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Thioredoxin-like protein CITRX, chloroplastic (EC 1.8.-.-) (Cf-9-interacting thioredoxin) (AtCiTrx) (PEP-associated protein 10) (Thioredoxin Trx p) (Thioredoxin Z)

 CITRX_ARATH             Reviewed;         183 AA.
Q9M7X9; C0Z2V5; Q8LFA3;
15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 127.
RecName: Full=Thioredoxin-like protein CITRX, chloroplastic {ECO:0000303|PubMed:15131698};
EC=1.8.-.- {ECO:0000269|PubMed:20511297};
AltName: Full=Cf-9-interacting thioredoxin {ECO:0000303|PubMed:15131698};
Short=AtCiTrx {ECO:0000303|PubMed:15131698};
AltName: Full=PEP-associated protein 10 {ECO:0000303|PubMed:21949211};
AltName: Full=Thioredoxin Trx p {ECO:0000303|PubMed:20133584};
AltName: Full=Thioredoxin Z {ECO:0000303|PubMed:20511297};
Flags: Precursor;
Name=CITRX {ECO:0000303|PubMed:19825616};
Synonyms=PAP10 {ECO:0000303|PubMed:21949211},
TRX P {ECO:0000303|PubMed:20133584},
TRX Z {ECO:0000303|PubMed:20511297};
OrderedLocusNames=At3g06730 {ECO:0000312|Araport:AT3G06730};
ORFNames=F3E22.13 {ECO:0000312|EMBL:AAF63825.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15131698; DOI=10.1038/sj.emboj.7600224;
Rivas S., Rougon-Cardoso A., Smoker M., Schauser L., Yoshioka H.,
Jones J.D.;
"CITRX thioredoxin interacts with the tomato Cf-9 resistance protein
and negatively regulates defence.";
EMBO J. 23:2156-2165(2004).
[7]
FUNCTION.
PubMed=16326926; DOI=10.1105/tpc.105.036392;
Pfalz J., Liere K., Kandlbinder A., Dietz K.-J., Oelmueller R.;
"pTAC2, -6, and -12 are components of the transcriptionally active
plastid chromosome that are required for plastid gene expression.";
Plant Cell 18:176-197(2006).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19825616; DOI=10.1093/mp/ssn076;
Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
"Comparative genomic study of the thioredoxin family in photosynthetic
organisms with emphasis on Populus trichocarpa.";
Mol. Plant 2:308-322(2009).
[9]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
FLN1 AND FLN2, AND MUTAGENESIS OF CYS-106 AND CYS-109.
PubMed=20511297; DOI=10.1105/tpc.109.071001;
Arsova B., Hoja U., Wimmelbacher M., Greiner E., Ustun S., Melzer M.,
Petersen K., Lein W., Bornke F.;
"Plastidial thioredoxin z interacts with two fructokinase-like
proteins in a thiol-dependent manner: evidence for an essential role
in chloroplast development in Arabidopsis and Nicotiana benthamiana.";
Plant Cell 22:1498-1515(2010).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=20133584; DOI=10.1073/pnas.0913759107;
Meng L., Wong J.H., Feldman L.J., Lemaux P.G., Buchanan B.B.;
"A membrane-associated thioredoxin required for plant growth moves
from cell to cell, suggestive of a role in intercellular
communication.";
Proc. Natl. Acad. Sci. U.S.A. 107:3900-3905(2010).
[11]
FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=21949211; DOI=10.1104/pp.111.184515;
Steiner S., Schroeter Y., Pfalz J., Pfannschmidt T.;
"Identification of essential subunits in the plastid-encoded RNA
polymerase complex reveals building blocks for proper plastid
development.";
Plant Physiol. 157:1043-1055(2011).
[12]
INTERACTION WITH MRL7.
PubMed=23956074; DOI=10.1093/mp/sst092;
Yua Q.B., Ma Q., Kong M.M., Zhao T.T., Zhang X.L., Zhou Q., Huang C.,
Chong K., Yang Z.N.;
"AtECB1/MRL7, a thioredoxin-like fold protein with disulfide reductase
activity, regulates chloroplast gene expression and chloroplast
biogenesis in Arabidopsis thaliana.";
Mol. Plant 7:206-217(2014).
-!- FUNCTION: Thiol-disulfide oxidoreductase that plays a role in
proper chloroplast development, most likely through regulating
plastid-encoded polymerase (PEP) dependent chloroplast
transcription. Acts as a component of the transcriptionally active
plastid chromosome that is required for plastid gene expression.
May be involved in cell death and defense responses (By
similarity). {ECO:0000250|UniProtKB:Q9LKW0,
ECO:0000269|PubMed:16326926, ECO:0000269|PubMed:20133584,
ECO:0000269|PubMed:20511297, ECO:0000269|PubMed:21949211}.
