GLRX1_RAT
ID GLRX1_RAT Reviewed; 107 AA.
AC Q9ESH6; Q99PB7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glutaredoxin-1;
DE AltName: Full=Thioltransferase-1;
DE Short=TTase-1;
GN Name=Glrx; Synonyms=Glrx1, Grx;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miranda-Vizuete A.;
RT "Cloning of rat glutaredoxin.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu C.Z., Xie Z.H., He Y.H., Wang A.M., Ma C.;
RT "Cloning and expression of glutaredoxin cDNA gene from PC12 cell line in
RT E.coli.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; AF167981; AAF89637.3; -; mRNA.
DR EMBL; AF319950; AAK07419.1; -; mRNA.
DR EMBL; BC061555; AAH61555.1; -; mRNA.
DR RefSeq; NP_071614.1; NM_022278.1.
DR AlphaFoldDB; Q9ESH6; -.
DR SMR; Q9ESH6; -.
DR STRING; 10116.ENSRNOP00000016372; -.
DR iPTMnet; Q9ESH6; -.
DR PhosphoSitePlus; Q9ESH6; -.
DR SwissPalm; Q9ESH6; -.
DR PaxDb; Q9ESH6; -.
DR PRIDE; Q9ESH6; -.
DR Ensembl; ENSRNOT00000016372; ENSRNOP00000016372; ENSRNOG00000012183.
DR GeneID; 64045; -.
DR KEGG; rno:64045; -.
DR UCSC; RGD:70951; rat.
DR CTD; 2745; -.
DR RGD; 70951; Glrx.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00900000141068; -.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; Q9ESH6; -.
DR OMA; KPGHLEC; -.
DR OrthoDB; 1535999at2759; -.
DR PhylomeDB; Q9ESH6; -.
DR TreeFam; TF326994; -.
DR Reactome; R-RNO-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:Q9ESH6; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012183; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q9ESH6; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IDA:RGD.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:InterPro.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IMP:RGD.
DR GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; IMP:RGD.
DR GO; GO:0022602; P:ovulation cycle process; IEP:RGD.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; IMP:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:0045838; P:positive regulation of membrane potential; ISO:RGD.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:RGD.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
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 Acetylation; Cytoplasm; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P10575"
FT CHAIN 2..107
FT /note="Glutaredoxin-1"
FT /id="PRO_0000141604"
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:0000250|UniProtKB:P10575"
FT MOD_RES 9
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QUH0"
FT DISULFID 23..26
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 79..83
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="K -> R (in Ref. 2; AAK07419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 107 AA; 11879 MW; C46C67042138E9E8 CRC64;
MAQEFVNCKI QSGKVVVFIK PTCPYCRKTQ EILSQLPFKR GLLEFVDITA TNNTNAIQDY
LQQLTGARTV PRVFIGKDCI GGCSDLLSMQ QNGELTARLK QIGALQL
