ID   TRXR1_MOUSE             Reviewed;         613 AA.
AC   Q9JMH6; Q3UEB7; Q3UK84; Q8CI31; Q99P49; Q9CSV5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Thioredoxin reductase 1, cytoplasmic {ECO:0000305};
DE            Short=TR;
DE            EC=1.8.1.9 {ECO:0000250|UniProtKB:Q16881};
DE   AltName: Full=Peroxidase TXNRD1 {ECO:0000250|UniProtKB:Q16881};
DE            EC=1.11.1.2 {ECO:0000250|UniProtKB:Q16881};
DE   AltName: Full=Thioredoxin reductase TR1;
GN   Name=Txnrd1 {ECO:0000312|MGI:MGI:1354175}; Synonyms=Trxr1;
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] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RC   TISSUE=Thymus;
RX   PubMed=10721726; DOI=10.1016/s0378-1119(99)00498-9;
RA   Kawai H., Ota T., Suzuki F., Tatsuka M.;
RT   "Molecular cloning of mouse thioredoxin reductases.";
RL   Gene 242:321-330(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX   PubMed=11737861; DOI=10.1186/1471-2164-2-10;
RA   Osborne S.A., Tonissen K.F.;
RT   "Genomic organisation and alternative splicing of mouse and human
RT   thioredoxin reductase 1 genes.";
RL   BMC Genomics 2:10-10(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [8]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
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: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-
CC       containing form. Homodimeric flavoprotein involved in the regulation of
CC       cellular redox reactions, growth and differentiation. Contains a
CC       selenocysteine residue at the C-terminal active site that is essential
CC       for catalysis. Also has reductase activity on hydrogen peroxide (H2O2).
CC       {ECO:0000250|UniProtKB:Q16881}.
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:Q16881};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC         Evidence={ECO:0000250|UniProtKB:Q16881};
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:0000250|UniProtKB:Q16881};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174;
CC         Evidence={ECO:0000250|UniProtKB:Q16881};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q16881};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q16881};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10721726}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JMH6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JMH6-2; Sequence=VSP_031566;
CC   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:Q16881}.
CC   -!- MISCELLANEOUS: The thioredoxin reductase active site is a redox-active
CC       disulfide bond. The selenocysteine residue is also essential for
CC       catalytic activity. {ECO:0000250|UniProtKB:O89049}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37643.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE26918.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE40292.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB027565; BAA86985.2; -; mRNA.
DR   EMBL; AF333036; AAK01140.1; -; mRNA.
DR   EMBL; AK011902; BAB27905.1; -; mRNA.
DR   EMBL; AK146125; BAE26918.1; ALT_SEQ; mRNA.
DR   EMBL; AK149625; BAE28994.1; -; mRNA.
DR   EMBL; AK168356; BAE40292.1; ALT_SEQ; mRNA.
DR   EMBL; BC037643; AAH37643.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS24072.1; -. [Q9JMH6-2]
DR   CCDS; CCDS88064.1; -. [Q9JMH6-1]
DR   RefSeq; NP_001035978.1; NM_001042513.1. [Q9JMH6-2]
DR   RefSeq; NP_001035979.1; NM_001042514.1. [Q9JMH6-2]
DR   RefSeq; NP_001035988.1; NM_001042523.1. [Q9JMH6-1]
DR   RefSeq; NP_056577.2; NM_015762.2. [Q9JMH6-2]
DR   BioGRID; 206041; 10.
DR   IntAct; Q9JMH6; 1.
DR   MINT; Q9JMH6; -.
DR   STRING; 10090.ENSMUSP00000152046; -.
DR   GlyGen; Q9JMH6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9JMH6; -.
DR   PhosphoSitePlus; Q9JMH6; -.
DR   SwissPalm; Q9JMH6; -.
DR   REPRODUCTION-2DPAGE; Q9JMH6; -.
DR   EPD; Q9JMH6; -.
DR   jPOST; Q9JMH6; -.
DR   MaxQB; Q9JMH6; -.
DR   PaxDb; 10090-ENSMUSP00000020484; -.
DR   PeptideAtlas; Q9JMH6; -.
DR   ProteomicsDB; 297528; -. [Q9JMH6-1]
DR   ProteomicsDB; 297529; -. [Q9JMH6-2]
DR   Pumba; Q9JMH6; -.
DR   Antibodypedia; 3897; 522 antibodies from 43 providers.
DR   DNASU; 50493; -.
DR   Ensembl; ENSMUST00000020484.9; ENSMUSP00000020484.8; ENSMUSG00000020250.12. [Q9JMH6-2]
DR   Ensembl; ENSMUST00000219368.3; ENSMUSP00000151629.3; ENSMUSG00000020250.12. [Q9JMH6-1]
DR   Ensembl; ENSMUST00000219442.3; ENSMUSP00000152046.3; ENSMUSG00000020250.12. [Q9JMH6-2]
DR   Ensembl; ENSMUST00000219962.3; ENSMUSP00000151825.3; ENSMUSG00000020250.12. [Q9JMH6-2]
DR   GeneID; 50493; -.
