CITRX_SOLLC
ID CITRX_SOLLC Reviewed; 175 AA.
AC Q9LKW0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Thioredoxin-like protein CITRX, chloroplastic {ECO:0000305};
DE EC=1.8.-.- {ECO:0000305};
DE AltName: Full=Cf-9-interacting thioredoxin {ECO:0000303|PubMed:15131698};
DE Short=LeCiTrx {ECO:0000303|PubMed:15131698};
DE Flags: Precursor;
GN Name=CITRX {ECO:0000303|PubMed:15131698}; OrderedLocusNames=Solyc01g096480;
GN ORFNames=LOC543657;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Moneymaker; TISSUE=Seedling;
RA Min X., Kamiya Y.;
RT "Molecular cloning of a putative thioredoxin gene in tomato.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [3]
RP DISRUPTION PHENOTYPE, AND 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 [4]
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 [5]
RP INTERACTION WITH CF-9.
RX PubMed=26315781; DOI=10.1111/mpp.12315;
RA Chakrabarti A., Velusamy T., Tee C.Y., Jones D.A.;
RT "A mutational analysis of the cytosolic domain of the tomato Cf-9 disease-
RT resistance protein shows that membrane-proximal residues are important for
RT Avr9-dependent necrosis.";
RL Mol. Plant Pathol. 17:565-576(2016).
CC -!- FUNCTION: Probable thiol-disulfide oxidoreductase that may play a role
CC in proper chloroplast development. {ECO:0000250|UniProtKB:Q9M7X9}.
CC -!- SUBUNIT: Interacts with Cf-9 resistance protein.
CC {ECO:0000269|PubMed:26315781}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Yellowish coloration in the leaves.
CC {ECO:0000269|PubMed:15131698}.
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; AF261142; AAF75752.1; -; mRNA.
DR RefSeq; NP_001234469.1; NM_001247540.2.
DR AlphaFoldDB; Q9LKW0; -.
DR SMR; Q9LKW0; -.
DR STRING; 4081.Solyc01g096480.2.1; -.
DR PaxDb; Q9LKW0; -.
DR PRIDE; Q9LKW0; -.
DR EnsemblPlants; Solyc01g096475.1.1; Solyc01g096475.1.1; Solyc01g096475.1.
DR GeneID; 543657; -.
DR Gramene; Solyc01g096475.1.1; Solyc01g096475.1.1; Solyc01g096475.1.
DR KEGG; sly:543657; -.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_110012_1_0_1; -.
DR InParanoid; Q9LKW0; -.
DR OMA; PLQMMRD; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q9LKW0; -.
DR Proteomes; UP000004994; Chromosome 1.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0009657; P:plastid organization; IBA:GO_Central.
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 Chloroplast; Disulfide bond; Electron transport; Oxidoreductase; Plastid;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..175
FT /note="Thioredoxin-like protein CITRX, chloroplastic"
FT /id="PRO_0000430874"
FT DOMAIN 74..175
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 92
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 99
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT SITE 100
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT DISULFID 98..101
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ 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
