ID A6IFH4_RAT Unreviewed; 611 AA. AC A6IFH4; DT 28-JUN-2023, integrated into UniProtKB/TrEMBL. DT 28-JUN-2023, sequence version 1. DT 29-MAY-2024, entry version 6. DE RecName: Full=Thioredoxin reductase 1, cytoplasmic {ECO:0000256|ARBA:ARBA00044068}; DE EC=1.11.1.2 {ECO:0000256|ARBA:ARBA00044049}; DE EC=1.8.1.9 {ECO:0000256|ARBA:ARBA00012610}; DE AltName: Full=Peroxidase TXNRD1 {ECO:0000256|ARBA:ARBA00044275}; DE AltName: Full=Thioredoxin reductase TR1 {ECO:0000256|ARBA:ARBA00044212}; GN Name=Txnrd1 {ECO:0000313|EMBL:EDM17071.1, ECO:0000313|RGD:61959}; GN ORFNames=rCG_48959 {ECO:0000313|EMBL:EDM17071.1}; 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 {ECO:0000313|EMBL:EDM17071.1}; RN [1] {ECO:0000313|EMBL:EDM17071.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDM17071.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [2] {ECO:0000313|EMBL:EDM17071.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDM17071.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F., RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + H2O2 + NADPH = 2 H2O + NADP(+); Xref=Rhea:RHEA:15173, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.11.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00043653}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174; CC Evidence={ECO:0000256|ARBA:ARBA00043653}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00029303}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347; CC Evidence={ECO:0000256|ARBA:ARBA00029303}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532, CC ECO:0000256|RuleBase:RU003691}. 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; CH473960; EDM17071.1; -; Genomic_DNA. DR RGD; 61959; Txnrd1. DR Proteomes; UP000234681; Chromosome 7. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:TreeGrafter. DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter. DR GO; GO:0006749; P:glutathione metabolic process; IEA:TreeGrafter. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf. DR InterPro; IPR046952; GSHR/TRXR-like. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase. DR NCBIfam; TIGR01438; TGR; 1. DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1. DR PANTHER; PTHR42737:SF8; THIOREDOXIN REDUCTASE 1; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU003691}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003691}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, KW ECO:0000256|RuleBase:RU003691}; KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933}. FT DOMAIN 127..464 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 484..595 FT /note="Pyridine nucleotide-disulphide oxidoreductase FT dimerisation" FT /evidence="ECO:0000259|Pfam:PF02852" FT REGION 60..109 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 611 AA; 66826 MW; 4488A10F88EC44A3 CRC64; MPVDGCWLCF PTSRGRAFAQ TVWVTRTCPN CCWVPGFFPP VPQPPRVPCV LPRGSRGAVL PASHPSKGLP SSSQTPRPAD PRLCPPPSTP ESRQEKNTRP GLPNKKGLLR KLSTMNDSKD APKSYDFDLI IIGGGSGGLA AAKEAAKFDK KVMVLDFVTP TPLGTRWGLG GTCVNVGCIP KKLMHQAALL GQALKDSRNY GWKLEDTVKH DWEKMTESVQ NHIGSLNWGY RVALREKKVV YENAYGKFIG PHKIMATNNK GKEKVYSAER FLIATGERPR YLGIPGDKEY CISSDDLFSL PYCPGKTLVV GASYVALECA GFLAGIGLDV TVMVRSILLR GFDQDMANKI GEHMEEHGIK FIRQFVPTKI EQIEAGTPGR LKVTAKSTNS EETIEDEFNT VLLAVGRDSC TRTIGLETVG VKINEKTGKI PVTDEEQTNV PYIYAIGDIL EGKLELTPVA IQAGRLLAQR LYGGSTVKCD YDNVPTTVFT PLEYGCCGLS EEKAVEKFGE ENIEVYHSFF WPLEWTVPSR DNNKCYAKVV CNLKDNERVV GFHVLGPNAG EVTQGFAAAL KCGLTKQQLD STIGIHPVCA EIFTTLSVTK RSGGDILQSG C //