(data stored in ACNUC13479 zone)

SWISSPROT: 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   12-APR-2017, entry version 112.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   phosphorylation 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
RT   require 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.,
RA   Aro E.M.;
RT   "Light regulation of CaS, a novel phosphoprotein in the thylakoid
RT   membrane 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
RT   folding 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
RT   protein 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
CC       psbA/D1, psbD/D2, psbC/CP43 and psbH, which are components of the
CC       core antenna complex of photosystem II. Phosphorylation of PSII
CC       core components facilitates the exchange of chlorophyll proteins
CC       between the grana and the stroma lamellae. Also involved in the
CC       phosphorylation of the calcium-sensing receptor (CaS).
CC       {ECO:0000269|PubMed:16040609, ECO:0000269|PubMed:16237446,
CC       ECO:0000269|PubMed:18331354, ECO:0000269|PubMed:20230505}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid
CC       {ECO:0000305|PubMed:16237446}.
CC   -!- DISRUPTION PHENOTYPE: Not significantly affected in state
CC       transitions. Enhanced thylakoid folding and reduced mobility of
CC       thylakoid proteins under low-light conditions.
CC       {ECO:0000269|PubMed:15729347, ECO:0000269|PubMed:20028840,
CC       ECO:0000269|PubMed:20230505}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41802.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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   UniGene; At.23739; -.
DR   UniGene; At.67158; -.
DR   ProteinModelPortal; Q9LZV4; -.
DR   BioGrid; 17017; 2.
DR   STRING; 3702.AT5G01920.1; -.
DR   PaxDb; Q9LZV4; -.
DR   PRIDE; Q9LZV4; -.
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   eggNOG; ENOG410XPP3; LUCA.
DR   HOGENOM; HOG000029907; -.
DR   InParanoid; Q9LZV4; -.
DR   OMA; WRERTRT; -.
DR   OrthoDB; EOG09360BQA; -.
DR   PhylomeDB; Q9LZV4; -.
DR   PRO; PR:Q9LZV4; -.
DR   Proteomes; UP000006548; Chromosome 5.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042549; P:photosystem II stabilization; IMP:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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;
DR   PRODOM; Q9LZV4.
DR   SWISS-2DPAGE; Q9LZV4.
KW   ATP-binding; Chloroplast; Complete proteome; Kinase;
KW   Nucleotide-binding; Plastid; Reference proteome;
KW   Serine/threonine-protein kinase; Thylakoid; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     49       Chloroplast. {ECO:0000255}.
FT   CHAIN        50    495       Serine/threonine-protein kinase STN8,
FT                                chloroplastic.
FT                                /FTId=PRO_0000401138.
FT   DOMAIN      133    477       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     139    147       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    308    308       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     186    186       ATP. {ECO:0000255|PROSITE-
FT                                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
//

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