DR   KEGG; mmu:50493; -.
DR   UCSC; uc007gjy.1; mouse. [Q9JMH6-1]
DR   AGR; MGI:1354175; -.
DR   CTD; 7296; -.
DR   MGI; MGI:1354175; Txnrd1.
DR   VEuPathDB; HostDB:ENSMUSG00000020250; -.
DR   eggNOG; KOG4716; Eukaryota.
DR   GeneTree; ENSGT00940000160180; -.
DR   HOGENOM; CLU_016755_2_4_1; -.
DR   InParanoid; Q9JMH6; -.
DR   OMA; GTCINWG; -.
DR   OrthoDB; 5473641at2759; -.
DR   PhylomeDB; Q9JMH6; -.
DR   TreeFam; TF314782; -.
DR   BRENDA; 1.8.1.9; 3474.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR   Reactome; R-MMU-5263617; Metabolism of ingested MeSeO2H into MeSeH.
DR   Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR   SABIO-RK; Q9JMH6; -.
DR   BioGRID-ORCS; 50493; 24 hits in 78 CRISPR screens.
DR   ChiTaRS; Txnrd1; mouse.
DR   PRO; PR:Q9JMH6; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9JMH6; Protein.
DR   Bgee; ENSMUSG00000020250; Expressed in somite and 288 other cell types or tissues.
DR   ExpressionAtlas; Q9JMH6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0045340; F:mercury ion binding; ISO:MGI.
DR   GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; ISO:MGI.
DR   GO; GO:0050137; F:NADPH peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0033797; F:selenate reductase activity; ISO:MGI.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IDA:MGI.
DR   GO; GO:0042537; P:benzene-containing compound metabolic process; ISO:MGI.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0007369; P:gastrulation; IMP:MGI.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0070995; P:NADPH oxidation; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR   GO; GO:0016259; P:selenocysteine metabolic process; ISO:MGI.
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.
DR   Genevisible; Q9JMH6; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW   Oxidoreductase; Phosphoprotein; Redox-active center; Reference proteome;
KW   Selenocysteine; Ubl conjugation.
FT   CHAIN           1..613
FT                   /note="Thioredoxin reductase 1, cytoplasmic"
FT                   /id="PRO_0000067982"
FT   REGION          57..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        586
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..137
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         156..157
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         172..173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         177..181
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         245..246
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         275
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         280
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         312..318
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         314
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         335..336
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         340..342
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         340
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O89049"
FT   BINDING         406..407
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         429
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         448
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         455..457
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         455
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   BINDING         586
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q16881"
FT   NON_STD         612
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         182
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         245
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   DISULFID        173..178
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        611..612
FT                   /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..114
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10721726,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031566"
FT   CONFLICT        238
FT                   /note="K -> E (in Ref. 3; BAE28994)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        372
FT                   /note="Q -> R (in Ref. 3; BAE26918)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        607
FT                   /note="L -> V (in Ref. 3; BAE26918)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   613 AA;  67084 MW;  C9FD2E2E8C55118C CRC64;
     MPVDDCWLYF PASRGRTFVQ TVWVAPTCPN CCWFPGFLPP VPRPPHVPRV LLRGPRGAVL
     PASRPSKTLP SSSQTPCPTD PCICPPPSTP DSRQEKNTQS ELPNKKGQLQ KLPTMNGSKD
     PPGSYDFDLI IIGGGSGGLA AAKEAAKFDK KVLVLDFVTP TPLGTRWGLG GTCVNVGCIP
     KKLMHQAALL GQALKDSRNY GWKVEDTVKH DWEKMTESVQ SHIGSLNWGY RVALREKKVV
     YENAYGRFIG PHRIVATNNK GKEKIYSAER FLIATGERPR YLGIPGDKEY CISSDDLFSL
     PYCPGKTLVV GASYVALECA GFLAGIGLDV TVMVRSILLR GFDQDMANKI GEHMEEHGIK
     FIRQFVPTKI EQIEAGTPGR LRVTAQSTNS EETIEGEFNT VLLAVGRDSC TRTIGLETVG
     VKINEKTGKI PVTDEEQTNV PYIYAIGDIL EGKLELTPVA IQAGRLLAQR LYGGSNVKCD
     YDNVPTTVFT PLEYGCCGLS EEKAVEKFGE ENIEVYHSFF WPLEWTVPSR DNNKCYAKII
     CNLKDDERVV GFHVLGPNAG EVTQGFAAAL KCGLTKQQLD STIGIHPVCA EIFTTLSVTK
     RSGGDILQSG CUG
//