PSBQ1_ARATH
ID PSBQ1_ARATH Reviewed; 224 AA.
AC Q9XFT3; O49568; Q2V3G5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Oxygen-evolving enhancer protein 3-1, chloroplastic;
DE Short=OEE3;
DE AltName: Full=16 kDa subunit of oxygen evolving system of photosystem II;
DE AltName: Full=OEC 16 kDa subunit;
DE Flags: Precursor;
GN Name=PSBQ1; Synonyms=PSBQ, PSBQA; OrderedLocusNames=At4g21280;
GN ORFNames=F7J7.220, T6K22.20;
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 [GENOMIC DNA], AND INDUCTION BY LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=10470848; DOI=10.1093/dnares/6.3.173;
RA Grover M., Gaur T., Kochhar A., Maheshwari S.C., Tyagi A.K.;
RT "Nucleotide sequence of psbQ gene for 16-kDa protein of oxygen-evolving
RT complex from Arabidopsis thaliana and regulation of its expression.";
RL DNA Res. 6:173-177(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 76-89, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [7]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11826309; DOI=10.1105/tpc.010304;
RA Peltier J.-B., Emanuelsson O., Kalume D.E., Ytterberg J., Friso G.,
RA Rudella A., Liberles D.A., Soederberg L., Roepstorff P., von Heijne G.,
RA van Wijk K.J.;
RT "Central functions of the lumenal and peripheral thylakoid proteome of
RT Arabidopsis determined by experimentation and genome-wide prediction.";
RL Plant Cell 14:211-236(2002).
RN [8]
RP TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=15198198; DOI=10.1023/b:trag.0000026050.23122.29;
RA Gaur T., Tyagi A.K.;
RT "Analysis of Arabidopsis PsbQA gene expression in transgenic tobacco
RT reveals differential role of its promoter and transcribed region in organ-
RT specific and light-mediated regulation.";
RL Transgenic Res. 13:97-108(2004).
RN [9]
RP FUNCTION.
RX PubMed=16822865; DOI=10.1074/jbc.m603582200;
RA Yi X., Hargett S.R., Frankel L.K., Bricker T.M.;
RT "The PsbQ protein is required in Arabidopsis for photosystem II
RT assembly/stability and photoautotrophy under low light conditions.";
RL J. Biol. Chem. 281:26260-26267(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189; TYR-209 AND THR-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
CC -!- FUNCTION: Required for photosystem II assembly/stability and
CC photoautotrophic growth under low light conditions.
CC {ECO:0000269|PubMed:16822865}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11719511}; Lumenal side
CC {ECO:0000269|PubMed:11719511}. Note=Associated with the photosystem II
CC complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XFT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XFT3-2; Sequence=VSP_034388;
CC -!- TISSUE SPECIFICITY: Expressed in green tissue, with high steady-state
CC mRNA levels in leaves. Not expressed in roots.
CC {ECO:0000269|PubMed:15198198}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:10470848,
CC ECO:0000269|PubMed:15198198}.
CC -!- SIMILARITY: Belongs to the psbQ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40384.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y16847; CAB40384.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL021960; CAA17547.1; -; Genomic_DNA.
DR EMBL; AL031187; CAA20194.1; -; Genomic_DNA.
DR EMBL; AL161554; CAB79128.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84435.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84436.1; -; Genomic_DNA.
DR EMBL; AY050328; AAK91345.1; -; mRNA.
DR EMBL; AY094048; AAM16204.1; -; mRNA.
DR EMBL; AY088330; AAM65869.1; -; mRNA.
DR PIR; T04959; T04959.
DR RefSeq; NP_001031687.1; NM_001036610.1. [Q9XFT3-1]
DR RefSeq; NP_193860.1; NM_118247.3. [Q9XFT3-2]
DR AlphaFoldDB; Q9XFT3; -.
DR SMR; Q9XFT3; -.
DR BioGRID; 13168; 1.
DR STRING; 3702.AT4G21280.2; -.
DR TCDB; 3.E.2.2.3; the photosynthetic reaction center (prc) family.
DR iPTMnet; Q9XFT3; -.
DR SWISS-2DPAGE; Q9XFT3; -.
DR PaxDb; Q9XFT3; -.
DR PRIDE; Q9XFT3; -.
DR ProteomicsDB; 226418; -. [Q9XFT3-1]
DR EnsemblPlants; AT4G21280.1; AT4G21280.1; AT4G21280. [Q9XFT3-2]
DR EnsemblPlants; AT4G21280.2; AT4G21280.2; AT4G21280. [Q9XFT3-1]
DR GeneID; 827877; -.
DR Gramene; AT4G21280.1; AT4G21280.1; AT4G21280. [Q9XFT3-2]
DR Gramene; AT4G21280.2; AT4G21280.2; AT4G21280. [Q9XFT3-1]
DR KEGG; ath:AT4G21280; -.
DR Araport; AT4G21280; -.
DR TAIR; locus:2127393; AT4G21280.
DR eggNOG; ENOG502QQF9; Eukaryota.
DR HOGENOM; CLU_085524_0_0_1; -.
DR InParanoid; Q9XFT3; -.
DR OMA; KKAWPFV; -.
DR OrthoDB; 1248380at2759; -.
DR PhylomeDB; Q9XFT3; -.
DR BioCyc; MetaCyc:AT4G21280-MON; -.
DR PRO; PR:Q9XFT3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XFT3; baseline and differential.
DR Genevisible; Q9XFT3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro.
DR GO; GO:0009654; C:photosystem II oxygen evolving complex; IEA:InterPro.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IBA:GO_Central.
DR Gene3D; 1.20.120.290; -; 1.
DR InterPro; IPR023222; PsbQ-like_dom_sf.
DR InterPro; IPR008797; PSII_PsbQ.
DR PANTHER; PTHR33399; PTHR33399; 1.
DR Pfam; PF05757; PsbQ; 1.
DR SUPFAM; SSF101112; SSF101112; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Direct protein sequencing; Membrane;
KW Phosphoprotein; Photosynthesis; Photosystem II; Plastid;
KW Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 45..75
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511,
FT ECO:0000269|PubMed:11826309"
FT CHAIN 76..224
FT /note="Oxygen-evolving enhancer protein 3-1, chloroplastic"
FT /id="PRO_0000029589"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 209
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT VAR_SEQ 94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172, ECO:0000303|Ref.5"
FT /id="VSP_034388"
SQ SEQUENCE 224 AA; 23866 MW; 3FBD68B52BB40462 CRC64;
MASMGGLHGA SPAVLEGSLK INGSSRLNGS GRVAVAQRSR LVVRAQQSEE TSRRSVIGLV
AAGLAGGSFV QAVLADAISI KVGPPPAPSG GLPAGTDNSD QARDFALALK DRFYLQPLPP
TEAAARAKES AKDIINVKPL IDRKAWPYVQ NDLRSKASYL RYDLNTIISS KPKDEKKSLK
DLTTKLFDTI DNLDYAAKKK SPSQAEKYYA ETVSALNEVL AKLG
