LTO1_ARATH
ID LTO1_ARATH Reviewed; 376 AA.
AC Q8L540; O81807; Q8L9V9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Thiol-disulfide oxidoreductase LTO1 {ECO:0000303|PubMed:22209765};
DE EC=1.17.4.- {ECO:0000305};
DE AltName: Full=Protein LUMEN THIOL OXIDOREDUCTASE 1 {ECO:0000303|PubMed:22209765};
DE AltName: Full=Vitamin K reductase {ECO:0000303|PubMed:20626653};
DE Flags: Precursor;
GN Name=LTO1 {ECO:0000303|PubMed:22209765};
GN Synonyms=VKOR {ECO:0000303|PubMed:20626653};
GN OrderedLocusNames=At4g35760 {ECO:0000312|Araport:AT4G35760};
GN ORFNames=F8D20.270 {ECO:0000312|EMBL:CAA20046.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20626653; DOI=10.1111/j.1365-313x.2010.04305.x;
RA Furt F., Van Oostende C., Widhalm J.R., Dale M.A., Wertz J., Basset G.J.;
RT "A bimodular oxidoreductase mediates the specific reduction of
RT phylloquinone (vitamin K(1)) in chloroplasts.";
RL Plant J. 64:38-46(2010).
RN [6]
RP FUNCTION, INTERACTION WITH PSBO1 AND PSBO2, TOPOLOGY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22209765; DOI=10.1105/tpc.111.089680;
RA Karamoko M., Cline S., Redding K., Ruiz N., Hamel P.P.;
RT "Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is
RT required for the assembly of photosystem II in Arabidopsis.";
RL Plant Cell 23:4462-4475(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF CYS-46;
RP CYS-109; CYS-116; CYS-195; CYS-198; CYS-230; CYS-293; CYS-296; CYS-316 AND
RP CYS-331.
RX PubMed=21781282; DOI=10.1111/j.1742-4658.2011.08265.x;
RA Feng W.K., Wang L., Lu Y., Wang X.Y.;
RT "A protein oxidase catalysing disulfide bond formation is localized to the
RT chloroplast thylakoids.";
RL FEBS J. 278:3419-3430(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23689258; DOI=10.1007/s00299-013-1455-9;
RA Lu Y., Wang H.R., Li H., Cui H.R., Feng Y.G., Wang X.Y.;
RT "A chloroplast membrane protein LTO1/AtVKOR involving in redox regulation
RT and ROS homeostasis.";
RL Plant Cell Rep. 32:1427-1440(2013).
RN [9]
RP FUNCTION, AND INTERACTION WITH TL20.3; HCF164; PETJ; VDE1; EDA3; TL17;
RP FKBP13 AND FKBP20-2.
RX PubMed=25412899; DOI=10.2174/0929866521666141121153138;
RA Lu Y., Du J.J., Yu Z.B., Peng J.J., Xu J.N., Wang X.Y.;
RT "Identification of potential targets for thylakoid oxidoreductase
RT AtVKOR/LTO1 in chloroplasts.";
RL Protein Pept. Lett. 22:219-225(2014).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase catalyzing disulfide bond
CC formation of chloroplast proteins and involved in redox regulation and
CC photosynthetic electron transport. Required for the assembly of
CC photosystem II (PSII) through the formation of disulfide bond in PSBO,
CC a subunit of the PSII oxygen-evolving complex in the thylakoid lumen.
CC Involved in the formation of disulfide bonds in the lumenal protein
CC FKBP13. In vitro, reduces phylloquinone (vitamin K1) and menaquinone
CC (vitamin K2) to their respective quinol. Cannot reduce phylloquinone
CC epoxide to phylloquinone (PubMed:20626653, PubMed:21781282,
CC PubMed:22209765, PubMed:23689258). Plays an important role in
CC regulating the thylakoid lumen redox (PubMed:25412899).
CC {ECO:0000269|PubMed:20626653, ECO:0000269|PubMed:21781282,
CC ECO:0000269|PubMed:22209765, ECO:0000269|PubMed:23689258,
CC ECO:0000269|PubMed:25412899}.
CC -!- SUBUNIT: Interacts with the PSII subunits PSBO1 and PSBO2
CC (PubMed:22209765). Interacts with TL17, TL20.3, HCF164, PETJ, VDE1,
CC EDA3, FKBP13 and FKBP20-2 (PubMed:25412899).
CC {ECO:0000269|PubMed:22209765, ECO:0000269|PubMed:25412899}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000305|PubMed:20626653, ECO:0000305|PubMed:21781282}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:20626653,
CC ECO:0000305|PubMed:21781282}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, rosette leaves, stems,
CC cauline leaves and flowers. {ECO:0000269|PubMed:20626653}.
CC -!- DOMAIN: Cysteine residues from the thioredoxin-like domain participate
CC in a series of disulfide-exchange reactions that regenerate the redox-
CC active cysteine residues in the transmembrane domain.
CC {ECO:0000250|UniProtKB:Q2JJF6}.
