CITRX_ARATH
ID CITRX_ARATH Reviewed; 183 AA.
AC Q9M7X9; C0Z2V5; Q8LFA3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Thioredoxin-like protein CITRX, chloroplastic {ECO:0000305};
DE EC=1.8.-.- {ECO:0000269|PubMed:20511297};
DE AltName: Full=Cf-9-interacting thioredoxin {ECO:0000303|PubMed:15131698};
DE Short=AtCiTrx {ECO:0000303|PubMed:15131698};
DE AltName: Full=PEP-associated protein 10 {ECO:0000303|PubMed:21949211};
DE AltName: Full=Thioredoxin Trx p {ECO:0000303|PubMed:20133584};
DE AltName: Full=Thioredoxin Z {ECO:0000303|PubMed:20511297};
DE Flags: Precursor;
GN Name=CITRX {ECO:0000303|PubMed:19825616};
GN Synonyms=PAP10 {ECO:0000303|PubMed:21949211},
GN TRX P {ECO:0000303|PubMed:20133584}, TRX Z {ECO:0000303|PubMed:20511297};
GN OrderedLocusNames=At3g06730 {ECO:0000312|Araport:AT3G06730};
GN ORFNames=F3E22.13 {ECO:0000312|EMBL:AAF63825.1};
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=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 [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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 RETRACTED PAPER.
RX PubMed=15131698; DOI=10.1038/sj.emboj.7600224;
RA Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H.,
RA Jones J.D.;
RT "CITRX thioredoxin interacts with the tomato Cf-9 resistance protein and
RT negatively regulates defence.";
RL EMBO J. 23:2156-2165(2004).
RN [7]
RP RETRACTION NOTICE OF PUBMED:15131698.
RX PubMed=31310343; DOI=10.15252/embj.2019102435;
RA Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H.,
RA Jones J.D.;
RL EMBO J. 38:e102435-e102435(2019).
RN [8]
RP FUNCTION.
RX PubMed=16326926; DOI=10.1105/tpc.105.036392;
RA Pfalz J., Liere K., Kandlbinder A., Dietz K.-J., Oelmueller R.;
RT "pTAC2, -6, and -12 are components of the transcriptionally active plastid
RT chromosome that are required for plastid gene expression.";
RL Plant Cell 18:176-197(2006).
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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH FLN1
RP AND FLN2, AND MUTAGENESIS OF CYS-106 AND CYS-109.
RX PubMed=20511297; DOI=10.1105/tpc.109.071001;
RA Arsova B., Hoja U., Wimmelbacher M., Greiner E., Ustun S., Melzer M.,
RA Petersen K., Lein W., Bornke F.;
RT "Plastidial thioredoxin z interacts with two fructokinase-like proteins in
RT a thiol-dependent manner: evidence for an essential role in chloroplast
RT development in Arabidopsis and Nicotiana benthamiana.";
RL Plant Cell 22:1498-1515(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20133584; DOI=10.1073/pnas.0913759107;
RA Meng L., Wong J.H., Feldman L.J., Lemaux P.G., Buchanan B.B.;
RT "A membrane-associated thioredoxin required for plant growth moves from
RT cell to cell, suggestive of a role in intercellular communication.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3900-3905(2010).
RN [12]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21949211; DOI=10.1104/pp.111.184515;
RA Steiner S., Schroeter Y., Pfalz J., Pfannschmidt T.;
RT "Identification of essential subunits in the plastid-encoded RNA polymerase
RT complex reveals building blocks for proper plastid development.";
RL Plant Physiol. 157:1043-1055(2011).
RN [13]
RP INTERACTION WITH MRL7.
RX PubMed=23956074; DOI=10.1093/mp/sst092;
RA Yua Q.B., Ma Q., Kong M.M., Zhao T.T., Zhang X.L., Zhou Q., Huang C.,
RA Chong K., Yang Z.N.;
RT "AtECB1/MRL7, a thioredoxin-like fold protein with disulfide reductase
RT activity, regulates chloroplast gene expression and chloroplast biogenesis
RT in Arabidopsis thaliana.";
RL Mol. Plant 7:206-217(2014).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase that plays a role in proper
CC chloroplast development, most likely through regulating plastid-encoded
CC polymerase (PEP) dependent chloroplast transcription. Acts as a
CC component of the transcriptionally active plastid chromosome that is
CC required for plastid gene expression. {ECO:0000269|PubMed:16326926,
CC ECO:0000269|PubMed:20133584, ECO:0000269|PubMed:20511297,
CC ECO:0000269|PubMed:21949211}.
