STN8_ARATH
ID STN8_ARATH Reviewed; 495 AA.
AC Q9LZV4; Q8GZ98;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine/threonine-protein kinase STN8, chloroplastic;
DE EC=2.7.11.1;
DE AltName: Full=Protein STATE TRANSITION 8;
DE Flags: Precursor;
GN Name=STN8; OrderedLocusNames=At5g01920; ORFNames=T20L15_190;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=16040609; DOI=10.1074/jbc.m505729200;
RA Vainonen J.P., Hansson M., Vener A.V.;
RT "STN8 protein kinase in Arabidopsis thaliana is specific in phosphorylation
RT of photosystem II core proteins.";
RL J. Biol. Chem. 280:33679-33686(2005).
RN [6]
RP DISRUPTION PHENOTYPE.
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [8]
RP FUNCTION.
RX PubMed=18331354; DOI=10.1111/j.1742-4658.2008.06335.x;
RA Vainonen J.P., Sakuragi Y., Stael S., Tikkanen M., Allahverdiyeva Y.,
RA Paakkarinen V., Aro E., Suorsa M., Scheller H.V., Vener A.V., Aro E.M.;
RT "Light regulation of CaS, a novel phosphoprotein in the thylakoid membrane
RT of Arabidopsis thaliana.";
RL FEBS J. 275:1767-1777(2008).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=20028840; DOI=10.1105/tpc.109.069435;
RA Fristedt R., Willig A., Granath P., Crevecoeur M., Rochaix J.D.,
RA Vener A.V.;
RT "Phosphorylation of photosystem II controls functional macroscopic folding
RT of photosynthetic membranes in Arabidopsis.";
RL Plant Cell 21:3950-3964(2009).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20230505; DOI=10.1111/j.0960-7412.2010.04207.x;
RA Goral T.K., Johnson M.P., Brain A.P., Kirchhoff H., Ruban A.V.,
RA Mullineaux C.W.;
RT "Visualizing the mobility and distribution of chlorophyll proteins in
RT higher plant thylakoid membranes: effects of photoinhibition and protein
RT phosphorylation.";
RL Plant J. 62:948-959(2010).
CC -!- FUNCTION: Light-dependent serine/threonine protein kinase that
CC specifically phosphorylates N-terminal threonine residues in psbA/D1,
CC psbD/D2, psbC/CP43 and psbH, which are components of the core antenna
CC complex of photosystem II. Phosphorylation of PSII core components
CC facilitates the exchange of chlorophyll proteins between the grana and
CC the stroma lamellae. Also involved in the phosphorylation of the
CC calcium-sensing receptor (CaS). {ECO:0000269|PubMed:16040609,
CC ECO:0000269|PubMed:16237446, ECO:0000269|PubMed:18331354,
CC ECO:0000269|PubMed:20230505}.
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
CC {ECO:0000305|PubMed:16237446}.
CC -!- DISRUPTION PHENOTYPE: Not significantly affected in state transitions.
CC Enhanced thylakoid folding and reduced mobility of thylakoid proteins
CC under low-light conditions. {ECO:0000269|PubMed:15729347,
CC ECO:0000269|PubMed:20028840, ECO:0000269|PubMed:20230505}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41802.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL162351; CAB82762.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90410.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70167.1; -; Genomic_DNA.
DR EMBL; AK117124; BAC41802.1; ALT_INIT; mRNA.
DR EMBL; AK117628; BAC42284.1; -; mRNA.
DR EMBL; BT006132; AAP04117.1; -; mRNA.
DR PIR; T48213; T48213.
DR RefSeq; NP_001331798.1; NM_001342626.1.
DR RefSeq; NP_195812.1; NM_120270.4.
DR AlphaFoldDB; Q9LZV4; -.
DR SMR; Q9LZV4; -.
DR BioGRID; 17017; 2.
DR STRING; 3702.AT5G01920.1; -.
DR PaxDb; Q9LZV4; -.
DR PRIDE; Q9LZV4; -.
DR ProteomicsDB; 228427; -.
DR EnsemblPlants; AT5G01920.1; AT5G01920.1; AT5G01920.
DR EnsemblPlants; AT5G01920.2; AT5G01920.2; AT5G01920.
DR GeneID; 831741; -.
DR Gramene; AT5G01920.1; AT5G01920.1; AT5G01920.
DR Gramene; AT5G01920.2; AT5G01920.2; AT5G01920.
DR KEGG; ath:AT5G01920; -.
DR Araport; AT5G01920; -.
DR TAIR; locus:2181067; AT5G01920.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_029162_0_0_1; -.
DR InParanoid; Q9LZV4; -.
DR OMA; KFEGDRD; -.
DR OrthoDB; 1139314at2759; -.
DR PhylomeDB; Q9LZV4; -.
DR PRO; PR:Q9LZV4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZV4; baseline and differential.
DR Genevisible; Q9LZV4; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009534; C:chloroplast thylakoid; IEA:UniProtKB-SubCell.
DR GO; GO:0009579; C:thylakoid; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IMP:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0042549; P:photosystem II stabilization; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; 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; Thylakoid;
KW Transferase; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..495
FT /note="Serine/threonine-protein kinase STN8, chloroplastic"
FT /id="PRO_0000401138"
FT DOMAIN 133..477
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 308
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 139..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 495 AA; 54979 MW; 319005953DF3B1DD CRC64;
MASLLSPATP TATSAAFHSC STAGFSTPTH ISSQNSSLSL LSRRGCMMRC SFSPQDIPVD
SLSHLPPFLD FQNSLATFSD TQKWGFFVSA GIVWFYLTAR PGVLIGAIDA YLLAPLQLGL
DTLIGRRLKR SDFLVTEKLG EGSFGVVYAG VLLPKNSTLV DDVRVSKARA KAMDFTGEFK
QRVILKKVKV GVRGAEEFGE YEEWFNYRLS RAAPDTCAEF LGSFVADKTN TMFTKGGKWL
VWRFEGDRDL ADYMKDRSFP SNLESIMFGR VLQGVESVKR RALIIKQIMR QIITSLRKIH
GTGIVHRDVK PANLVVTKKG QIKLIDFGAA ADLRIGKNYI PERTLLDPDY CPPELYVLPE
ETPSPPPEPI AALLSPILWQ LNSPDLFDMY SAGIVLLQMA VPTLRSTAGL KNFNLEIKSV
EYDLNRWRER TRTRPDLSIL DLDSGRGWDL VTKLISERGS LRRGRLSAAA ALRHPYFLLG
GDQAAAVLSK LSFSK