-!- SUBUNIT: Interacts with FLN1 and FLN2 (PubMed:20511297). Interacts
with MRL7 (PubMed:23956074). {ECO:0000269|PubMed:20511297,
ECO:0000269|PubMed:23956074}.
-!- INTERACTION:
Q9M394:FLN1; NbExp=3; IntAct=EBI-9823626, EBI-9823647;
F4I0K2:FLN2; NbExp=3; IntAct=EBI-9823626, EBI-9823671;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:20133584, ECO:0000269|PubMed:20511297}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9M7X9-1; Sequence=Displayed;
Name=2;
IsoId=Q9M7X9-2; Sequence=VSP_039287, VSP_039288;
Note=May be due to intron retention. No experimental
confirmation available.;
-!- DISRUPTION PHENOTYPE: Albino seedlings leading to lethality.
Abnormal plastids lacking internal membrane structures.
{ECO:0000269|PubMed:20133584, ECO:0000269|PubMed:20511297}.
-!- SIMILARITY: Belongs to the thioredoxin family. Plant CITRX-type
subfamily. {ECO:0000303|PubMed:15131698,
ECO:0000303|PubMed:19825616}.
-----------------------------------------------------------------------
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EMBL; AC023912; AAF63825.1; -; Genomic_DNA.
EMBL; CP002686; AEE74449.1; -; Genomic_DNA.
EMBL; AF370315; AAK44130.1; -; mRNA.
EMBL; AY063100; AAL34274.1; -; mRNA.
EMBL; AK318919; BAH57034.1; -; mRNA.
EMBL; AY084959; AAM61520.1; -; mRNA.
RefSeq; NP_187329.1; NM_111553.4. [Q9M7X9-1]
UniGene; At.18842; -.
ProteinModelPortal; Q9M7X9; -.
SMR; Q9M7X9; -.
BioGrid; 5193; 3.
IntAct; Q9M7X9; 2.
STRING; 3702.AT3G06730.1; -.
PaxDb; Q9M7X9; -.
EnsemblPlants; AT3G06730.1; AT3G06730.1; AT3G06730. [Q9M7X9-1]
GeneID; 819858; -.
Gramene; AT3G06730.1; AT3G06730.1; AT3G06730.
KEGG; ath:AT3G06730; -.
Araport; AT3G06730; -.
TAIR; locus:2083398; AT3G06730.
eggNOG; KOG0907; Eukaryota.
eggNOG; COG0526; LUCA.
HOGENOM; HOG000292977; -.
InParanoid; Q9M7X9; -.
OMA; MMRDIIN; -.
OrthoDB; EOG09360SS7; -.
PhylomeDB; Q9M7X9; -.
PRO; PR:Q9M7X9; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q9M7X9; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009295; C:nucleoid; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IDA:TAIR.
GO; GO:0047134; F:protein-disulfide reductase activity; IDA:TAIR.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
GO; GO:0008219; P:cell death; ISS:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IMP:TAIR.
GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
GO; GO:0034051; P:negative regulation of plant-type hypersensitive response; ISS:UniProtKB.
GO; GO:0009657; P:plastid organization; IMP:TAIR.
GO; GO:0031347; P:regulation of defense response; ISS:UniProtKB.
InterPro; IPR005746; Thioredoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10438; PTHR10438; 1.
Pfam; PF00085; Thioredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Chloroplast; Complete proteome;
Disulfide bond; Electron transport; Oxidoreductase; Plant defense;
Plastid; Redox-active center; Reference proteome; Transit peptide;
Transport.
TRANSIT 1 81 Chloroplast. {ECO:0000255}.
CHAIN 82 183 Thioredoxin-like protein CITRX,
chloroplastic.
/FTId=PRO_0000394545.
DOMAIN 82 183 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 106 106 Nucleophile.
{ECO:0000250|UniProtKB:P10599}.
ACT_SITE 109 109 Nucleophile.
{ECO:0000250|UniProtKB:P10599}.
SITE 100 100 Deprotonates C-terminal active site Cys.
{ECO:0000250|UniProtKB:P10599}.
SITE 107 107 Contributes to redox potential value.
{ECO:0000250|UniProtKB:P10599}.
SITE 108 108 Contributes to redox potential value.
{ECO:0000250|UniProtKB:P10599}.
DISULFID 106 109 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VAR_SEQ 147 170 RGLPTLFFISPDPSKDAIRTEGLI -> YCNLQLMFLNFMN
LLSAYQCKFLH (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_039287.
VAR_SEQ 171 183 Missing (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_039288.
MUTAGEN 106 106 C->S: Strongly reduces the interaction
with FLN1 or FLN2.
{ECO:0000269|PubMed:20511297}.
MUTAGEN 109 109 C->S: Does not affect the interaction
with FLN1 or FLN2.
{ECO:0000269|PubMed:20511297}.
CONFLICT 9 9 F -> L (in Ref. 5; AAM61520).
{ECO:0000305}.
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


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