GLRX1_MOUSE
ID GLRX1_MOUSE Reviewed; 107 AA.
AC Q9QUH0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Glutaredoxin-1;
DE AltName: Full=Thioltransferase-1;
DE Short=TTase-1;
GN Name=Glrx; Synonyms=Glrx1, Grx, Grx1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
RC TISSUE=Spleen;
RX PubMed=10517541; DOI=10.1080/10715769900300931;
RA Nakamura T., Ohno T., Hirota K., Nishiyama A., Nakamura H., Wada H.,
RA Yodoi J.;
RT "Mouse glutaredoxin -- cDNA cloning, high level expression in E. coli and
RT its possible implication in redox regulation of the DNA binding activity in
RT transcription factor PEBP2.";
RL Free Radic. Res. 31:357-365(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10647820; DOI=10.3109/10425179909033944;
RA Miranda-Vizuete A., Pedrajas J.R., Damdimopoulos A.E., Spyrou G.;
RT "Cloning and sequencing of mouse glutaredoxin (grx) cDNA.";
RL DNA Seq. 10:179-182(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CFW; TISSUE=Lens;
RA Reddy P.G., Bhuyan D.K., Bhuyan K.C.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-9, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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; AB013137; BAA86926.1; -; mRNA.
DR EMBL; AF109314; AAF04780.1; -; mRNA.
DR EMBL; AF276917; AAF86464.1; -; mRNA.
DR EMBL; BC012642; AAH12642.1; -; mRNA.
DR CCDS; CCDS26651.1; -.
DR RefSeq; NP_444338.2; NM_053108.4.
DR RefSeq; XP_006517540.1; XM_006517477.1.
DR AlphaFoldDB; Q9QUH0; -.
DR SMR; Q9QUH0; -.
DR BioGRID; 220242; 1.
DR STRING; 10090.ENSMUSP00000022082; -.
DR iPTMnet; Q9QUH0; -.
DR PhosphoSitePlus; Q9QUH0; -.
DR SwissPalm; Q9QUH0; -.
DR EPD; Q9QUH0; -.
DR jPOST; Q9QUH0; -.
DR MaxQB; Q9QUH0; -.
DR PaxDb; Q9QUH0; -.
DR PRIDE; Q9QUH0; -.
DR ProteomicsDB; 267730; -.
DR Antibodypedia; 3264; 271 antibodies from 31 providers.
DR DNASU; 93692; -.
DR Ensembl; ENSMUST00000022082; ENSMUSP00000022082; ENSMUSG00000021591.
DR Ensembl; ENSMUST00000223120; ENSMUSP00000152802; ENSMUSG00000021591.
DR GeneID; 93692; -.
DR KEGG; mmu:93692; -.
DR UCSC; uc007rfx.2; mouse.
DR CTD; 2745; -.
DR MGI; MGI:2135625; Glrx.
DR VEuPathDB; HostDB:ENSMUSG00000021591; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00900000141068; -.
DR HOGENOM; CLU_026126_7_2_1; -.
DR InParanoid; Q9QUH0; -.
DR OMA; KPGHLEC; -.
DR OrthoDB; 1535999at2759; -.
DR PhylomeDB; Q9QUH0; -.
DR TreeFam; TF326994; -.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 93692; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Glrx; mouse.
DR PRO; PR:Q9QUH0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9QUH0; protein.
DR Bgee; ENSMUSG00000021591; Expressed in granulocyte and 262 other tissues.
DR ExpressionAtlas; Q9QUH0; baseline and differential.
DR Genevisible; Q9QUH0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; ISO:MGI.
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:MGI.
DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; TAS:MGI.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI.
DR GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
DR GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0045838; P:positive regulation of membrane potential; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISO:MGI.
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; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..107
FT /note="Glutaredoxin-1"
FT /id="PRO_0000141601"
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:0007744|PubMed:23806337"
FT MOD_RES 9
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT DISULFID 23..26
FT /note="Redox-active"
FT DISULFID 79..83
FT /evidence="ECO:0000250"
FT MUTAGEN 23
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10517541"
FT MUTAGEN 26
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10517541"
SQ SEQUENCE 107 AA; 11871 MW; DC0C7718DCD8805F CRC64;
MAQEFVNCKI QSGKVVVFIK PTCPYCRKTQ EILSQLPFKQ GLLEFVDITA TNNTSAIQDY
LQQLTGARTV PRVFIGKDCI GGCSDLISMQ QTGELMTRLK QIGALQL
