TRXF1_ARATH
ID TRXF1_ARATH Reviewed; 178 AA.
AC Q9XFH8; Q9M8R5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Thioredoxin F1, chloroplastic;
DE Short=AtTrxf1;
DE AltName: Full=Thioredoxin F2;
DE Short=AtTrxf2;
DE Flags: Precursor;
GN OrderedLocusNames=At3g02730; ORFNames=F13E7.33;
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 [MRNA].
RX PubMed=10498962; DOI=10.1016/s1360-1385(99)01475-2;
RA Meyer Y., Verdoucq L., Vignols F.;
RT "Plant thioredoxins and glutaredoxins: identity and putative roles.";
RL Trends Plant Sci. 4:388-394(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [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 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 [6]
RP FUNCTION, GLUTATHIONYLATION AT CYS-126, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16263928; DOI=10.1073/pnas.0507498102;
RA Michelet L., Zaffagnini M., Marchand C., Collin V., Decottignies P.,
RA Tsan P., Lancelin J.M., Trost P., Miginiac-Maslow M., Noctor G.,
RA Lemaire S.D.;
RT "Glutathionylation of chloroplast thioredoxin f is a redox signaling
RT mechanism in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16478-16483(2005).
RN [7]
RP FUNCTION.
RX PubMed=19631646; DOI=10.1016/j.febslet.2009.07.035;
RA Nee G., Zaffagnini M., Trost P., Issakidis-Bourguet E.;
RT "Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: a new
RT role for f-type thioredoxin.";
RL FEBS Lett. 583:2827-2832(2009).
RN [8]
RP FUNCTION.
RX PubMed=19825612; DOI=10.1093/mp/ssn061;
RA Marri L., Zaffagnini M., Collin V., Issakidis-Bourguet E., Lemaire S.D.,
RA Pupillo P., Sparla F., Miginiac-Maslow M., Trost P.;
RT "Prompt and easy activation by specific thioredoxins of calvin cycle
RT enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK
RT supramolecular complex.";
RL Mol. Plant 2:259-269(2009).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825616; DOI=10.1093/mp/ssn076;
RA Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
RT "Comparative genomic study of the thioredoxin family in photosynthetic
RT organisms with emphasis on Populus trichocarpa.";
RL Mol. Plant 2:308-322(2009).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=19259774; DOI=10.1007/s11103-009-9471-4;
RA Cain P., Hall M., Schroder W.P., Kieselbach T., Robinson C.;
RT "A novel extended family of stromal thioredoxins.";
RL Plant Mol. Biol. 70:273-281(2009).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase involved in the redox
CC regulation of enzymes of both reductive pentose phosphate pathway
CC (Calvin-Benson cycle) and oxidative pentose phosphate pathway. Under
CC light or reducing conditions, activates in chloroplast the
CC glyceraldehyde-3-phosphate dehydrogenase, the phosphoribulokinase and
CC the fructose-1,6-bisphosphate phosphatase, and inhibits the glucose-6-
CC phosphate dehydrogenase. {ECO:0000269|PubMed:16263928,
CC ECO:0000269|PubMed:19631646, ECO:0000269|PubMed:19825612}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19259774}.
CC -!- PTM: Glutathionylation at Cys-126 decreases its ability to be reduced
CC by ferredoxin-thioredoxin reductase and reduces its efficiency in
CC activating target chloroplastic enzymes. {ECO:0000269|PubMed:16263928}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant F-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AF144385; AAD35003.1; -; mRNA.
DR EMBL; AC018363; AAF26987.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73852.1; -; Genomic_DNA.
DR EMBL; AY065391; AAL38832.1; -; mRNA.
DR EMBL; AY096721; AAM20355.1; -; mRNA.
DR EMBL; AY084778; AAM61345.1; -; mRNA.
DR RefSeq; NP_186922.1; NM_111141.3.
DR AlphaFoldDB; Q9XFH8; -.
DR SMR; Q9XFH8; -.
DR BioGRID; 6593; 2.
DR STRING; 3702.AT3G02730.1; -.
DR PaxDb; Q9XFH8; -.
DR PRIDE; Q9XFH8; -.
DR ProteomicsDB; 232451; -.
DR EnsemblPlants; AT3G02730.1; AT3G02730.1; AT3G02730.
DR GeneID; 821260; -.
DR Gramene; AT3G02730.1; AT3G02730.1; AT3G02730.
DR KEGG; ath:AT3G02730; -.
DR Araport; AT3G02730; -.
DR TAIR; locus:2075522; AT3G02730.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_9_0_1; -.
DR InParanoid; Q9XFH8; -.
DR OMA; TTKIGFC; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q9XFH8; -.
DR PRO; PR:Q9XFH8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9XFH8; baseline and differential.
DR Genevisible; Q9XFH8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0045454; P:cell redox homeostasis; IGI:TAIR.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0009642; P:response to light intensity; IGI:TAIR.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Disulfide bond; Electron transport; Glutathionylation;
KW Plastid; Redox-active center; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..178
FT /note="Thioredoxin F1, chloroplastic"
FT /id="PRO_0000034156"
FT DOMAIN 58..174
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 93
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 100
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 101
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 126
FT /note="S-glutathionyl cysteine; transient"
FT /evidence="ECO:0000269|PubMed:16263928"
FT DISULFID 99..102
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 134
FT /note="A -> P (in Ref. 1; AAD35003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 19325 MW; 7B4E6CFE8F2714BD CRC64;
MPLSLRLSPS PTALSPTTGG FGPSRKQCRI PYSGVPTTKI GFCSLDSRKR GDSSVVRCSL
ETVNVSVGQV TEVDKDTFWP IVKAAGEKLV VLDMYTQWCG PCKVIAPKYK ALSEKYDDVV
FLKLDCNPDN RPLAKELGIR VVPTFKILKD NKVVKEVTGA KYDDLVAAIE TARSAASG
