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MGP003227

UniProt Annotations

Entry Information
Gene Namethioredoxin reductase 1
Protein EntryTRXR1_HUMAN
UniProt IDQ16881
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=7; Name=1; Synonyms=V, TXNRD1_v3; IsoId=Q16881-1; Sequence=Displayed; Note=Minor isoform.; Name=2; Synonyms=II, TXNRD1_v4; IsoId=Q16881-2; Sequence=VSP_031560, VSP_031565; Name=3; Synonyms=III, TXNRD1_v5; IsoId=Q16881-3; Sequence=VSP_031562, VSP_031563; Name=4; Synonyms=IV, TXNRD1_v2, TrxR1b; IsoId=Q16881-4; Sequence=VSP_031561, VSP_031564; Name=5; Synonyms=I, TXNRD1_v1, TrxR1a; IsoId=Q16881-5; Sequence=VSP_031558; Note=Major isoform. The N-terminus of the sequence is processed into a mature form that lacks residues Met-151 and Asn-152 at the N-terminus.; Name=6; Synonyms=VI; IsoId=Q16881-6; Sequence=VSP_031559; Name=7; IsoId=Q16881-7; Sequence=VSP_053819; Note=No experimental confirmation.;
Catalytic ActivityThioredoxin + NADP(+) = thioredoxin disulfide + NADPH.
CofactorName=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.;
DomainThe N-terminal glutaredoxin domain found in isoform 1 does not contain the C-P-Y-C redox-active motif normally found in glutaredoxins and has been found to be inactive in classical glutaredoxin assays. {ECO:0000269|PubMed:15379556}.
FunctionIsoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid. {ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8577704, ECO:0000269|PubMed:9774665}.
InductionIsoform 5 is induced by a combination of interferon- beta and retinoic acid (at protein level). Isoform 1 is induced by estradiol or testosterone in HeLa cells. {ECO:0000269|PubMed:9774665}.
InteractionQ03135:CAV1; NbExp=4; IntAct=EBI-716617, EBI-603614; P03372:ESR1; NbExp=4; IntAct=EBI-9080335, EBI-78473; Q92731:ESR2; NbExp=3; IntAct=EBI-9080335, EBI-78505;
MiscellaneousThe thioredoxin reductase active site is a redox- active disulfide bond. The selenocysteine residue is also essential for catalytic activity.
PtmISGylated. {ECO:0000305|PubMed:16815975}.
PtmThe N-terminus of isoform 5 is blocked.
Sequence CautionSequence=AAB35418.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=AAC69621.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=AAF15900.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=AAV38446.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=AAZ67916.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=BAA13674.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=BAH11490.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=BAH12374.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=BAH14140.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=CAA04503.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=CAA62629.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=CAG38744.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305}; Sequence=EAW97745.1; Type=Erroneous termination; Positions=648; Note=Translated as Sec.; Evidence={ECO:0000305};
SimilarityBelongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. {ECO:0000305}.
SimilarityContains 1 glutaredoxin domain. {ECO:0000255|PROSITE- ProRule:PRU00686}.
Subcellular LocationCytoplasm {ECO:0000250}.
Subcellular LocationIsoform 4: Cytoplasm. Nucleus.
Subcellular LocationIsoform 5: Cytoplasm.
SubunitHomodimer. Isoform 4 interacts with ESR1 and ESR2. Interacts with HERC5. {ECO:0000269|PubMed:15199063, ECO:0000269|PubMed:16815975}.
Tissue SpecificityIsoform 1 is expressed predominantly in Leydig cells (at protein level). Also expressed in ovary, spleen, heart, liver, kidney and pancreas and in a number of cancer cell lines. Isoform 4 is widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver. {ECO:0000269|PubMed:18042542, ECO:0000269|PubMed:8999974}.
Web ResourceName=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/txnrd1/";
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