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Glutaredoxin-1 (Thioltransferase-1) (TTase-1)

 GLRX1_RAT               Reviewed;         107 AA.
Q9ESH6; Q99PB7;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 121.
RecName: Full=Glutaredoxin-1;
AltName: Full=Thioltransferase-1;
Short=TTase-1;
Name=Glrx; Synonyms=Glrx1, Grx;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Miranda-Vizuete A.;
"Cloning of rat glutaredoxin.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Liu C.Z., Xie Z.H., He Y.H., Wang A.M., Ma C.;
"Cloning and expression of glutaredoxin cDNA gene from PC12 cell line
in E.coli.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in
the presence of NADPH and glutathione reductase. Reduces low
molecular weight disulfides and proteins.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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EMBL; AF167981; AAF89637.3; -; mRNA.
EMBL; AF319950; AAK07419.1; -; mRNA.
EMBL; BC061555; AAH61555.1; -; mRNA.
RefSeq; NP_071614.1; NM_022278.1.
UniGene; Rn.1484; -.
ProteinModelPortal; Q9ESH6; -.
SMR; Q9ESH6; -.
STRING; 10116.ENSRNOP00000016372; -.
iPTMnet; Q9ESH6; -.
PhosphoSitePlus; Q9ESH6; -.
SwissPalm; Q9ESH6; -.
PaxDb; Q9ESH6; -.
PRIDE; Q9ESH6; -.
Ensembl; ENSRNOT00000016372; ENSRNOP00000016372; ENSRNOG00000012183.
GeneID; 64045; -.
KEGG; rno:64045; -.
UCSC; RGD:70951; rat.
CTD; 2745; -.
RGD; 70951; Glrx.
eggNOG; KOG1752; Eukaryota.
eggNOG; COG0695; LUCA.
GeneTree; ENSGT00900000141068; -.
HOGENOM; HOG000095204; -.
HOVERGEN; HBG000283; -.
InParanoid; Q9ESH6; -.
KO; K03676; -.
OMA; KPGHLEC; -.
OrthoDB; EOG091G0WLY; -.
PhylomeDB; Q9ESH6; -.
TreeFam; TF326994; -.
Reactome; R-RNO-499943; Interconversion of nucleotide di- and triphosphates.
PRO; PR:Q9ESH6; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000012183; -.
Genevisible; Q9ESH6; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IDA:RGD.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IMP:RGD.
GO; GO:2000587; P:negative regulation of platelet-derived growth factor receptor-beta signaling pathway; IMP:RGD.
GO; GO:0022602; P:ovulation cycle process; IEP:RGD.
GO; GO:0060355; P:positive regulation of cell adhesion molecule production; IMP:RGD.
GO; GO:0045921; P:positive regulation of exocytosis; IMP:RGD.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:RGD.
GO; GO:0002931; P:response to ischemia; IEP:RGD.
InterPro; IPR011767; GLR_AS.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR011899; Glutaredoxin_euk/vir.
InterPro; IPR014025; Glutaredoxin_subgr.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00462; Glutaredoxin; 1.
PRINTS; PR00160; GLUTAREDOXIN.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR02180; GRX_euk; 1.
PROSITE; PS00195; GLUTAREDOXIN_1; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
3: Inferred from homology;
Acetylation; Complete proteome; Cytoplasm; Disulfide bond;
Electron transport; Redox-active center; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P10575}.
CHAIN 2 107 Glutaredoxin-1.
/FTId=PRO_0000141604.
DOMAIN 3 106 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P10575}.
MOD_RES 9 9 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9QUH0}.
DISULFID 23 26 Redox-active. {ECO:0000250}.
DISULFID 79 83 {ECO:0000250}.
CONFLICT 9 9 K -> R (in Ref. 2; AAK07419).
{ECO:0000305}.
SEQUENCE 107 AA; 11879 MW; C46C67042138E9E8 CRC64;
MAQEFVNCKI QSGKVVVFIK PTCPYCRKTQ EILSQLPFKR GLLEFVDITA TNNTNAIQDY
LQQLTGARTV PRVFIGKDCI GGCSDLLSMQ QNGELTARLK QIGALQL


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