PGL1A_ARATH
ID PGL1A_ARATH Reviewed; 324 AA.
AC Q8H112; A8MS43; A8MSD4; O82738;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=PGR5-like protein 1A, chloroplastic;
DE AltName: Full=Ferredoxin-plastoquinone reductase 1;
DE Flags: Precursor;
GN Name=PGRL1A; OrderedLocusNames=At4g22890; ORFNames=F7H19.70;
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=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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 FUNCTION, SUBUNIT, INTERACTION WITH PGR5 AND PETC, DISULFIDE BONDS,
RP MUTAGENESIS OF CYS-82; CYS-183; CYS-272; CYS-275; CYS-300 AND CYS-303, AND
RP ACTIVITY REGULATION.
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.
CC {ECO:0000269|PubMed:23290914}.
CC -!- SUBUNIT: Homodimer and heterodimer with PGR5. Interacts with PGR5, FD2,
CC petC, psaD1, LFNR1 and LFNR2. Interacts also with a Fe-containing
CC cofactor (FCC). {ECO:0000269|PubMed:18243102,
CC ECO:0000269|PubMed:23290914}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:18243102}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18243102}. Note=Predominantly located in the
CC appressed regions of the thylakoids and less abundant in the stroma
CC lamellae.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8H112-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H112-2; Sequence=VSP_031964;
CC Name=3;
CC IsoId=Q8H112-3; Sequence=VSP_031963;
CC -!- INDUCTION: Up-regulated by drought stress.
CC {ECO:0000269|PubMed:20392519}.
CC -!- DOMAIN: The C-terminal loop (258-324) is required for ferredoxin
CC binding.
CC -!- PTM: Disulfide bonds; Cys-300 and Cys-303 are probably involved in the
CC formation of disulfide bridges with 'Cys-11' and 'Cys-105' of PGR5
CC while Cys-272 and Cys-275 are probably involved in the binding of a Fe-
CC containing cofactor (FCC).
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC PGRL1B. Pgrl1a and pgrl1b double mutant grows slowly and has pale green
CC leaves. {ECO:0000269|PubMed:18243102}.
CC -!- MISCELLANEOUS: Thioredoxins prevent homodimerization.
CC {ECO:0000305|PubMed:23290914}.
CC -!- SIMILARITY: Belongs to the PGR5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA19804.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79244.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL031018; CAA19804.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161558; CAB79244.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84674.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84675.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84677.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84678.1; -; Genomic_DNA.
DR EMBL; BT000905; AAN41305.1; -; mRNA.
DR PIR; T05120; T05120.
DR RefSeq; NP_001078431.1; NM_001084962.1. [Q8H112-3]
DR RefSeq; NP_001078432.1; NM_001084963.1. [Q8H112-2]
DR RefSeq; NP_567672.1; NM_118418.4. [Q8H112-1]
DR RefSeq; NP_849423.1; NM_179092.1. [Q8H112-1]
DR AlphaFoldDB; Q8H112; -.
DR BioGRID; 13677; 25.
DR IntAct; Q8H112; 18.
DR MINT; Q8H112; -.
DR STRING; 3702.AT4G22890.1; -.
DR iPTMnet; Q8H112; -.
DR PaxDb; Q8H112; -.
DR PRIDE; Q8H112; -.
DR ProteomicsDB; 235051; -. [Q8H112-1]
DR EnsemblPlants; AT4G22890.1; AT4G22890.1; AT4G22890. [Q8H112-1]
DR EnsemblPlants; AT4G22890.3; AT4G22890.3; AT4G22890. [Q8H112-1]
DR EnsemblPlants; AT4G22890.4; AT4G22890.4; AT4G22890. [Q8H112-3]
DR EnsemblPlants; AT4G22890.5; AT4G22890.5; AT4G22890. [Q8H112-2]
DR GeneID; 828388; -.
DR Gramene; AT4G22890.1; AT4G22890.1; AT4G22890. [Q8H112-1]
DR Gramene; AT4G22890.3; AT4G22890.3; AT4G22890. [Q8H112-1]
DR Gramene; AT4G22890.4; AT4G22890.4; AT4G22890. [Q8H112-3]
DR Gramene; AT4G22890.5; AT4G22890.5; AT4G22890. [Q8H112-2]
DR KEGG; ath:AT4G22890; -.
DR Araport; AT4G22890; -.
DR TAIR; locus:2127233; AT4G22890.
DR eggNOG; ENOG502QRSK; Eukaryota.
