ID   CITRX_SOLTU             Reviewed;         175 AA.
AC   M1A3D5;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 48.
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=StCiTrx {ECO:0000303|PubMed:15131698};
DE   Flags: Precursor;
GN   Name=CITRX {ECO:0000303|PubMed:15131698};
GN   ORFNames=PGSC0003DMG400005407
GN   {ECO:0000312|EnsemblPlants:PGSC0003DMT400013827};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000312|EnsemblPlants:PGSC0003DMT400013827};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2]
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   [3]
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).
CC   -!- FUNCTION: Probable thiol-disulfide oxidoreductase that may play a role
CC       in proper chloroplast development. {ECO:0000250|UniProtKB:Q9M7X9}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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CC   -!- CAUTION: The article has been retracted, because it has become clear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CC       be withdrawn from the scientific literature.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   RefSeq; XP_006347665.1; XM_006347603.2.
DR   AlphaFoldDB; M1A3D5; -.
DR   SMR; M1A3D5; -.
DR   STRING; 4113.PGSC0003DMT400013827; -.
DR   EnsemblPlants; PGSC0003DMT400013827; PGSC0003DMT400013827; PGSC0003DMG400005407.
DR   GeneID; 102585257; -.
DR   Gramene; PGSC0003DMT400013827; PGSC0003DMT400013827; PGSC0003DMG400005407.
DR   KEGG; sot:102585257; -.
DR   eggNOG; KOG0907; Eukaryota.
DR   HOGENOM; CLU_110012_1_0_1; -.
DR   InParanoid; M1A3D5; -.
DR   OMA; EYESSAM; -.
DR   OrthoDB; 1482186at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Chloroplast; Disulfide bond; Electron transport; Oxidoreductase; Plastid;
KW   Redox-active center; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..73
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           74..175
FT                   /note="Thioredoxin-like protein CITRX, chloroplastic"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000430875"
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;  19879 MW;  E70339C0AF6957BD CRC64;
     MQAASLAFHP PALHTSPSYF SSKLPHHLNY SLFSHTPPTS TLSLTQTLSR KSICQPRAVG
     KYVREDYLVK KLSAKEIQEL IKGERNVPLI IDFYATWCGP CILMAQELEM LAVEYENNAL
     IVKVDTDDEY EFARDMQVRG LPTLYFISPD SSKDAIRTEG LIPIQMMRDI INNDL