ID TRXR2_HUMAN Reviewed; 524 AA.
AC Q9NNW7; O95840; Q96IJ2; Q9H2Z5; Q9NZV3; Q9NZV4; Q9P2Y0; Q9P2Y1; Q9UQU8;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=Thioredoxin reductase 2, mitochondrial {ECO:0000305};
DE EC=1.8.1.9 {ECO:0000250|UniProtKB:Q9N2I8, ECO:0000250|UniProtKB:Q9Z0J5};
DE AltName: Full=Selenoprotein Z;
DE Short=SelZ;
DE AltName: Full=TR-beta;
DE AltName: Full=Thioredoxin reductase TR3;
DE Flags: Precursor;
GN Name=TXNRD2 {ECO:0000312|HGNC:HGNC:18155}; Synonyms=KIAA1652, TRXR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:AAD51324.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10455115; DOI=10.1074/jbc.274.35.24522;
RA Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Redox regulation of cell signaling by selenocysteine in mammalian
RT thioredoxin reductases.";
RL J. Biol. Chem. 274:24522-24530(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP SER-66.
RC TISSUE=Fetal heart, and Placenta;
RX PubMed=9923614; DOI=10.1016/s0014-5793(98)01638-x;
RA Gasdaska P.Y., Berggren M.M., Berry M.J., Powis G.;
RT "Cloning, sequencing and functional expression of a novel human thioredoxin
RT reductase.";
RL FEBS Lett. 442:105-111(1999).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Adrenal gland, and Testis;
RX PubMed=10215850; DOI=10.1046/j.1432-1327.1999.00286.x;
RA Miranda-Vizuete A., Damdimopoulos A.E., Pedrajas J.R., Gustafsson J.-A.,
RA Spyrou G.;
RT "Human mitochondrial thioredoxin reductase: cDNA cloning, expression and
RT genomic organization.";
RL Eur. J. Biochem. 261:405-412(1999).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), AND VARIANT THR-370.
RA Toji S., Yano M., Tamai K.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND VARIANT THR-370.
RC TISSUE=Cervix carcinoma;
RX PubMed=10608886; DOI=10.1074/jbc.274.53.38147;
RA Lescure A., Gautheret D., Carbon P., Krol A.;
RT "Novel selenoproteins identified in silico and in vivo by using a conserved
RT RNA structural motif.";
RL J. Biol. Chem. 274:38147-38154(1999).
RN [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND VARIANTS SER-66 AND THR-370.
RA Kim J.-R., Lee Y.H., Lee S.-R., Kim B.H., Rhee S.G., Kim J.H.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 40-524, AND VARIANT SER-66.
RC TISSUE=Skin;
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 [9]
RP ALTERNATIVE SPLICING.
RX PubMed=11060283; DOI=10.1074/jbc.m004750200;
RA Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Heterogeneity within animal thioredoxin reductases: evidence for
RT alternative first exon splicing.";
RL J. Biol. Chem. 276:3106-3114(2001).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN GCCD5, VARIANT GCCD5
RP 447-TYR--GLY-524 DEL, CHARACTERIZATION OF VARIANT GCCD5 447-TYR--GLY-524
RP DEL, AND VARIANTS SER-66; ARG-299 AND THR-370.
RX PubMed=24601690; DOI=10.1210/jc.2013-3844;
RA Prasad R., Chan L.F., Hughes C.R., Kaski J.P., Kowalczyk J.C., Savage M.O.,
RA Peters C.J., Nathwani N., Clark A.J., Storr H.L., Metherell L.A.;
RT "Thioredoxin Reductase 2 (TXNRD2) mutation associated with familial
RT glucocorticoid deficiency (FGD).";
RL J. Clin. Endocrinol. Metab. 99:E1556-E1563(2014).
CC -!- FUNCTION: Involved in the control of reactive oxygen species levels and
CC the regulation of mitochondrial redox homeostasis (PubMed:24601690).
CC Maintains thioredoxin in a reduced state. May play a role in redox-
CC regulated cell signaling. {ECO:0000250|UniProtKB:Q9Z0J5,
CC ECO:0000269|PubMed:24601690}.
