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Cytochrome b6-f complex iron-sulfur subunit, chloroplastic (EC 1.10.9.1) (Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein) (Proton gradient regulation protein 1) (Rieske iron-sulfur protein) (ISP) (RISP)

 UCRIA_ARATH             Reviewed;         229 AA.
Q9ZR03; Q94EI4; Q9FYB6;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-APR-2018, entry version 147.
RecName: Full=Cytochrome b6-f complex iron-sulfur subunit, chloroplastic;
EC=1.10.9.1;
AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein;
AltName: Full=Proton gradient regulation protein 1;
AltName: Full=Rieske iron-sulfur protein;
Short=ISP;
Short=RISP;
Flags: Precursor;
Name=petC; Synonyms=PGR1; OrderedLocusNames=At4g03280;
ORFNames=F4C21.21;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=cv. Landsberg erecta;
PubMed=12040099; DOI=10.1093/pcp/pcf062;
Knight J.S., Duckett C.M., Sullivan J.A., Walker A.R., Gray J.C.;
"Tissue-specific, light-regulated and plastid-regulated expression of
the single-copy nuclear gene encoding the chloroplast Rieske FeS
protein of Arabidopsis thaliana.";
Plant Cell Physiol. 43:522-531(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
Legen J., Misera S., Herrmann R.G., Altschmied L.;
"Sequences and map position of 31 Arabidopsis thaliana cDNAs encoding
organellar polypeptides.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION, AND MUTAGENESIS OF PRO-194.
PubMed=11722777; DOI=10.1046/j.1365-313X.2001.01178.x;
Munekage Y., Takeda S., Endo T., Jahns P., Hashimoto T., Shikanai T.;
"Cytochrome b6/f mutation specifically affects thermal dissipation of
absorbed light energy in Arabidopsis.";
Plant J. 28:351-359(2001).
[7]
FUNCTION, INDUCTION, AND MUTAGENESIS OF PRO-194.
PubMed=12023025; DOI=10.1016/S0014-5793(02)02719-9;
Jahns P., Graf M., Munekage Y., Shikanai T.;
"Single point mutation in the Rieske iron-sulfur subunit of cytochrome
b6/f leads to an altered pH dependence of plastoquinol oxidation in
Arabidopsis.";
FEBS Lett. 519:99-102(2002).
[8]
FUNCTION.
PubMed=12970486; DOI=10.1104/pp.103.024190;
Maiwald D., Dietzmann A., Jahns P., Pesaresi P., Joliot P., Joliot A.,
Levin J.Z., Salamini F., Leister D.;
"Knock-out of the genes coding for the Rieske protein and the ATP-
synthase delta-subunit of Arabidopsis. Effects on photosynthesis,
thylakoid protein composition, and nuclear chloroplast gene
expression.";
Plant Physiol. 133:191-202(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22092075; DOI=10.1021/pr200917t;
Aryal U.K., Krochko J.E., Ross A.R.;
"Identification of phosphoproteins in Arabidopsis thaliana leaves
using polyethylene glycol fractionation, immobilized metal-ion
affinity chromatography, two-dimensional gel electrophoresis and mass
spectrometry.";
J. Proteome Res. 11:425-437(2012).
[10]
INTERACTION WITH PGRL1A.
PubMed=23290914; DOI=10.1016/j.molcel.2012.11.030;
Hertle A.P., Blunder T., Wunder T., Pesaresi P., Pribil M.,
Armbruster U., Leister D.;
"PGRL1 is the elusive ferredoxin-plastoquinone reductase in
photosynthetic cyclic electron flow.";
Mol. Cell 49:511-523(2013).
-!- FUNCTION: Essential protein for photoautotrophism. Confers
resistance to photo-oxidative damages by contributing to the
thermal dissipation of light energy and to lumenal acidification
(increase of pH gradient). Component of the cytochrome b6-f
complex, which mediates electron transfer between photosystem II
(PSII) and photosystem I (PSI), cyclic electron flow around PSI,
and state transitions (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11722777, ECO:0000269|PubMed:12023025,
ECO:0000269|PubMed:12970486}.
-!- CATALYTIC ACTIVITY: Plastoquinol + 2 oxidized plastocyanin + 2
H(+)(Side 1) = plastoquinone + 2 reduced plastocyanin + 4
H(+)(Side 2).
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
-!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f
and the Rieske protein, while the 4 small subunits are petG, petL,
petM and petN. The complex functions as a dimer (By similarity).
Interacts with PGRL1A. {ECO:0000250, ECO:0000269|PubMed:23290914}.
-!- INTERACTION:
Q9SCY3:PNSL4; NbExp=3; IntAct=EBI-2436968, EBI-2436954;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Note=The transmembrane helix obliquely spans the membrane in one
monomer, and its extrinsic C-terminal domain is part of the other
monomer. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9ZR03-1; Sequence=Displayed;
Name=2;
IsoId=Q9ZR03-2; Sequence=VSP_015096;
Note=May be due to an intron retention. No experimental
confirmation available.;
-!- TISSUE SPECIFICITY: Confined to photosynthetic tissues, with
highest levels in flowers. In leaves, mostly localized in
mesophyll cells. In stems, confined to the peripheral ring of
chlorenchyma and adjoining groups of cells associated with the
vascular bundles. In siliques, present in green wall of the fruit
and in peduncle but not in the translucide white septum of the
seeds. {ECO:0000269|PubMed:12040099}.
-!- INDUCTION: Light-dependent expression. Inhibited by acidification
of thylakoids (below pH 5), sucrose and norflurazon (caroteonid
synthesis inhibitor leading to photobleaching).
{ECO:0000269|PubMed:12023025, ECO:0000269|PubMed:12040099}.