CC -!- SUBUNIT: Interacts with FLN1 and FLN2 (PubMed:20511297). Interacts with
CC MRL7 (PubMed:23956074). {ECO:0000269|PubMed:20511297,
CC ECO:0000269|PubMed:23956074}.
CC -!- INTERACTION:
CC Q9M7X9; Q9M394: FLN1; NbExp=3; IntAct=EBI-9823626, EBI-9823647;
CC Q9M7X9; F4I0K2: FLN2; NbExp=3; IntAct=EBI-9823626, EBI-9823671;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:20133584, ECO:0000269|PubMed:20511297}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M7X9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M7X9-2; Sequence=VSP_039287, VSP_039288;
CC -!- DISRUPTION PHENOTYPE: Albino seedlings leading to lethality. Abnormal
CC plastids lacking internal membrane structures.
CC {ECO:0000269|PubMed:20133584, ECO:0000269|PubMed:20511297}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant CITRX-type
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: The article has been retracted, because it has become clear
CC that the thioredoxin that interacts in yeast 2-hybrid with the Cf-9 C-
CC terminus is in fact localized in the chloroplast, rendering a role in
CC Cf-9 signaling unlikely. All the authors agree that this paper should
CC be withdrawn from the scientific literature.
CC {ECO:0000305|PubMed:31310343}.
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DR EMBL; AC023912; AAF63825.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74449.1; -; Genomic_DNA.
DR EMBL; AF370315; AAK44130.1; -; mRNA.
DR EMBL; AY063100; AAL34274.1; -; mRNA.
DR EMBL; AK318919; BAH57034.1; -; mRNA.
DR EMBL; AY084959; AAM61520.1; -; mRNA.
DR RefSeq; NP_187329.1; NM_111553.4. [Q9M7X9-1]
DR AlphaFoldDB; Q9M7X9; -.
DR SMR; Q9M7X9; -.
DR BioGRID; 5193; 10.
DR IntAct; Q9M7X9; 2.
DR STRING; 3702.AT3G06730.1; -.
DR PaxDb; Q9M7X9; -.
DR PRIDE; Q9M7X9; -.
DR ProteomicsDB; 246867; -. [Q9M7X9-1]
DR EnsemblPlants; AT3G06730.1; AT3G06730.1; AT3G06730. [Q9M7X9-1]
DR GeneID; 819858; -.
DR Gramene; AT3G06730.1; AT3G06730.1; AT3G06730. [Q9M7X9-1]
DR KEGG; ath:AT3G06730; -.
DR Araport; AT3G06730; -.
DR TAIR; locus:2083398; AT3G06730.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_110012_1_0_1; -.
DR InParanoid; Q9M7X9; -.
DR OMA; PLQMMRD; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q9M7X9; -.
DR PRO; PR:Q9M7X9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M7X9; baseline and differential.
DR Genevisible; Q9M7X9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IDA:TAIR.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:TAIR.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:TAIR.
DR GO; GO:0009657; P:plastid organization; IMP:TAIR.
DR InterPro; IPR044182; CITRX.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR47834; PTHR47834; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Disulfide bond; Electron transport;
KW Oxidoreductase; Plastid; Redox-active center; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..81
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 82..183
FT /note="Thioredoxin-like protein CITRX, chloroplastic"
FT /id="PRO_0000394545"
FT DOMAIN 82..183
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 100
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 107
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 108
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT DISULFID 106..109
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 147..170
FT /note="RGLPTLFFISPDPSKDAIRTEGLI -> YCNLQLMFLNFMNLLSAYQCKFLH
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039287"
FT VAR_SEQ 171..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039288"
FT MUTAGEN 106
FT /note="C->S: Strongly reduces the interaction with FLN1 or
FT FLN2."
FT /evidence="ECO:0000269|PubMed:20511297"
FT MUTAGEN 109
FT /note="C->S: Does not affect the interaction with FLN1 or
FT FLN2."
FT /evidence="ECO:0000269|PubMed:20511297"
FT CONFLICT 9
FT /note="F -> L (in Ref. 5; AAM61520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 20670 MW; 1A1152A76B5DE8D7 CRC64;
MALVQSRTFP HLNTPLSPIL SSLHAPSSLF IRREIRPVAA PFSSSTAGNL PFSPLTRPRK
LLCPPPRGKF VREDYLVKKL SAQELQELVK GDRKVPLIVD FYATWCGPCI LMAQELEMLA
VEYESNAIIV KVDTDDEYEF ARDMQVRGLP TLFFISPDPS KDAIRTEGLI PLQMMHDIID
NEM