DR InParanoid; Q8H112; -.
DR OMA; CISCIGC; -.
DR PhylomeDB; Q8H112; -.
DR PRO; PR:Q8H112; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H112; baseline and differential.
DR Genevisible; Q8H112; AT.
DR GO; GO:0009507; C:chloroplast; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IMP:UniProtKB.
DR InterPro; IPR039987; PGRL1.
DR PANTHER; PTHR31032; PTHR31032; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Disulfide bond; Electron transport;
KW Membrane; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..324
FT /note="PGR5-like protein 1A, chloroplastic"
FT /id="PRO_0000322592"
FT TOPO_DOM 61..198
FT /note="Stromal"
FT TRANSMEM 199..219
FT /note="Helical; Name=1"
FT TOPO_DOM 220..236
FT /note="Lumenal, thylakoid"
FT TRANSMEM 237..257
FT /note="Helical; Name=2"
FT TOPO_DOM 258..324
FT /note="Stromal"
FT REGION 16..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 82..183
FT /note="In monomeric form"
FT /evidence="ECO:0000269|PubMed:23290914"
FT DISULFID 82
FT /note="Interchain (with C-183); in homodimeric form"
FT /evidence="ECO:0000269|PubMed:23290914"
FT DISULFID 183
FT /note="Interchain (with C-82); in homodimeric form"
FT /evidence="ECO:0000269|PubMed:23290914"
FT VAR_SEQ 67..69
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_031963"
FT VAR_SEQ 67..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_031964"
FT MUTAGEN 82
FT /note="C->S: Loss of photosynthetic cyclic electron flow,
FT loss of formation of oxidized monomer, and decreased FCC
FT binding and dimer formation with PGR5. Loss of
FT dimerization; when associated with S-183."
FT /evidence="ECO:0000269|PubMed:23290914"
FT MUTAGEN 183
FT /note="C->S: Loss of photosynthetic cyclic electron flow,
FT loss of formation of oxidized monomer, and decreased FCC
FT binding and dimer formation with PGR5. Loss of
FT dimerization; when associated with S-82."
FT /evidence="ECO:0000269|PubMed:23290914"
FT MUTAGEN 272
FT /note="C->S: Loss of photosynthetic cyclic electron flow,
FT loss of FCC binding, but no effect on dimer formation with
FT PGR5; when associated with S-275. Loss of dimer formation
FT with PGR5; when associated with S-275; S-300 and S-303."
FT /evidence="ECO:0000269|PubMed:23290914"
FT MUTAGEN 275
FT /note="C->S: Loss of photosynthetic cyclic electron flow,
FT loss of FCC binding, but no effect on dimer formation with
FT PGR5; when associated with S-272. Loss of dimer formation
FT with PGR5; when associated with S-272; S-300 and S-303."
FT /evidence="ECO:0000269|PubMed:23290914"
FT MUTAGEN 300
FT /note="C->S: Loss of photosynthetic cyclic electron flow.
FT No effect on FCC binding or dimer formation with PGR5; when
FT associated with S-303. Loss of dimer formation with PGR5;
FT when associated with S-272; S-275 and S-303."
FT /evidence="ECO:0000269|PubMed:23290914"
FT MUTAGEN 303
FT /note="C->S: Loss of photosynthetic cyclic electron flow.
FT No effect on FCC binding or dimer formation with PGR5; when
FT associated with S-300. Loss of dimer formation with PGR5;
FT when associated with S-272; S-275 and S-300."
FT /evidence="ECO:0000269|PubMed:23290914"
SQ SEQUENCE 324 AA; 35721 MW; 1031BBF1B049C8B6 CRC64;
MGSKMLFSLT SPRLFSAVSR KPSSSFSPSP PSPSSRTQWT QLSPGKSISL RRRVFLLPAK
ATTEQSGPVG GDNVDSNVLP YCSINKAEKK TIGEMEQEFL QALQSFYYDG KAIMSNEEFD
NLKEELMWEG SSVVMLSSDE QRFLEASMAY VSGNPILNDE EYDKLKLKLK IDGSDIVSEG
PRCSLRSKKV YSDLAVDYFK MLLLNVPATV VALGLFFFLD DITGFEITYI MELPEPYSFI
FTWFAAVPVI VYLALSITKL IIKDFLILKG PCPNCGTENT SFFGTILSIS SGGKTNTVKC
TNCGTAMVYD SGSRLITLPE GSQA
