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Thioredoxin-like protein CITRX, chloroplastic (EC 1.8.-.-) (Cf-9-interacting thioredoxin) (LeCiTrx)

 CITRX_SOLLC             Reviewed;         175 AA.
Q9LKW0;
29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
31-JAN-2018, entry version 94.
RecName: Full=Thioredoxin-like protein CITRX, chloroplastic {ECO:0000303|PubMed:15131698};
EC=1.8.-.- {ECO:0000305};
AltName: Full=Cf-9-interacting thioredoxin {ECO:0000303|PubMed:15131698};
Short=LeCiTrx {ECO:0000303|PubMed:15131698};
Flags: Precursor;
Name=CITRX {ECO:0000303|PubMed:15131698};
OrderedLocusNames=Solyc01g096480
{ECO:0000312|EnsemblPlants:Solyc01g096480.2.1};
ORFNames=LOC543657 {ECO:0000312|EnsemblPlants:Solyc01g096480.2.1};
Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
Solaneae; Solanum; Lycopersicon.
NCBI_TaxID=4081;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Moneymaker; TISSUE=Seedling;
Min X., Kamiya Y.;
"Molecular cloning of a putative thioredoxin gene in tomato.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Heinz 1706;
PubMed=22660326; DOI=10.1038/nature11119;
Tomato Genome Consortium;
"The tomato genome sequence provides insights into fleshy fruit
evolution.";
Nature 485:635-641(2012).
[3]
GENE FAMILY, NOMENCLATURE, INTERACTION WITH CF-9, FUNCTION, AND
DISRUPTION PHENOTYPE.
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).
[4]
INTERACTION WITH CF-9.
PubMed=26315781; DOI=10.1111/mpp.12315;
Chakrabarti A., Velusamy T., Tee C.Y., Jones D.A.;
"A mutational analysis of the cytosolic domain of the tomato Cf-9
disease-resistance protein shows that membrane-proximal residues are
important for Avr9-dependent necrosis.";
Mol. Plant Pathol. 17:565-576(2016).
-!- FUNCTION: Probable thiol-disulfide oxidoreductase that may play a
role in proper chloroplast development (By similarity). Negatively
regulates Cf-9/Avr9-mediated cell death and defense responses.
{ECO:0000250|UniProtKB:Q9M7X9, ECO:0000269|PubMed:15131698}.
-!- SUBUNIT: Interacts with Cf-9 resistance protein.
{ECO:0000269|PubMed:15131698, ECO:0000269|PubMed:26315781}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
Cytoplasm {ECO:0000303|PubMed:15131698}.
-!- DISRUPTION PHENOTYPE: Yellowish coloration in the leaves.
Accelerated Cf-9/Avr9-triggered hypersensitive response.
{ECO:0000269|PubMed:15131698}.
-!- SIMILARITY: Belongs to the thioredoxin family. Plant CITRX-type
subfamily. {ECO:0000303|PubMed:15131698}.
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EMBL; AF261142; AAF75752.1; -; mRNA.
RefSeq; NP_001234469.1; NM_001247540.2.
UniGene; Les.194; -.
ProteinModelPortal; Q9LKW0; -.
SMR; Q9LKW0; -.
STRING; 4081.Solyc01g096480.2.1; -.
PaxDb; Q9LKW0; -.
EnsemblPlants; Solyc01g096480.2.1; Solyc01g096480.2.1; Solyc01g096480.2.
GeneID; 543657; -.
Gramene; Solyc01g096480.2.1; Solyc01g096480.2.1; Solyc01g096480.2.
KEGG; sly:543657; -.
eggNOG; KOG0907; Eukaryota.
eggNOG; COG0526; LUCA.
InParanoid; Q9LKW0; -.
OMA; MMRDIIN; -.
OrthoDB; EOG09360SS7; -.
Proteomes; UP000004994; Chromosome 1.
GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0009295; C:nucleoid; IEA:EnsemblPlants.
GO; GO:0009579; C:thylakoid; IEA:EnsemblPlants.
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; IBA:GO_Central.
GO; GO:0047134; F:protein-disulfide reductase activity; IBA:GO_Central.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
GO; GO:0008219; P:cell death; IMP:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; IMP:UniProtKB.
GO; GO:0009657; P:plastid organization; IEA:EnsemblPlants.
GO; GO:0031347; P:regulation of defense response; IMP: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;
Apoptosis; Chloroplast; Complete proteome; Cytoplasm; Disulfide bond;
Electron transport; Oxidoreductase; Plant defense; Plastid;
Redox-active center; Reference proteome; Transit peptide; Transport.
TRANSIT 1 64 Chloroplast. {ECO:0000255}.
CHAIN 65 175 Thioredoxin-like protein CITRX,
chloroplastic.
/FTId=PRO_0000430874.
DOMAIN 74 175 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 98 98 Nucleophile.
{ECO:0000250|UniProtKB:P10599}.
ACT_SITE 101 101 Nucleophile.
{ECO:0000250|UniProtKB:P10599}.
SITE 92 92 Deprotonates C-terminal active site Cys.
{ECO:0000250|UniProtKB:P10599}.
SITE 99 99 Contributes to redox potential value.
{ECO:0000250|UniProtKB:P10599}.
SITE 100 100 Contributes to redox potential value.
{ECO:0000250|UniProtKB:P10599}.
DISULFID 98 101 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
SEQUENCE 175 AA; 19805 MW; C6F3CBAE3F38FF70 CRC64;
MQAASLAFHP PALRTSPSYL SSKLPHHLNY SLFKHAPSTS TLSLTQVLSR NTICKPPAVG
KYVREDYLVK KLSAKEIQEL IKGERNVPLI IDFYATWCGP CILMAQELEM LAVEYENNAL
IVKVDTDDEY EFARDMQVRG LPTLYFISPD SSKDAIRTEG LIPIQMMRDI IDNDL


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