ID   GLRX1_CHICK             Reviewed;         101 AA.
AC   P79764;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Glutaredoxin-1;
DE   AltName: Full=Thioltransferase-1;
DE            Short=TTase-1;
GN   Name=GLRX; Synonyms=GRX;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9671415; DOI=10.1038/sj.onc.1201819;
RA   Goller M.E., Iacovoni J.S., Vogt P.K., Kruse U.;
RT   "Glutaredoxin is a direct target of oncogenic jun.";
RL   Oncogene 16:2945-2948(1998).
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.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; Y09235; CAA70437.1; -; mRNA.
DR   RefSeq; NP_990491.1; NM_205160.1.
DR   AlphaFoldDB; P79764; -.
DR   SMR; P79764; -.
DR   STRING; 9031.ENSGALP00000043300; -.
DR   PaxDb; P79764; -.
DR   GeneID; 396069; -.
DR   KEGG; gga:396069; -.
DR   CTD; 2745; -.
DR   VEuPathDB; HostDB:geneid_396069; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   InParanoid; P79764; -.
DR   OrthoDB; 1535999at2759; -.
DR   PhylomeDB; P79764; -.
DR   PRO; PR:P79764; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
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; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 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   Reference proteome; Transport.
FT   CHAIN           1..101
FT                   /note="Glutaredoxin-1"
FT                   /id="PRO_0000141605"
FT   DOMAIN          3..101
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   DISULFID        23..26
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   101 AA;  11397 MW;  50619DB1E54656F2 CRC64;
     MVDSFVQSKL RDNKVTLFVK GSCPYCKNAI VLLKEFNFLP GCLEVVDITG MDDIQDYFQK
     TTGQRTVPRV FIGTKCIGGF SDLQKMEQQL PMMLRQIGAL V