UCRIA_ARATH
ID UCRIA_ARATH Reviewed; 229 AA.
AC Q9ZR03; Q94EI4; Q9FYB6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytochrome b6-f complex iron-sulfur subunit, chloroplastic;
DE EC=7.1.1.6;
DE AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein;
DE AltName: Full=Proton gradient regulation protein 1;
DE AltName: Full=Rieske iron-sulfur protein;
DE Short=ISP;
DE Short=RISP;
DE Flags: Precursor;
GN Name=petC; Synonyms=PGR1; OrderedLocusNames=At4g03280; ORFNames=F4C21.21;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12040099; DOI=10.1093/pcp/pcf062;
RA Knight J.S., Duckett C.M., Sullivan J.A., Walker A.R., Gray J.C.;
RT "Tissue-specific, light-regulated and plastid-regulated expression of the
RT single-copy nuclear gene encoding the chloroplast Rieske FeS protein of
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:522-531(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Legen J., Misera S., Herrmann R.G., Altschmied L.;
RT "Sequences and map position of 31 Arabidopsis thaliana cDNAs encoding
RT organellar polypeptides.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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 [6]
RP FUNCTION, AND MUTAGENESIS OF PRO-194.
RX PubMed=11722777; DOI=10.1046/j.1365-313x.2001.01178.x;
RA Munekage Y., Takeda S., Endo T., Jahns P., Hashimoto T., Shikanai T.;
RT "Cytochrome b6/f mutation specifically affects thermal dissipation of
RT absorbed light energy in Arabidopsis.";
RL Plant J. 28:351-359(2001).
RN [7]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF PRO-194.
RX PubMed=12023025; DOI=10.1016/s0014-5793(02)02719-9;
RA Jahns P., Graf M., Munekage Y., Shikanai T.;
RT "Single point mutation in the Rieske iron-sulfur subunit of cytochrome b6/f
RT leads to an altered pH dependence of plastoquinol oxidation in
RT Arabidopsis.";
RL FEBS Lett. 519:99-102(2002).
RN [8]
RP FUNCTION.
RX PubMed=12970486; DOI=10.1104/pp.103.024190;
RA Maiwald D., Dietzmann A., Jahns P., Pesaresi P., Joliot P., Joliot A.,
RA Levin J.Z., Salamini F., Leister D.;
RT "Knock-out of the genes coding for the Rieske protein and the ATP-synthase
RT delta-subunit of Arabidopsis. Effects on photosynthesis, thylakoid protein
RT composition, and nuclear chloroplast gene expression.";
RL Plant Physiol. 133:191-202(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP 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).
RN [10]
RP INTERACTION WITH PGRL1A.
RX PubMed=23290914; DOI=10.1016/j.molcel.2012.11.030;
RA Hertle A.P., Blunder T., Wunder T., Pesaresi P., Pribil M., Armbruster U.,
RA Leister D.;
RT "PGRL1 is the elusive ferredoxin-plastoquinone reductase in photosynthetic
RT cyclic electron flow.";
RL Mol. Cell 49:511-523(2013).
CC -!- FUNCTION: Essential protein for photoautotrophism. Confers resistance
CC to photo-oxidative damages by contributing to the thermal dissipation
CC of light energy and to lumenal acidification (increase of pH gradient).
CC Component of the cytochrome b6-f complex, which mediates electron
CC transfer between photosystem II (PSII) and photosystem I (PSI), cyclic
CC electron flow around PSI, and state transitions (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11722777, ECO:0000269|PubMed:12023025,
CC ECO:0000269|PubMed:12970486}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] = a
CC plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin];
CC Xref=Rhea:RHEA:22148, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17757, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:62192; EC=7.1.1.6;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and
CC the Rieske protein, while the 4 small subunits are petG, petL, petM and
CC petN. The complex functions as a dimer (By similarity). Interacts with
CC PGRL1A. {ECO:0000250, ECO:0000269|PubMed:23290914}.
CC -!- INTERACTION:
CC Q9ZR03; Q9SCY3: PNSL4; NbExp=3; IntAct=EBI-2436968, EBI-2436954;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The
CC transmembrane helix obliquely spans the membrane in one monomer, and
CC its extrinsic C-terminal domain is part of the other monomer.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZR03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZR03-2; Sequence=VSP_015096;
CC -!- TISSUE SPECIFICITY: Confined to photosynthetic tissues, with highest
CC levels in flowers. In leaves, mostly localized in mesophyll cells. In
CC stems, confined to the peripheral ring of chlorenchyma and adjoining
CC groups of cells associated with the vascular bundles. In siliques,
CC present in green wall of the fruit and in peduncle but not in the
CC translucide white septum of the seeds. {ECO:0000269|PubMed:12040099}.
