ID   GLRX1_RABIT             Reviewed;         106 AA.
AC   P12864;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   18-JUN-2025, entry version 119.
DE   RecName: Full=Glutaredoxin-1;
DE   AltName: Full=Thioltransferase-1;
DE            Short=TTase-1;
GN   Name=GLRX; Synonyms=GRX;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Bone marrow;
RX   PubMed=2684977; DOI=10.1016/s0021-9258(19)47081-6;
RA   Hopper S., Johnson R.S., Vath J.E., Biemann K.;
RT   "Glutaredoxin from rabbit bone marrow. Purification, characterization, and
RT   amino acid sequence determined by tandem mass spectrometry.";
RL   J. Biol. Chem. 264:20438-20447(1989).
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   PIR; A32682; GDRB.
DR   AlphaFoldDB; P12864; -.
DR   SMR; P12864; -.
DR   FunCoup; P12864; 286.
DR   IntAct; P12864; 1.
DR   STRING; 9986.ENSOCUP00000013612; -.
DR   PaxDb; 9986-ENSOCUP00000013612; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   InParanoid; P12864; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR   GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IDA:BHF-UCL.
DR   CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR047185; GLRX1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02180; GRX_euk; 1.
DR   PANTHER; PTHR46185; GLUTAREDOXIN-1; 1.
DR   PANTHER; PTHR46185:SF1; GLUTAREDOXIN-1; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Redox-active center; Reference proteome; Transport.
FT   CHAIN           1..106
FT                   /note="Glutaredoxin-1"
FT                   /id="PRO_0000141603"
FT   DOMAIN          2..105
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P10575"
FT   MOD_RES         8
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QUH0"
FT   DISULFID        22..25
FT                   /note="Redox-active"
FT   DISULFID        78..82
SQ   SEQUENCE   106 AA;  11822 MW;  F6A1D7CC096A2105 CRC64;
     AQEFVNSKIQ PGKVVVFIKP TCPYCRKTQE ILSQLPFKQG LLEFVDITAT SDMSEIQDYL
     QQLTGARTVP RVFLGKDCIG GCSDLIAMQE KGELLARLKE MGALRQ
//