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:0000250|UniProtKB:Q9N2I8,
CC ECO:0000250|UniProtKB:Q9Z0J5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000250|UniProtKB:Q9N2I8,
CC ECO:0000250|UniProtKB:Q9Z0J5};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|RuleBase:RU000402, ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P38816}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10215850}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Alpha {ECO:0000305};
CC IsoId=Q9NNW7-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta {ECO:0000305};
CC IsoId=Q9NNW7-2; Sequence=VSP_008304;
CC Name=3; Synonyms=SelZf2;
CC IsoId=Q9NNW7-3; Sequence=VSP_008305;
CC Name=4; Synonyms=SelZf1;
CC IsoId=Q9NNW7-4; Sequence=VSP_008306;
CC -!- TISSUE SPECIFICITY: Highly expressed in the prostate, ovary, liver,
CC testis, uterus, colon and small intestine. Intermediate levels in
CC brain, skeletal muscle, heart and spleen. Low levels in placenta,
CC pancreas, thymus and peripheral blood leukocytes. According to
CC PubMed:10608886, high levels in kidney, whereas according to
CC PubMed:9923614, levels are low. High expression is observed in the
CC adrenal cortex (PubMed:24601690). {ECO:0000269|PubMed:10215850,
CC ECO:0000269|PubMed:10608886, ECO:0000269|PubMed:24601690,
CC ECO:0000269|PubMed:9923614}.
CC -!- DISEASE: Glucocorticoid deficiency 5 (GCCD5) [MIM:617825]: A form of
CC glucocorticoid deficiency, a rare autosomal recessive disorder
CC characterized by resistance to ACTH action on the adrenal cortex,
CC adrenal insufficiency and an inability of the adrenal cortex to produce
CC cortisol. It usually presents in the neonatal period or in early
CC childhood with episodes of hypoglycemia and other symptoms related to
CC cortisol deficiency, including failure to thrive, recurrent illnesses
CC or infections, convulsions, and shock. In a small number of patients
CC hypoglycemia can be sufficiently severe and persistent that it leads to
CC serious long-term neurological damage or death. The diagnosis is
CC readily confirmed with a low plasma cortisol measurement in the
CC presence of an elevated ACTH level, and normal aldosterone and plasma
CC renin measurements. {ECO:0000269|PubMed:24601690}. Note=The disease may
CC be caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. The
CC selenocysteine residue is essential for enzymatic activity (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25167.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG47635.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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; AF171054; AAD51324.1; -; mRNA.
DR EMBL; AF106697; AAD19597.1; -; mRNA.
DR EMBL; AF044212; AAD25167.1; ALT_INIT; mRNA.
DR EMBL; AB019694; BAA77601.2; -; mRNA.
DR EMBL; AB019695; BAA77602.2; -; mRNA.
DR EMBL; AF166126; AAF21431.1; -; mRNA.
DR EMBL; AF166127; AAF21432.1; -; mRNA.
DR EMBL; AF201385; AAG47635.1; ALT_SEQ; mRNA.
DR EMBL; AC000078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC000080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC000090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007489; AAH07489.3; -; mRNA.
DR CCDS; CCDS42981.1; -. [Q9NNW7-1]
DR CCDS; CCDS86998.1; -. [Q9NNW7-3]
DR RefSeq; NP_006431.2; NM_006440.4. [Q9NNW7-1]
DR BioGRID; 115836; 58.
DR IntAct; Q9NNW7; 9.
DR MINT; Q9NNW7; -.
DR STRING; 9606.ENSP00000383365; -.
DR BindingDB; Q9NNW7; -.
DR ChEMBL; CHEMBL2403; -.
DR DrugBank; DB05428; Motexafin gadolinium.
DR GlyGen; Q9NNW7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NNW7; -.
DR PhosphoSitePlus; Q9NNW7; -.
DR SwissPalm; Q9NNW7; -.
DR BioMuta; TXNRD2; -.
DR DMDM; 182705230; -.
DR EPD; Q9NNW7; -.
DR jPOST; Q9NNW7; -.
DR MassIVE; Q9NNW7; -.
DR MaxQB; Q9NNW7; -.
DR PaxDb; 9606-ENSP00000383365; -.
DR PeptideAtlas; Q9NNW7; -.
DR ProteomicsDB; 81857; -. [Q9NNW7-1]
DR ProteomicsDB; 81858; -. [Q9NNW7-2]
DR ProteomicsDB; 81859; -. [Q9NNW7-3]
DR ProteomicsDB; 81860; -. [Q9NNW7-4]
DR Pumba; Q9NNW7; -.
DR Antibodypedia; 230; 295 antibodies from 34 providers.
DR DNASU; 10587; -.
DR Ensembl; ENST00000400521.7; ENSP00000383365.1; ENSG00000184470.21. [Q9NNW7-1]
DR Ensembl; ENST00000542719.6; ENSP00000485128.2; ENSG00000184470.21. [Q9NNW7-3]
DR GeneID; 10587; -.
DR KEGG; hsa:10587; -.
DR MANE-Select; ENST00000400521.7; ENSP00000383365.1; NM_006440.5; NP_006431.2.
DR AGR; HGNC:18155; -.
DR CTD; 10587; -.
DR DisGeNET; 10587; -.
DR GeneCards; TXNRD2; -.