CC -!- INDUCTION: Light-dependent expression. Inhibited by acidification of
CC thylakoids (below pH 5), sucrose and norflurazon (caroteonid synthesis
CC inhibitor leading to photobleaching). {ECO:0000269|PubMed:12023025,
CC ECO:0000269|PubMed:12040099}.
CC -!- MISCELLANEOUS: This protein is 1 of 2 subunits of the cytochrome b6-f
CC complex that are encoded in the nucleus.
CC -!- MISCELLANEOUS: The Rieske iron-sulfur protein is a high potential 2Fe-
CC 2S protein.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000255|HAMAP-Rule:MF_01335}.
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DR EMBL; AJ292972; CAC03598.1; -; Genomic_DNA.
DR EMBL; AJ243702; CAB52433.1; -; mRNA.
DR EMBL; AC005275; AAD14456.1; -; Genomic_DNA.
DR EMBL; AL161496; CAB77813.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82301.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82302.1; -; Genomic_DNA.
DR EMBL; AF370566; AAK49572.1; -; mRNA.
DR EMBL; AF410296; AAK95282.1; -; mRNA.
DR EMBL; AY093726; AAM10350.1; -; mRNA.
DR PIR; F85041; F85041.
DR PIR; PA0041; PA0041.
DR RefSeq; NP_192237.1; NM_116566.4. [Q9ZR03-1]
DR RefSeq; NP_849295.1; NM_178964.2. [Q9ZR03-2]
DR AlphaFoldDB; Q9ZR03; -.
DR SMR; Q9ZR03; -.
DR BioGRID; 13287; 4.
DR IntAct; Q9ZR03; 3.
DR STRING; 3702.AT4G03280.1; -.
DR TCDB; 3.D.3.5.2; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR iPTMnet; Q9ZR03; -.
DR PaxDb; Q9ZR03; -.
DR PRIDE; Q9ZR03; -.
DR ProteomicsDB; 233038; -. [Q9ZR03-1]
DR EnsemblPlants; AT4G03280.1; AT4G03280.1; AT4G03280. [Q9ZR03-1]
DR EnsemblPlants; AT4G03280.2; AT4G03280.2; AT4G03280. [Q9ZR03-2]
DR GeneID; 827996; -.
DR Gramene; AT4G03280.1; AT4G03280.1; AT4G03280. [Q9ZR03-1]
DR Gramene; AT4G03280.2; AT4G03280.2; AT4G03280. [Q9ZR03-2]
DR KEGG; ath:AT4G03280; -.
DR Araport; AT4G03280; -.
DR TAIR; locus:2005534; AT4G03280.
DR eggNOG; KOG1671; Eukaryota.
DR InParanoid; Q9ZR03; -.
DR OrthoDB; 1361271at2759; -.
DR PhylomeDB; Q9ZR03; -.
DR BioCyc; ARA:AT4G03280-MON; -.
DR PRO; PR:Q9ZR03; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZR03; baseline and differential.
DR Genevisible; Q9ZR03; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0009512; C:cytochrome b6f complex; TAS:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046028; F:electron transporter, transferring electrons from cytochrome b6/f complex of photosystem II activity; TAS:TAIR.
DR GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010196; P:nonphotochemical quenching; IMP:TAIR.
DR GO; GO:0009767; P:photosynthetic electron transport chain; TAS:TAIR.
DR Gene3D; 2.102.10.10; -; 1.
DR HAMAP; MF_01335; Cytb6_f_Rieske; 1.
DR InterPro; IPR023960; Cyt_b6_f_Rieske.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Alternative splicing; Chloroplast; Disulfide bond;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Phosphoprotein; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..229
FT /note="Cytochrome b6-f complex iron-sulfur subunit,
FT chloroplastic"
FT /id="PRO_0000030684"
FT TRANSMEM 68..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 115..211
FT /note="Rieske"
FT BINDING 157
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT DISULFID 162..177
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_015096"
FT MUTAGEN 194
FT /note="P->L: In pgr1; reduces electron transfer from cyt
FT b6/f to photosystem I at high light intensity, and shifts
FT pH-dependent inactivation of electron transport to more
FT alkaline pH."
FT /evidence="ECO:0000269|PubMed:11722777,
FT ECO:0000269|PubMed:12023025"
FT CONFLICT 48
FT /note="S -> A (in Ref. 2; CAC03598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 24366 MW; D79FAE03D85EA2F5 CRC64;
MASSSLSPAT QLGSSRSALM AMSSGLFVKP TKMNHQMVRK EKIGLRISCQ ASSIPADRVP
DMEKRKTLNL LLLGALSLPT GYMLVPYATF FVPPGTGGGG GGTPAKDALG NDVVAAEWLK
THGPGDRTLT QGLKGDPTYL VVENDKTLAT YGINAVCTHL GCVVPWNKAE NKFLCPCHGS
QYNAQGRVVR GPAPLSLALA HADIDEAGKV LFVPWVETDF RTGDAPWWS
