CSK_ARATH
ID CSK_ARATH Reviewed; 611 AA.
AC F4HVG8; F4HVG9; Q94AA5; Q9FXE6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Chloroplast sensor kinase, chloroplastic {ECO:0000303|PubMed:18632566};
DE EC=2.7.10.2 {ECO:0000305|PubMed:18632566};
DE Flags: Precursor;
GN Name=CSK {ECO:0000303|PubMed:18632566};
GN OrderedLocusNames=At1g67840 {ECO:0000312|Araport:AT1G67840};
GN ORFNames=F12A21.3 {ECO:0000312|EMBL:AAG28912.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP AND AUTOPHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=18632566; DOI=10.1073/pnas.0803928105;
RA Puthiyaveetil S., Kavanagh T.A., Cain P., Sullivan J.A., Newell C.A.,
RA Gray J.C., Robinson C., van der Giezen M., Rogers M.B., Allen J.F.;
RT "The ancestral symbiont sensor kinase CSK links photosynthesis with gene
RT expression in chloroplasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10061-10066(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22039472; DOI=10.1371/journal.pone.0026372;
RA Allen J.F., Santabarbara S., Allen C.A., Puthiyaveetil S.;
RT "Discrete redox signaling pathways regulate photosynthetic light-harvesting
RT and chloroplast gene transcription.";
RL PLoS ONE 6:E26372-E26372(2011).
RN [7]
RP REVIEW.
RX PubMed=21554328; DOI=10.1111/j.1365-3040.2011.02349.x;
RA Puthiyaveetil S., Ibrahim I.M., Allen J.F.;
RT "Oxidation-reduction signalling components in regulatory pathways of state
RT transitions and photosystem stoichiometry adjustment in chloroplasts.";
RL Plant Cell Environ. 35:347-359(2012).
RN [8]
RP FUNCTION, INTERACTION WITH QUINONE ANALOG AND SIGA/SIG1, AND SUBUNIT.
RX PubMed=23754813; DOI=10.1098/rstb.2012.0260;
RA Puthiyaveetil S., Ibrahim I.M., Allen J.F.;
RT "Evolutionary rewiring: a modified prokaryotic gene-regulatory pathway in
RT chloroplasts.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 368:20120260-20120260(2013).
RN [9]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-188, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Col-0;
RX PubMed=31925322; DOI=10.1038/s42003-019-0728-4;
RA Ibrahim I.M., Wu H., Ezhov R., Kayanja G.E., Zakharov S.D., Du Y.,
RA Tao W.A., Pushkar Y., Cramer W.A., Puthiyaveetil S.;
RT "An evolutionarily conserved iron-sulfur cluster underlies redox sensory
RT function of the Chloroplast Sensor Kinase.";
RL Commun. Biol. 3:13-13(2020).
CC -!- FUNCTION: Sensor kinase that senses the plastoquinone (PQ) redox state
CC involved in stoichiometry adjustment of both photosystems (e.g. long-
CC term adaptation via transcriptional regulation of reaction center genes
CC of photosystems I and II) and state transitions (e.g. short-term
CC adaptation involving reversible post-translational phosphorylation of
CC light-harvesting complex II, LHC II), thus linking photosynthesis with
CC gene expression in chloroplasts (PubMed:18632566, PubMed:22039472).
CC Autophosphorylates, probably on a tyrosine residue (PubMed:18632566).
CC Probably phosphorylates SIGA/SIG1 in response to plastoquinone redox
CC state modification (PubMed:23754813). Reduced PQ suppresses its
CC autophosphorylation activity. Represses expression of a number of
CC chloroplast-encoded genes (PubMed:31925322).
CC {ECO:0000269|PubMed:18632566, ECO:0000269|PubMed:22039472,
CC ECO:0000269|PubMed:23754813, ECO:0000269|PubMed:31925322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000305|PubMed:18632566};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:31925322};
CC Note=The 3Fe-4S cluster is redox-responsive, binds 1 cluster per
CC monomer. {ECO:0000269|PubMed:31925322};
CC -!- SUBUNIT: Self-interacts. Interacts with the plastoquinone analog 2,5-
CC dibromo-3-methyl-5-isopropyl-p-benzoquinone (DBMIB) and with SIGA/SIG1.
