ID   CITX1_NICBE             Reviewed;         181 AA.
AC   Q6JE38;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Thioredoxin-like protein CITRX1, chloroplastic {ECO:0000305};
DE            EC=1.8.-.- {ECO:0000305};
DE   AltName: Full=Cf-9-interacting thioredoxin 1 {ECO:0000303|PubMed:15131698};
DE            Short=NbCiTrx1 {ECO:0000303|PubMed:15131698};
DE   Flags: Precursor;
GN   Name=CITRX1 {ECO:0000303|PubMed:15131698};
OS   Nicotiana benthamiana.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], 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   [2]
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CC   -!- CAUTION: The article has been retracted, because it has become clear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CC       be withdrawn from the scientific literature.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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY500242; AAS80319.1; -; mRNA.
DR   AlphaFoldDB; Q6JE38; -.
DR   SMR; Q6JE38; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Chloroplast; Disulfide bond; Electron transport; Oxidoreductase; Plastid;
KW   Redox-active center; Transit peptide; Transport.
FT   TRANSIT         1..70
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           71..181
FT                   /note="Thioredoxin-like protein CITRX1, chloroplastic"
FT                   /id="PRO_0000430871"
FT   DOMAIN          71..181
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        104
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            98
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            105
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   SITE            106
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250|UniProtKB:P10599"
FT   DISULFID        104..107
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   181 AA;  20435 MW;  EA62DB57B53C39AC CRC64;
     MQAATLSFHP SAPPPQTSAC HFSSKQPNQL KYSLFSYTCP ILKRSLLSTQ TLSRKSICKP
     PAVATGKYVR EDYLVKKVSA KDIQELIKGE RNVPLIIDFY ATWCGPCILM AQELEMLAVE
     YESNALIVKV DADDEYEFAR DMQVRGLPTL YFISPDPNKD AIRTEGLIPI QMMRDIINND
     L