STT7_ARATH
ID STT7_ARATH Reviewed; 562 AA.
AC Q9S713; A4FVQ4; Q56WW0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Serine/threonine-protein kinase STN7, chloroplastic;
DE EC=2.7.11.1;
DE AltName: Full=Protein STATE TRANSITION 7;
DE AltName: Full=Stt7 homolog;
DE Flags: Precursor;
GN Name=STN7; OrderedLocusNames=At1g68830; ORFNames=F14K14.6, T6L1.2;
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=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].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-562.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-167.
RX PubMed=15729347; DOI=10.1038/nature03286;
RA Bellafiore S., Barneche F., Peltier G., Rochaix J.-D.;
RT "State transitions and light adaptation require chloroplast thylakoid
RT protein kinase STN7.";
RL Nature 433:892-895(2005).
RN [6]
RP FUNCTION.
RX PubMed=16237446; DOI=10.1038/nature04016;
RA Bonardi V., Pesaresi P., Becker T., Schleiff E., Wagner R.,
RA Pfannschmidt T., Jahns P., Leister D.;
RT "Photosystem II core phosphorylation and photosynthetic acclimation require
RT two different protein kinases.";
RL Nature 437:1179-1182(2005).
RN [7]
RP FUNCTION.
RX PubMed=16897465; DOI=10.1007/s11103-006-9044-8;
RA Tikkanen M., Piippo M., Suorsa M., Sirpioe S., Mulo P., Vainonen J.,
RA Vener A.V., Allahverdiyeva Y., Aro E.-M.;
RT "State transitions revisited-a buffering system for dynamic low light
RT acclimation of Arabidopsis.";
RL Plant Mol. Biol. 62:779-793(2006).
RN [8]
RP FUNCTION.
RX PubMed=19113838; DOI=10.1021/bi8016334;
RA Fristedt R., Carlberg I., Zygadlo A., Piippo M., Nurmi M., Aro E.M.,
RA Scheller H.V., Vener A.V.;
RT "Intrinsically unstructured phosphoprotein TSP9 regulates light harvesting
RT in Arabidopsis thaliana.";
RL Biochemistry 48:499-509(2009).
RN [9]
RP FUNCTION.
RX PubMed=19706797; DOI=10.1105/tpc.108.064964;
RA Pesaresi P., Hertle A., Pribil M., Kleine T., Wagner R., Strissel H.,
RA Ihnatowicz A., Bonardi V., Scharfenberg M., Schneider A., Pfannschmidt T.,
RA Leister D.;
RT "Arabidopsis STN7 kinase provides a link between short- and long-term
RT photosynthetic acclimation.";
RL Plant Cell 21:2402-2423(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526; THR-537 AND THR-541, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=22616989; DOI=10.1016/j.febslet.2012.03.061;
RA Ingelsson B., Vener A.V.;
RT "Phosphoproteomics of Arabidopsis chloroplasts reveals involvement of the
RT STN7 kinase in phosphorylation of nucleoid protein pTAC16.";
RL FEBS Lett. 586:1265-1271(2012).
CC -!- FUNCTION: Serine/threonine protein kinase required for state transition
CC by phosphorylating light-harvesting complex II outer antennae (LCHII).
CC State transition plays a central role in response to environmental
CC changes and allows to adjust to changing light conditions via the
CC redistribution of light excitation energy between photosystem II (PSII)
CC and photosystem I (PSI). Phosphorylates the minor light harvesting
CC protein LHCB4.2/CP29 and is involved in the light-dependent
CC phosphorylation of TSP9. Acts as a key component of the long-term
CC response (LTR) signaling pathway. Mediates phosphorylation-dependent
CC PTAC16 subcellular localization to regulate plastid gene expression
CC (PubMed:22616989). {ECO:0000269|PubMed:15729347,
CC ECO:0000269|PubMed:16237446, ECO:0000269|PubMed:16897465,
CC ECO:0000269|PubMed:19113838, ECO:0000269|PubMed:19706797,
CC ECO:0000269|PubMed:22616989}.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:15729347}.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC011665; AAG51596.1; -; Genomic_DNA.
DR EMBL; AC011914; AAG52037.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34846.1; -; Genomic_DNA.
DR EMBL; BT030352; ABO38765.1; -; mRNA.
DR EMBL; AK221920; BAD94332.1; -; mRNA.
DR PIR; A96713; A96713.
DR RefSeq; NP_564946.1; NM_105557.6.
DR AlphaFoldDB; Q9S713; -.
DR SMR; Q9S713; -.
DR BioGRID; 28436; 3.
DR IntAct; Q9S713; 1.
DR MINT; Q9S713; -.
DR STRING; 3702.AT1G68830.1; -.
DR iPTMnet; Q9S713; -.
DR PaxDb; Q9S713; -.
DR PRIDE; Q9S713; -.
DR ProteomicsDB; 245351; -.
DR EnsemblPlants; AT1G68830.1; AT1G68830.1; AT1G68830.
DR GeneID; 843215; -.
DR Gramene; AT1G68830.1; AT1G68830.1; AT1G68830.
DR KEGG; ath:AT1G68830; -.
DR Araport; AT1G68830; -.
DR TAIR; locus:2205465; AT1G68830.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_029227_0_0_1; -.
DR InParanoid; Q9S713; -.
DR OMA; MILGKVQ; -.
DR OrthoDB; 1139314at2759; -.
DR PhylomeDB; Q9S713; -.
DR PRO; PR:Q9S713; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S713; baseline and differential.
DR Genevisible; Q9S713; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042651; C:thylakoid membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0009643; P:photosynthetic acclimation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0042548; P:regulation of photosynthesis, light reaction; IMP:TAIR.
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 InterPro; IPR044803; STT7-like.
DR PANTHER; PTHR46699; PTHR46699; 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 ATP-binding; Chloroplast; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Plastid; Reference proteome;
KW Serine/threonine-protein kinase; Thylakoid; Transferase; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..562
FT /note="Serine/threonine-protein kinase STN7, chloroplastic"
FT /id="PRO_0000024386"
FT DOMAIN 134..452
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 140..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 167
FT /note="K->R,Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:15729347"
SQ SEQUENCE 562 AA; 63252 MW; F06E0940E6D470C0 CRC64;
MATISPGGAY IGTPSPFLGK KLKPFSLTSP ILSFKPTVKL NSSCRAQLID TVHNLFIGVG
VGLPCTVMEC GDMIYRSTLP KSNGLTITAP GVALALTALS YLWATPGVAP GFFDMFVLAF
VERLFRPTFR KDDFVVGKKL GEGSFGVVYK VSLSKKRSNE EGEYVLKKAT EYGAVEIWMN
ERVRRACGNS CADFVYGFLD KSSKKGPEYW LLWKYEGEST LAGLMQSKEF PYNVETIILG
KVQDLPKGLE RENKIIQTIM RQLLFALDGL HSTGIIHRDV KPQNIIFSEG SRSFKIIDLG
AAADLRVGIN YIPKEFLLDP RYAAPEQYIM STQTPSAPSA PVAAALSPVL WQMNLPDRFD
IYSIGLIFLQ MAFPSLRSDS NLIQFNRQLK RCDYDLTAWR KLVEPRASAD LRRGFELVDL
DGGIGWELLT SMVRYKARQR ISAKAALAHP YFDRQGLLAL SVMQNLRMQY FRATQQDYSE
AANWVIQLMA KNGTEKDGGF TETQLQELRE KEPRKKANAQ RNALASALRL QRKLVKTVTE
TIDEISDGRK TVWWNRWIPR EE