CC {ECO:0000269|PubMed:23754813}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18632566}. Note=Associates with thylakoid
CC membranes. {ECO:0000305|PubMed:31925322}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4HVG8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HVG8-2; Sequence=VSP_057631, VSP_057632;
CC -!- PTM: Autophosphorylated, possibly on tyrosine residues, in photosystem
CC I (PS I) light and in the presence of manganese ions Mn(2+), to a
CC lesser degree, in the presence of calcium ions Ca(2+), but not in the
CC presence of magnesium ions Mg(2+). Dithiothreitol (DTT) stimulates
CC autophosphorylation (PubMed:18632566). Phosphorylated on Ser-188 in
CC vivo after exposure to far-red light (when plastoquinone (PQ) is
CC oxidized). Not phosphorylated under orange light (reduces PQ)
CC (PubMed:31925322). {ECO:0000269|PubMed:18632566,
CC ECO:0000269|PubMed:31925322}.
CC -!- DISRUPTION PHENOTYPE: Abnormal regulation of psaA gene expression by
CC light variation and reduced plastoquinone (PQ) pool (PubMed:18632566,
CC PubMed:22039472). Accentuated superimposition effect of light leading
CC to PQ oxidation. Increased level of non-photochemical quenching, faster
CC pre-steady state kinetics of the 'Kautsky' transient (PubMed:22039472).
CC Up-regulation of chloroplast-encoded photosystem and non-photosystem
CC genes (PubMed:31925322). {ECO:0000269|PubMed:18632566,
CC ECO:0000269|PubMed:22039472, ECO:0000269|PubMed:31925322}.
CC -!- SIMILARITY: Belongs to the chloroplast sensor kinase protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG28912.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK83586.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK83586.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM47338.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC008113; AAG28912.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34704.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34705.1; -; Genomic_DNA.
DR EMBL; AY049244; AAK83586.1; ALT_SEQ; mRNA.
DR EMBL; AY113030; AAM47338.1; ALT_SEQ; mRNA.
DR EMBL; BX814127; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A96701; A96701.
DR RefSeq; NP_564908.1; NM_105452.2. [F4HVG8-1]
DR RefSeq; NP_974101.1; NM_202372.2. [F4HVG8-2]
DR AlphaFoldDB; F4HVG8; -.
DR STRING; 3702.AT1G67840.1; -.
DR PaxDb; F4HVG8; -.
DR PRIDE; F4HVG8; -.
DR ProteomicsDB; 220365; -. [F4HVG8-1]
DR EnsemblPlants; AT1G67840.1; AT1G67840.1; AT1G67840. [F4HVG8-1]
DR EnsemblPlants; AT1G67840.2; AT1G67840.2; AT1G67840. [F4HVG8-2]
DR GeneID; 843110; -.
DR Gramene; AT1G67840.1; AT1G67840.1; AT1G67840. [F4HVG8-1]
DR Gramene; AT1G67840.2; AT1G67840.2; AT1G67840. [F4HVG8-2]
DR KEGG; ath:AT1G67840; -.
DR Araport; AT1G67840; -.
DR TAIR; locus:2008525; AT1G67840.
DR eggNOG; ENOG502QPUM; Eukaryota.
DR HOGENOM; CLU_030225_0_0_1; -.
DR InParanoid; F4HVG8; -.
DR OMA; QGDHLKD; -.
DR OrthoDB; 516337at2759; -.
DR PRO; PR:F4HVG8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HVG8; baseline and differential.
DR Genevisible; F4HVG8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IDA:UniProtKB.
DR GO; GO:0051776; P:detection of redox state; IMP:UniProtKB.
DR GO; GO:0080005; P:photosystem stoichiometry adjustment; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0010109; P:regulation of photosynthesis; IMP:UniProtKB.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S; Alternative splicing; Chloroplast; Coiled coil; Iron; Iron-sulfur;
KW Kinase; Metal-binding; Phosphoprotein; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..79
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 80..611
FT /note="Chloroplast sensor kinase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432898"
FT DOMAIN 312..602
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 17..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..300
FT /note="GAF"
FT /evidence="ECO:0000305|PubMed:31925322"
FT REGION 385..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 345..380
FT /evidence="ECO:0000255"
FT COMPBIAS 385..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000305|PubMed:31925322"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:31925322"
FT VAR_SEQ 440..445
FT /note="PCDISN -> KTMRHF (in isoform 2)"
FT /id="VSP_057631"
FT VAR_SEQ 446..611
FT /note="Missing (in isoform 2)"
FT /id="VSP_057632"
FT CONFLICT 33
FT /note="S -> T (in Ref. 4; BX814127)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..348
FT /note="DL -> EI (in Ref. 4; BX814127)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="V -> M (in Ref. 3; AAK83586/AAM47338)"
FT /evidence="ECO:0000305"
SQ 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