-!- MISCELLANEOUS: This protein is 1 of 2 subunits of the cytochrome
b6-f complex that are encoded in the nucleus.
-!- MISCELLANEOUS: The Rieske iron-sulfur protein is a high potential
2Fe-2S protein.
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EMBL; AJ292972; CAC03598.1; -; Genomic_DNA.
EMBL; AJ243702; CAB52433.1; -; mRNA.
EMBL; AC005275; AAD14456.1; -; Genomic_DNA.
EMBL; AL161496; CAB77813.1; -; Genomic_DNA.
EMBL; CP002687; AEE82301.1; -; Genomic_DNA.
EMBL; CP002687; AEE82302.1; -; Genomic_DNA.
EMBL; AF370566; AAK49572.1; -; mRNA.
EMBL; AF410296; AAK95282.1; -; mRNA.
EMBL; AY093726; AAM10350.1; -; mRNA.
PIR; F85041; F85041.
PIR; PA0041; PA0041.
RefSeq; NP_192237.1; NM_116566.4. [Q9ZR03-1]
RefSeq; NP_849295.1; NM_178964.2. [Q9ZR03-2]
UniGene; At.486; -.
UniGene; At.67366; -.
ProteinModelPortal; Q9ZR03; -.
SMR; Q9ZR03; -.
BioGrid; 13287; 4.
IntAct; Q9ZR03; 3.
STRING; 3702.AT4G03280.1; -.
TCDB; 3.D.3.5.2; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
iPTMnet; Q9ZR03; -.
PaxDb; Q9ZR03; -.
PRIDE; Q9ZR03; -.
EnsemblPlants; AT4G03280.1; AT4G03280.1; AT4G03280. [Q9ZR03-1]
EnsemblPlants; AT4G03280.2; AT4G03280.2; AT4G03280. [Q9ZR03-2]
GeneID; 827996; -.
Gramene; AT4G03280.1; AT4G03280.1; AT4G03280. [Q9ZR03-1]
Gramene; AT4G03280.2; AT4G03280.2; AT4G03280. [Q9ZR03-2]
KEGG; ath:AT4G03280; -.
Araport; AT4G03280; -.
TAIR; locus:2005534; AT4G03280.
eggNOG; KOG1671; Eukaryota.
eggNOG; COG0723; LUCA.
HOGENOM; HOG000255192; -.
InParanoid; Q9ZR03; -.
KO; K02636; -.
OMA; RSALMAM; -.
OrthoDB; EOG09360NVS; -.
PhylomeDB; Q9ZR03; -.
BioCyc; ARA:AT4G03280-MONOMER; -.
PRO; PR:Q9ZR03; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9ZR03; baseline and differential.
Genevisible; Q9ZR03; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
GO; GO:0009512; C:cytochrome b6f complex; TAS:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046028; F:electron transporter, transferring electrons from cytochrome b6/f complex of photosystem II activity; TAS:TAIR.
GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-EC.
GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
GO; GO:0010196; P:nonphotochemical quenching; IMP:TAIR.
GO; GO:0009767; P:photosynthetic electron transport chain; TAS:TAIR.
GO; GO:0080167; P:response to karrikin; IEP:TAIR.
Gene3D; 2.102.10.10; -; 1.
HAMAP; MF_01335; Cytb6_f_Rieske; 1.
InterPro; IPR014909; Cyt_b6-f_cplx_Fe-S_su.
InterPro; IPR023960; Cyt_b6_f_Rieske.
InterPro; IPR017941; Rieske_2Fe-2S.
InterPro; IPR036922; Rieske_2Fe-2S_sf.
InterPro; IPR014349; Rieske_Fe-S_prot.
InterPro; IPR005805; Rieske_Fe-S_prot_C.
PANTHER; PTHR10134; PTHR10134; 1.
PANTHER; PTHR10134:SF5; PTHR10134:SF5; 1.
Pfam; PF08802; CytB6-F_Fe-S; 1.
Pfam; PF00355; Rieske; 1.
PRINTS; PR00162; RIESKE.
SUPFAM; SSF50022; SSF50022; 1.
PROSITE; PS51296; RIESKE; 1.
1: Evidence at protein level;
2Fe-2S; Alternative splicing; Chloroplast; Complete proteome;
Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
Metal-binding; Oxidoreductase; Phosphoprotein; Plastid;
Reference proteome; Thylakoid; Transit peptide; Transmembrane;
Transmembrane helix; Transport.
TRANSIT 1 50 Chloroplast. {ECO:0000255}.
CHAIN 51 229 Cytochrome b6-f complex iron-sulfur
subunit, chloroplastic.
/FTId=PRO_0000030684.
TRANSMEM 68 90 Helical. {ECO:0000255}.
DOMAIN 115 211 Rieske.
COMPBIAS 68 73 Poly-Leu.
COMPBIAS 95 102 Poly-Gly.
METAL 157 157 Iron-sulfur (2Fe-2S). {ECO:0000250}.
METAL 159 159 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000250}.
METAL 175 175 Iron-sulfur (2Fe-2S). {ECO:0000250}.
METAL 178 178 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000250}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000244|PubMed:22092075}.
DISULFID 162 177 {ECO:0000250}.
VAR_SEQ 1 19 Missing (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_015096.
MUTAGEN 194 194 P->L: In pgr1; reduces electron transfer
from cyt b6/f to photosystem I at high
light intensity, and shifts pH-dependent
inactivation of electron transport to
more alkaline pH.
{ECO:0000269|PubMed:11722777,
ECO:0000269|PubMed:12023025}.
CONFLICT 48 48 S -> A (in Ref. 2; CAC03598).
{ECO:0000305}.
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


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