PGL1B_ARATH
ID PGL1B_ARATH Reviewed; 313 AA.
AC Q8GYC7; Q9SZ61;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=PGR5-like protein 1B, chloroplastic;
DE AltName: Full=Ferredoxin-plastoquinone reductase 2;
DE Flags: Precursor;
GN Name=PGRL1B; OrderedLocusNames=At4g11960; ORFNames=F16J13.30;
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=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 [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, SUBCELLULAR LOCATION, INTERACTION WITH PGR5, FD2, PASD1, LFNR1
RP AND LFNR2, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18243102; DOI=10.1016/j.cell.2007.12.028;
RA DalCorso G., Pesaresi P., Masiero S., Aseeva E., Schuenemann D.,
RA Finazzi G., Joliot P., Barbato R., Leister D.;
RT "A complex containing PGRL1 and PGR5 is involved in the switch between
RT linear and cyclic electron flow in Arabidopsis.";
RL Cell 132:273-285(2008).
RN [6]
RP INDUCTION BY DROUGHT.
RX PubMed=20392519; DOI=10.1016/j.jplph.2010.02.006;
RA Lehtimaeki N., Lintala M., Allahverdiyeva Y., Aro E.M., Mulo P.;
RT "Drought stress-induced upregulation of components involved in ferredoxin-
RT dependent cyclic electron transfer.";
RL J. Plant Physiol. 167:1018-1022(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-50, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER LYS-49, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP FUNCTION.
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: Ferredoxin-plastoquinone reductase involved in cyclic
CC electron flow (CEF) around photosystem I. The homodimer is probably not
CC involved in CEF. {ECO:0000269|PubMed:18243102,
CC ECO:0000269|PubMed:23290914}.
CC -!- ACTIVITY REGULATION: Inhibited by antimycin A. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and heterodimer with PGR5 (Probable). Interacts with
CC PGR5, FD2, psaD1, LFNR1 and LFNR2. Interacts also with petC and a Fe-
CC containing cofactor (FCC) (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18243102}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18243102}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8GYC7-1; Sequence=Displayed;
CC -!- INDUCTION: Up-regulated by drought stress.
CC {ECO:0000269|PubMed:20392519}.
CC -!- DOMAIN: The C-terminal loop (247-313) is required for ferredoxin
CC binding.
CC -!- PTM: Disulfide bonds; Cys-289 and Cys-292 are probably involved in the
CC formation of disulfide bridges with 'Cys-11' and 'Cys-105' of PGR5
CC while Cys-261 and Cys-264 are probably involved in the binding of a Fe-
CC containing cofactor (FCC). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC PGRL1A. Pgrl1a and pgrl1b double mutant grows slowly and has pale green
CC leaves. {ECO:0000269|PubMed:18243102}.
CC -!- MISCELLANEOUS: Thioredoxins prevent homodimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PGR5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78239.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049638; CAB40937.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161533; CAB78239.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83074.1; -; Genomic_DNA.
DR EMBL; AK117721; BAC42372.1; -; mRNA.
DR EMBL; BT005305; AAO63369.1; -; mRNA.
DR PIR; T06603; T06603.
DR RefSeq; NP_192933.2; NM_117266.4. [Q8GYC7-1]
DR AlphaFoldDB; Q8GYC7; -.
DR BioGRID; 12101; 14.
DR IntAct; Q8GYC7; 2.
DR STRING; 3702.AT4G11960.1; -.
DR iPTMnet; Q8GYC7; -.
DR PaxDb; Q8GYC7; -.
DR PRIDE; Q8GYC7; -.
DR ProteomicsDB; 234717; -. [Q8GYC7-1]
DR EnsemblPlants; AT4G11960.1; AT4G11960.1; AT4G11960. [Q8GYC7-1]
DR GeneID; 826803; -.
DR Gramene; AT4G11960.1; AT4G11960.1; AT4G11960. [Q8GYC7-1]
DR KEGG; ath:AT4G11960; -.
DR Araport; AT4G11960; -.
DR TAIR; locus:2118031; AT4G11960.
DR eggNOG; ENOG502S909; Eukaryota.
DR InParanoid; Q8GYC7; -.
DR OrthoDB; 1439465at2759; -.
DR PhylomeDB; Q8GYC7; -.
DR PRO; PR:Q8GYC7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GYC7; baseline and differential.
DR Genevisible; Q8GYC7; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IBA:GO_Central.
DR GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IBA:GO_Central.
DR InterPro; IPR039987; PGRL1.
DR PANTHER; PTHR31032; PTHR31032; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chloroplast; Disulfide bond;
KW Electron transport; Membrane; Plastid; Reference proteome; Thylakoid;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000305, ECO:0007744|PubMed:22223895"
FT CHAIN 50..313
FT /note="PGR5-like protein 1B, chloroplastic"
FT /id="PRO_0000322593"
FT TOPO_DOM 50..187
FT /note="Stromal"
FT TRANSMEM 188..208
FT /note="Helical; Name=1"
FT TOPO_DOM 209..225
FT /note="Lumenal, thylakoid"
FT TRANSMEM 226..246
FT /note="Helical; Name=2"
FT TOPO_DOM 247..313
FT /note="Stromal"
FT MOD_RES 50
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 71..172
FT /note="In monomeric form"
FT DISULFID 71
FT /note="Interchain (with C-172); in homodimeric form"
FT DISULFID 172
FT /note="Interchain (with C-71); in homodimeric form"
SQ SEQUENCE 313 AA; 34909 MW; 4548DF438D222650 CRC64;
MAFTLTIPRF SAISRKPITC SSSRTQCPAP FTHGRSISLR RRLTLLPLKA STDQSGQVGG
EEVDSKILPY CSINKNEKRT IGEMEQEFLQ AMQSFYYEGK AIMSNEEFDN LKEELMWEGS
SVVMLSSDEQ RFLEASMAYV SGNPILSDEE YDKLKMKLKM DGSEIVCEGP RCSLRSKKVY
SDLAIDYFKM FLLNVPATVV ALGLFFFLDD ITGFEITYLL ELPEPFSFIF TWFAAVPAIV
YLALSLTKLI LKDFLILKGP CPNCGTENVS FFGTILSIPN DSNTNNVKCS GCGTEMVYDS
GSRLITLPEG GKA
