ID   GLRX1_BOVIN             Reviewed;         106 AA.
AC   P10575; Q32KQ3;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Glutaredoxin-1;
DE   AltName: Full=Thioltransferase;
DE            Short=TTase;
GN   Name=GLRX; Synonyms=GRX;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-106.
RC   TISSUE=Thymus;
RX   PubMed=6386471; DOI=10.1111/j.1432-1033.1984.tb08481.x;
RA   Klintrot I.-M., Hoeoeg J.-O., Joernvall H., Holmgren A., Luthman M.;
RT   "The primary structure of calf thymus glutaredoxin. Homology with the
RT   corresponding Escherichia coli protein but elongation at both ends and with
RT   an additional half-cystine/cysteine pair.";
RL   Eur. J. Biochem. 144:417-423(1984).
RN   [3]
RP   SEQUENCE REVISION TO 1-3 AND 69-72, AND ACETYLATION AT ALA-2.
RC   TISSUE=Thymus;
RX   PubMed=2930571; DOI=10.1016/0006-291x(89)92272-9;
RA   Papayannopoulos I.A., Gan Z.-R., Wells W.W., Biemann K.;
RT   "A revised sequence of calf thymus glutaredoxin.";
RL   Biochem. Biophys. Res. Commun. 159:1448-1454(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}.
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; BC109978; AAI09979.1; -; mRNA.
DR   PIR; A30164; GDBO.
DR   RefSeq; NP_001032693.1; NM_001037604.2.
DR   AlphaFoldDB; P10575; -.
DR   SMR; P10575; -.
DR   STRING; 9913.ENSBTAP00000051774; -.
DR   iPTMnet; P10575; -.
DR   PaxDb; P10575; -.
DR   PeptideAtlas; P10575; -.
DR   PRIDE; P10575; -.
DR   Ensembl; ENSBTAT00000054658; ENSBTAP00000051774; ENSBTAG00000038186.
DR   GeneID; 515416; -.
DR   KEGG; bta:515416; -.
DR   CTD; 2745; -.
DR   VEuPathDB; HostDB:ENSBTAG00000038186; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   GeneTree; ENSGT00900000141068; -.
DR   HOGENOM; CLU_026126_7_2_1; -.
DR   InParanoid; P10575; -.
DR   OMA; GALEWIN; -.
DR   OrthoDB; 1535999at2759; -.
DR   TreeFam; TF326994; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000038186; Expressed in rumen papilla and 107 other tissues.
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; 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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Redox-active center; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2930571"
FT   CHAIN           2..106
FT                   /note="Glutaredoxin-1"
FT                   /id="PRO_0000141599"
FT   DOMAIN          3..106
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:2930571"
FT   MOD_RES         9
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QUH0"
FT   DISULFID        23..26
FT                   /note="Redox-active"
FT   DISULFID        79..83
SQ   SEQUENCE   106 AA;  11783 MW;  99E1C2260E9D02BF CRC64;
     MAQAFVNSKI QPGKVVVFIK PTCPYCRKTQ ELLSQLPFKQ GLLEFVDITA AGNISEIQDY
     LQQLTGARTV PRVFIGQECI GGCTDLVNMH ERGELLTRLK QMGALQ