ID   GLRX_RICCO              Reviewed;         102 AA.
AC   P55143;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Glutaredoxin;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sanguineus; TISSUE=Cotyledon;
RX   PubMed=9232906; DOI=10.1007/s004250050137;
RA   Szederkenyi J., Komor E., Schobert C.;
RT   "Cloning of the cDNA for glutaredoxin, an abundant sieve-tube exudate
RT   protein from Ricinus communis L. and characterisation of the glutathione-
RT   dependent thiol-reduction system in sieve tubes.";
RL   Planta 202:349-356(1997).
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC       presence of NADPH and glutathione reductase. Reduces low molecular
CC       weight disulfides and proteins.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z49699; CAA89699.1; -; mRNA.
DR   PIR; S54825; S54825.
DR   RefSeq; XP_002524673.1; XM_002524627.2.
DR   AlphaFoldDB; P55143; -.
DR   SMR; P55143; -.
DR   STRING; 3988.XP_002524673.1; -.
DR   GeneID; 8289824; -.
DR   KEGG; rcu:8289824; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   OrthoDB; 1535999at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02180; GRX_euk; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; Electron transport; Redox-active center;
KW   Transport.
FT   CHAIN           1..102
FT                   /note="Glutaredoxin"
FT                   /id="PRO_0000141608"
FT   DOMAIN          3..102
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        23..26
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   102 AA;  10878 MW;  9A82340EDBD92986 CRC64;
     MAMTKTKELV SSNAVVVFSK TYCPYCTSVK KLLDQLGAKY KVVELDTESD GSEIQTALAE
     WTGQRTVPNV FIGGKHIGGC DSTTAKHSQG QLVPLLTEAG AV