CC -!- DISRUPTION PHENOTYPE: Severe growth defects due to a limitation in the
CC electron flow from PSII. {ECO:0000269|PubMed:22209765,
CC ECO:0000269|PubMed:23689258}.
CC -!- SIMILARITY: Belongs to the VKOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65737.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA20046.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81485.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL031135; CAA20046.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161588; CAB81485.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86559.1; -; Genomic_DNA.
DR EMBL; AY099728; AAM20579.1; -; mRNA.
DR EMBL; AY128903; AAM91303.1; -; mRNA.
DR EMBL; AY088194; AAM65737.1; ALT_INIT; mRNA.
DR PIR; T04681; T04681.
DR RefSeq; NP_567988.1; NM_119742.4.
DR AlphaFoldDB; Q8L540; -.
DR SMR; Q8L540; -.
DR BioGRID; 15011; 10.
DR IntAct; Q8L540; 1.
DR MINT; Q8L540; -.
DR STRING; 3702.AT4G35760.1; -.
DR PaxDb; Q8L540; -.
DR PRIDE; Q8L540; -.
DR ProteomicsDB; 238805; -.
DR EnsemblPlants; AT4G35760.1; AT4G35760.1; AT4G35760.
DR GeneID; 829729; -.
DR Gramene; AT4G35760.1; AT4G35760.1; AT4G35760.
DR KEGG; ath:AT4G35760; -.
DR Araport; AT4G35760; -.
DR TAIR; locus:2128028; AT4G35760.
DR eggNOG; ENOG502QRER; Eukaryota.
DR HOGENOM; CLU_047345_1_0_1; -.
DR InParanoid; Q8L540; -.
DR OMA; WCPHCHE; -.
DR PhylomeDB; Q8L540; -.
DR PRO; PR:Q8L540; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L540; baseline and differential.
DR Genevisible; Q8L540; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:TAIR.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0010207; P:photosystem II assembly; IMP:TAIR.
DR CDD; cd12916; VKOR_1; 1.
DR Gene3D; 1.20.1440.130; -; 1.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR012932; VKOR.
DR InterPro; IPR044698; VKOR/LTO1.
DR InterPro; IPR038354; VKOR_sf.
DR Pfam; PF07884; VKOR; 1.
DR SMART; SM00756; VKc; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Disulfide bond; Membrane; Oxidoreductase; Plastid; Quinone;
KW Redox-active center; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..376
FT /note="Thiol-disulfide oxidoreductase LTO1"
FT /id="PRO_0000428663"
FT TOPO_DOM 46..81
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..125
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..165
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..192
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..223
FT /note="Stromal"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 44..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 109..116
FT /note="Redox-active"
FT /evidence="ECO:0000255"
FT DISULFID 195..198
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q2JJF6"
FT DISULFID 293..296
FT /note="Redox-active"
FT /evidence="ECO:0000255"
FT DISULFID 316..331
FT /note="Redox-active"
FT /evidence="ECO:0000255"
FT MUTAGEN 46
FT /note="C->A: No effect on catalysis of disulfide bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 109
FT /note="C->A: Loss of function in catalyzing disulfide
FT bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 116
FT /note="C->A: Loss of function in catalyzing disulfide
FT bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 195
FT /note="C->A: Loss of function in catalyzing disulfide
FT bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 198
FT /note="C->A: Loss of function in catalyzing disulfide
FT bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 230
FT /note="C->A: No effect on catalysis of disulfide bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 293
FT /note="C->A: Loss of function in catalyzing disulfide
FT bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 296
FT /note="C->A: Loss of function in catalyzing disulfide
FT bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 316
FT /note="C->A: Loss of function in catalyzing disulfide
FT bond."
FT /evidence="ECO:0000269|PubMed:21781282"
FT MUTAGEN 331
FT /note="C->A: Loss of function in catalyzing disulfide
FT bond."
FT /evidence="ECO:0000269|PubMed:21781282"
SQ SEQUENCE 376 AA; 40401 MW; 21D60947ADCB6D95 CRC64;
MMARFVSVSS CQFHFGFREV SPPSVTSYPR RFEVSDRRFP AIPIKCSSSE PENGEDSAPS
LSSSSSSSTS EVSTSNSSTY NWYTGIGGIG MLDTAYLTYL KVTGSDAFCP IGGGTCGDVL
NSDYAVVFGV PLPVIGFVMY GVVTALSAEL GEGNLPFGIS KSNGRFALFG ITTAMASASA
YFLYILSTKL SGSSCLYCLV SAFLSFSLFF LSVKDVKLQE IQQVVGLQIC LAIIVVASLT
ASYSTAQPIP SRSGDIELPY FRTEISSSSS PYAIALAKHL NSIGAKMYGA FWCSHCLEQK
EMFGREAAKE LNYVECFPDG YKKGTKILKA CADAAIEGFP TWIINDKVLS GEIELAELAE
MTGFSLDQAN ETNQLQ