DR HGNC; HGNC:18155; TXNRD2.
DR HPA; ENSG00000184470; Low tissue specificity.
DR MalaCards; TXNRD2; -.
DR MIM; 606448; gene.
DR MIM; 617825; phenotype.
DR neXtProt; NX_Q9NNW7; -.
DR OpenTargets; ENSG00000184470; -.
DR Orphanet; 361; Familial glucocorticoid deficiency.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR PharmGKB; PA38302; -.
DR VEuPathDB; HostDB:ENSG00000184470; -.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000158832; -.
DR InParanoid; Q9NNW7; -.
DR OMA; CFDYVKP; -.
DR OrthoDB; 5473641at2759; -.
DR PhylomeDB; Q9NNW7; -.
DR TreeFam; TF314782; -.
DR BRENDA; 1.8.1.9; 2681.
DR PathwayCommons; Q9NNW7; -.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR SignaLink; Q9NNW7; -.
DR BioGRID-ORCS; 10587; 29 hits in 1167 CRISPR screens.
DR ChiTaRS; TXNRD2; human.
DR GenomeRNAi; 10587; -.
DR Pharos; Q9NNW7; Tbio.
DR PRO; PR:Q9NNW7; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NNW7; Protein.
DR Bgee; ENSG00000184470; Expressed in right lobe of liver and 188 other cell types or tissues.
DR ExpressionAtlas; Q9NNW7; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; ISS:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:UniProtKB.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0000305; P:response to oxygen radical; TAS:UniProtKB.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
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:SF6; THIOREDOXIN REDUCTASE 2; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 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 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Disulfide bond; FAD; Flavoprotein;
KW Mitochondrion; NADP; Oxidoreductase; Redox-active center;
KW Reference proteome; Selenocysteine; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..524
FT /note="Thioredoxin reductase 2, mitochondrial"
FT /id="PRO_0000030288"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 41..70
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT NON_STD 523
FT /note="Selenocysteine"
FT MOD_RES 175
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLT4"
FT MOD_RES 329
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLT4"
FT DISULFID 86..91
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 522..523
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..247
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10608886"
FT /id="VSP_008306"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10608886"
FT /id="VSP_008305"
FT VAR_SEQ 1..30
FT /note="MAAMAVALRGLGGRFRWRTQAVAGGVRGAA -> MEDQ (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_008304"
FT VARIANT 14
FT /note="R -> L (in dbSNP:rs45593642)"
FT /id="VAR_051777"
FT VARIANT 66
FT /note="A -> S (in dbSNP:rs5748469)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:24601690, ECO:0000269|PubMed:9923614,
FT ECO:0000269|Ref.6"
FT /id="VAR_051778"
FT VARIANT 299
FT /note="S -> R (in dbSNP:rs5992495)"
FT /evidence="ECO:0000269|PubMed:24601690"
FT /id="VAR_051779"
FT VARIANT 370
FT /note="I -> T (in dbSNP:rs1139793)"
FT /evidence="ECO:0000269|PubMed:10608886,
FT ECO:0000269|PubMed:24601690, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.6"
FT /id="VAR_051780"
FT VARIANT 447..524
FT /note="Missing (in GCCD5; the mutant protein is
FT undetectable in patient cells)"
FT /evidence="ECO:0000269|PubMed:24601690"
FT /id="VAR_080529"
FT CONFLICT 33
FT /note="Missing (in Ref. 6; AAG47635)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="R -> K (in Ref. 6; AAG47635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 56507 MW; B575A185A2183DAC CRC64;
MAAMAVALRG LGGRFRWRTQ AVAGGVRGAA RGAAAGQRDY DLLVVGGGSG GLACAKEAAQ
LGRKVAVVDY VEPSPQGTRW GLGGTCVNVG CIPKKLMHQA ALLGGLIQDA PNYGWEVAQP
VPHDWRKMAE AVQNHVKSLN WGHRVQLQDR KVKYFNIKAS FVDEHTVCGV AKGGKEILLS
ADHIIIATGG RPRYPTHIEG ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI
GLDTTIMMRS IPLRGFDQQM SSMVIEHMAS HGTRFLRGCA PSRVRRLPDG QLQVTWEDST
TGKEDTGTFD TVLWAIGRVP DTRSLNLEKA GVDTSPDTQK ILVDSREATS VPHIYAIGDV
VEGRPELTPI AIMAGRLLVQ RLFGGSSDLM DYDNVPTTVF TPLEYGCVGL SEEEAVARHG
QEHVEVYHAH YKPLEFTVAG RDASQCYVKM VCLREPPQLV LGLHFLGPNA GEVTQGFALG
IKCGASYAQV MRTVGIHPTC SEEVVKLRIS KRSGLDPTVT GCUG
//
