the quinone analog 2,5-
dibromo-3-methyl-5-isopropyl-p-benzoquinone (DBMIB) and with
SIGA/SIG1. {ECO:0000269|PubMed:23754813}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:18632566}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=F4HVG8-1; Sequence=Displayed;
Name=2;
IsoId=F4HVG8-2; Sequence=VSP_057631, VSP_057632;
Note=No experimental confirmation available.
{ECO:0000312|EMBL:AEE34705.1};
-!- PTM: Autophosphorylated, probably on tyrosine residues, in
photosystem I (PS I) light and in the presence of manganese ions
Mn(2+), to a lesser degree, in the presence of calcium ions
Ca(2+), but not in the presence of magnesium ions Mg(2+).
Dithiothreitol (DTT) stimulates autophosphorylation.
{ECO:0000269|PubMed:18632566}.
-!- DISRUPTION PHENOTYPE: Abnormal regulation of psaA gene expression
by light variation and reduced plastoquinone pool
(PubMed:18632566, PubMed:22039472). Accentuated superimposition
effect of light leading to plastoquinone oxidation. Increased
level of non-photochemical quenching, faster pre-steady state
kinetics of the 'Kautsky' transient (PubMed:22039472).
{ECO:0000269|PubMed:18632566, ECO:0000269|PubMed:22039472}.
-!- SIMILARITY: Belongs to the chloroplast sensor kinase protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG28912.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAK83586.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAK83586.1; Type=Frameshift; Positions=141, 611; Evidence={ECO:0000305};
Sequence=AAM47338.1; Type=Frameshift; Positions=611; Evidence={ECO:0000305};
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EMBL; AC008113; AAG28912.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE34704.1; -; Genomic_DNA.
EMBL; CP002684; AEE34705.1; -; Genomic_DNA.
EMBL; AY049244; AAK83586.1; ALT_SEQ; mRNA.
EMBL; AY113030; AAM47338.1; ALT_SEQ; mRNA.
EMBL; BX814127; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A96701; A96701.
RefSeq; NP_564908.1; NM_105452.2. [F4HVG8-1]
RefSeq; NP_974101.1; NM_202372.2. [F4HVG8-2]
UniGene; At.26196; -.
ProteinModelPortal; F4HVG8; -.
STRING; 3702.AT1G67840.1; -.
PaxDb; F4HVG8; -.
EnsemblPlants; AT1G67840.1; AT1G67840.1; AT1G67840. [F4HVG8-1]
EnsemblPlants; AT1G67840.2; AT1G67840.2; AT1G67840. [F4HVG8-2]
GeneID; 843110; -.
Gramene; AT1G67840.1; AT1G67840.1; AT1G67840.
Gramene; AT1G67840.2; AT1G67840.2; AT1G67840.
KEGG; ath:AT1G67840; -.
Araport; AT1G67840; -.
TAIR; locus:2008525; AT1G67840.
eggNOG; ENOG410IK9Q; Eukaryota.
eggNOG; ENOG410Z19J; LUCA.
HOGENOM; HOG000077496; -.
InParanoid; F4HVG8; -.
OMA; MHCLAPF; -.
OrthoDB; EOG093607IA; -.
PRO; PR:F4HVG8; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; F4HVG8; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0016301; F:kinase activity; IDA:TAIR.
GO; GO:0004673; F:protein histidine kinase activity; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0048038; F:quinone binding; IDA:UniProtKB.
GO; GO:0051776; P:detection of redox state; IMP:UniProtKB.
GO; GO:0080005; P:photosystem stoichiometry adjustment; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
GO; GO:0010109; P:regulation of photosynthesis; IMP:UniProtKB.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR036890; HATPase_C_sf.
SUPFAM; SSF55874; SSF55874; 1.
1: Evidence at protein level;
Alternative splicing; Chloroplast; Coiled coil; Complete proteome;
Kinase; Phosphoprotein; Plastid; Reference proteome; Transferase;
Transit peptide.
TRANSIT 1 79 Chloroplast. {ECO:0000255}.
CHAIN 80 611 Chloroplast sensor kinase, chloroplastic.
{ECO:0000255}.
/FTId=PRO_0000432898.
DOMAIN 312 602 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
COILED 345 380 {ECO:0000255}.
COMPBIAS 224 235 Poly-Glu. {ECO:0000255}.
VAR_SEQ 440 445 PCDISN -> KTMRHF (in isoform 2).
/FTId=VSP_057631.
VAR_SEQ 446 611 Missing (in isoform 2).
/FTId=VSP_057632.
CONFLICT 33 33 S -> T (in Ref. 4; BX814127).
{ECO:0000305}.
CONFLICT 347 348 DL -> EI (in Ref. 4; BX814127).
{ECO:0000305}.
CONFLICT 374 374 V -> M (in Ref. 3; AAK83586/AAM47338).
{ECO:0000305}.
SEQUENCE 611 AA; 66843 MW; 529B85FFAE32203C CRC64;
MLLSAIASQT LLSSNPNLHF SNSIPNPRPS NPSLKLLNAS SSSSSSSSSS IFTRGLRYVN
HTVSNEESEP GGGETMVASA SAIASAIRGA STTPVEFTQM IEKDHLKTKI ILPSPDFQRL
CLEQLDLFRQ IVDPNAVLSI YVRPAGSYVM DRLELRRVTC YPSVNAGDVV ILVGNFGIPA
GLRAAEASLS SQQVELVSKH RAAVFPMVKH PFVVGFLVAE LPVEAEEEEE EEEEEKPHGV
NQFLSPEEAY ALPASANTKS PRVKLPSVKV FTEEQRSYAI NISRTLAMAY VMDQKTMLLQ
QSSWQNNVRM SKLVEQIRGP LSTMRTLSKM LSTHTKRNQI SHDIVEDLIV QGDQIKDTLE
ELQDAVHLTK ANIVRHNEEA LKKINKTHNE TRRSKYEHKD PIDGSQISST RLSLGSGLDD
SEMPMPPLAL APLQMHSIRP CDISNVLLDM VETVRPLALT QQRVVELGEN SASLQVAVEE
PALRQALSNL IEGALLRTHV GGKVEILSTR APAGGSLVVI DDDGPDMRYM TQMHSLTPFG
AELLSENMVE DNMTWNFVAG LTVAREILES YGCVIRVISP RSSDAALGAG GTRVELWLPA
FPAAVSEANE A


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